Biosafety and Biosecurity Challenges Facing Veterinary Diagnostic Laboratories in Lower-Middle Income Countries in Southeast Asia: A Case Study of Thailand

Biosafety and Biosecurity Challenges Facing Veterinary Diagnostic Laboratories in Lower-Middle Income Countries in Southeast Asia: A Case Study of Thailand

Introduction: Global issues over rising and transboundary infectious zoonotic ailments have elevated illness diagnostic calls for, particularly in the veterinary sector. In growing or newly developed nations the place the sector usually works beneath restricted capability, biosafety and biosecurity are unlikely to be high-priority points. A latest improvement program supported by the Biological Threat Reduction Program of the Defense Threat Reduction Agency funded by the US authorities aimed to extend biosafety and biosecurity measures of authorities veterinary diagnostic and analysis laboratories in Thailand.

Objective: The function of this text is to determine biosafety and biosecurity challenges, alternatives, and suggestions.

Methods: Eleven authorities laboratory facilities have been assessed towards the Biosafety in Microbiological and Biomedical Laboratories (BMBLbiosafety degree 2 (BSL-2) necessities guidelines. The BMBL evaluation outcomes have been then mixed with the outcomes of dialogue periods, and the outcomes of pre- and post-test questionnaires carried out throughout biosafety evaluation workshops and self-evaluation experiences utilizing the Food and Agriculture Organization Biosafety Laboratory Mapping Tool of every laboratory heart have been reviewed and summarized.

Results: Despite established nationwide insurance policies on laboratory biosafety and biosecurity, main challenges included (1) harmonization and enforcement of these insurance policies, particularly on the regional degree, and (2) engagement of personnel in implementations of biosafety and biosecurity measures.

Conclusion: Consistent biosafety coverage and allotted assets along with common coaching are required to develop sustainable biosafety and biosecurity on the nationwide degree. Collaboration between regional nations, worldwide organizations, and donors is crucial for bettering biosafety and biosecurity on a world scale by means of setting regional priorities, enacting regulatory requirements, and offering technical and monetary help.

 Biosafety and Biosecurity Challenges Facing Veterinary Diagnostic Laboratories in Lower-Middle Income Countries in Southeast Asia: A Case Study of Thailand
Biosafety and Biosecurity Challenges Facing Veterinary Diagnostic Laboratories in Lower-Middle Income Countries in Southeast Asia: A Case Study of Thailand

Lab-Scale Production of Recombinant Adeno-Associated Viruses (AAV) for Expression of Optogenetic Elements

Optogenetics, that’s, the use of photoswitchable/-activatable moieties to exactly management or monitor the exercise of cells and genes at unprecedented spatiotemporal decision, holds great promise for a wide selection of purposes in elementary and scientific analysis. To absolutely notice and harness this potential, the supply of gene switch autos (“vectors”) which can be simply produced and that permit to ship the important parts to desired goal cells in an environment friendly method is vital.

For in vivo purposes, it’s, furthermore, necessary that these vectors exhibit a excessive diploma of cell specificity in order to scale back the danger of adversarial uncomfortable side effects in off-targets and to reduce manufacturing prices. Here, we describe a set of fundamental protocols for the cloning, manufacturing, purification, and high quality management of a selected vector that may fulfill all these necessities, that’s, recombinant adeno-associated viruses (AAV).

The latter are very engaging owing to their apathogenicity, their compatibility with the bottom biosafety degree 1 circumstances, their incidence in a number of pure variants with distinct properties, and their distinctive amenability to engineering of the viral capsid and genome.

Human FLT-1/VEGFR-1 Control/blocking peptide #1

FLT11-P 100 ug
EUR 196.8

VEGFR binding peptide KH / QKRKRKKSRKKH

007-58 100 μg
EUR 158.76

VEGFR binding peptide IVLS / RKRKRKKSRYIVLS

007-59 100 μg
EUR 171.72

Mouse FLT-4/VEGFR-3 Control/blocking peptide #1

FLT41-P 100 ug
EUR 196.8

Human FLT-4/VEGFR-3 control/blocking peptide #2

FLT42-P 100 ug
EUR 196.8

Rabbit anti VEGFR-1/Flt-1 (human)

102-PA20S 100ug
EUR 240

Mouse anti VEGFR-1/Flt-1 (#EWC) (human)

101-M24 100ug
EUR 297.6

Mouse anti VEGFR-1/Flt-1 (#EIC) (human)

101-M26 100ug
EUR 297.6

Mouse anti VEGFR-1/Flt-1 (#EWF) (human)

101-M28 100ug
EUR 297.6

Mouse anti VEGFR-1/Flt-1 (#EWI) (human)

101-M30 100ug
EUR 297.6

anti- VEGFR-1/FLT-1 antibody

FNab09393 100µg
EUR 606.3
Description: Antibody raised against VEGFR-1/FLT-1

Anti-Human VEGFR-1/Flt-1 Antibody

101-MBi24 50 µg
EUR 246.75
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA.

Anti-Human VEGFR-1/Flt-1 Antibody

101-MBi30 50 µg
EUR 189
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA.

Anti-Human VEGFR-1/Flt-1 Antibody

102-PA20 200 µg
EUR 173.25
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA.

Anti-Human VEGFR-1/Flt-1 Antibody

102-PABi20 50 µg
EUR 157.5
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA.

Mouse anti VEGFR-3/Flt-4 (#1) (human)

101-M36 100ug
EUR 297.6

Mouse anti VEGFR-1/Flt-1-Biotin (#EWF) (human)

101-MBi28 50ug
EUR 297.6

VEGFR-1 / FLT-1 Antibody

abx239393-100ug 100 ug
EUR 577.2

VEGFR-1/FLT-1 antibody

E39-09393 100ug/100ul
EUR 225
Description: Available in various conjugation types.

VEGFR-1/FLT-1 antibody

CAF50629-100ug 100ug
EUR 312

Anti-Mouse VEGFR-1/Flt-1 Antibody

103-M31 100 µg
EUR 399
Description: Vascular Endothelial Growth Factor (VEGF or VEGF-A) family members are major mediators of vasculogenesis and angiogenesis. Specifically, biological activities attributed to VEGFs include: mitogenic activity on endothelial cells, increased permeability of endothelial cells to proteins, stimulation of monocyte migration across endothelial cells and angiogenic activity. Three VEGF family receptors have been described: Flt-1 (fms-like tyrosine kinase) also known as VEGF R1, KDR (kinase-insert domain-containing receptor) also known as Flk-1 and VEGF R2, and Flt-4 also known as VEGF R3. The three receptors contain seven extracellular immunoglobulin-like domains and share substantial sequence homology. In addition, neuropilin-1, a neuronal receptor, also acts as a co-receptor for VEGF when expressed on vascular endothelial cells, endothelial cell progenitors and monocytes. VEGF R1 is expressed primarily on endothelial cells but is also found on human peripheral blood monocytes. Through its endothelial mitogenic and hyperpermeability activities, VEGF influences a variety of immune functions related to wound healing and blood protein traffic across endothelial barriers.

Mouse anti VEGFR-3/Flt-4-Biotin (#1) (human)

101-MBi36 50ug
EUR 297.6

Recombinant Human FLT-1/VEGFR-1 Protein

RP01137 50μg
EUR 308.75

Rabbit anti VEGFR-3/Flt-4 (human)

102-PA22AG 50ug
EUR 240

Rabbit anti VEGFR-3/Flt-4 (human)

102-PA22S 100ug
EUR 240

Anti-Mouse VEGFR-2/Flk-1 (Peptide), soluble Antibody

103-PA19S 100 µg
EUR 126
Description: The antibody recognizes solely the endogenous soluble form of mouse vascular endothelial growth factor receptor 2, alos known as CD309, VEGFR2, KDR, protein tyrosine kinase receptor flk-1, and fetal liver kinase-1. The endogenous soluble mouse esFlk-1 generated by alternative splicing consists of the first 6 Ig-like loops followed by the unique C-terminal end: GMEASLGDRIAMP. Flk-1 is a member of the tyrosine protein kinase family, sub-family CSF-1/PDGF, that contains a single pass transmembrane receptor with a protein kinase domain and seven immunoglobulin-like domains in the extracellular region. Flk-1 is expressed at high levels in adult heart, lung, kidney, brain, and skeletal muscle; other tissues express at lower levels. Flk-1 is a receptor for VEGF-A or fully processed VEGF-C; ligand binding plays a key role in vascular development and vascular permeability.

Rabbit Anti-Mouse VEGFR-2 Flk-1 (Peptide), soluble

103-PA19 100ug
EUR 240

Anti-Inflammatory Peptide 1

004-01 200 μg
EUR 27

VEGFR-KDR/Flk-1 Antagonist Peptide

H-5896.0001 1.0mg
EUR 691.2
Description: Sum Formula: C77H99N23O18S; CAS# [492444-99-2] net

VEGFR-KDR/Flk-1 Antagonist Peptide

H-5896.0005 5.0mg
EUR 2648.4
Description: Sum Formula: C77H99N23O18S; CAS# [492444-99-2] net

Active Recombinant Human FLT-1/VEGFR-1 Protein

RP01188 5 μg
EUR 32.5

Anti-Hu/Mo VEGFR-1/Flt-1, Antagonistic Antibody

mV1004.1m-h-m 100 µg
EUR 645.75
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The antibody will bind near the ligand binding site of the receptor and has antagonistic activity by blocking the binding of natural ligands.

Biotinylated Recombinant Human FLT-1/VEGFR-1 Protein

RP02100 500μg
EUR 2843.75

Rabbit Anti-human FLT-1/VEGFR-1 IgG #1, aff pure

FLT11-A 100 ul
EUR 578.4

Human VEGFR-1/Flt-1 (D5), soluble Recombinant Protein

S01-011 5 µg
EUR 73.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-5 (sVEGFR-1(D5)) is a 70 kDa protein. The baculovirus generated, recombinant human sVEGFR-1 is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 70 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D5), soluble Recombinant Protein

S01-012 20 µg
EUR 157.5
Description: Recombinat human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-5 (sVEGFR-1(D5)) is a 70 kDa protein containing amino acid residues. The baculovirus generated, recombinant human sVEGFR-1 is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 70 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D4), soluble Recombinant Protein

S01-013 5 µg
EUR 103.95
Description: Recombinant Human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-4 (sVEGFR-1(D4)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 4 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 55 kDa containing 457 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D4), soluble Recombinant Protein

S01-014 20 µg
EUR 199.5
Description: Recombinant Human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-4 (sVEGFR-1(D4)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 4 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 55 kDa containing 457 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D3), soluble Recombinant Protein

S01-015 5 µg
EUR 103.95
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (D3), soluble Recombinant Protein

S01-016 20 µg
EUR 199.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Rabbit Anti-Human VEGFR-2/KDR (Peptide), soluble

102-PA19 100ug
EUR 240

Defensin I / Human Neutrophil Peptide-1 (HNP-1) (Human)

072-17 100 μg
EUR 370.44

Anti-Human VEGFR-2/KDR (Peptide), soluble Antibody

102-PA19S 100 µg
EUR 126
Description: VEGF R1 (Flt-1), VEGF R2 (KDR/Flk-1), and VEGF R3 (Flt-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domain and kinase insert domains in their intracellular region. They are best known for regulating VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. They are also mediators of neurotrophic activity and regulators of hematopoietic development. Human VEGF R2 is thought to be the primary inducer of VEGF-mediated blood vessel growth, while VEGF R3 plays a significant role in VEGF-C and VEGF-D-mediated lymphangiogenesis.

RFamide-Related Peptide 1 (RFRP-1) (Human)

048-42 500 μg
EUR 177.12

Human VEGFR-1/Flt-1 (native), soluble Recombinant Protein

S01-009 5 µg
EUR 73.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1) is the naturally occurring form and was cloned from total RNA of human umbilical vein endothelial cells. The recombinant mature sVEGFR-1 is a glycosylated monomeric protein with a mass of approximately 96 kDa. The soluble receptor precursor protein consists of the first 6 extracellular domains (Met1-His688) containing the unique 31 amino acids residues at the C-terminus. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly, a naturally occurring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

Human VEGFR-1/Flt-1 (native), soluble Recombinant Protein

S01-010 20 µg
EUR 157.5
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1) is the naturally occurring form and was cloned from total RNA of human umbilical vein endothelial cells. The recombinant mature sVEGFR-1 is a glycosylated monomeric protein with a mass of approximately 96 kDa. The soluble receptor protein consists of the first 6 extracellular domains (Met1-His688) containing the unique 31 amino acids residues at the C-terminus. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly, a naturally occurring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis binding VEGF with the same affinity as the full-length receptor.

Anti-Human VEGFR-3/FLT-4 Antibody

101-M37 100 µg
EUR 199.5
Description: VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk 1) and VEGFR-3 (FLT-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domains and kinase insert domains in their intracellular regions. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. These receptors play essential roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The VEGFR-3 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 24 aa residue signal peptide. Mature VEGFR-3 is composed of a 751 aa residue extracellular domain, a 22 aa residue transmembrane domain and a 482 aa residue cytoplasmic domain. Both VEGF-C and VEGF-D have been shown to bind and activate VEGF R3 (Flt-4). The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stage of development. It is important for lymphangiogenesis.

Anti-Human VEGFR-3/FLT-4 Antibody

101-M38 100 µg
EUR 399
Description: Receptor tyrosine Kinase VEGFR-3, also known as FLT4, together with VEGFR1 (Flt1) and VEGFR2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides which remain linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelial cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system.

Anti-Human VEGFR-3/FLT-4 Antibody

101-M870 100 µg
EUR 399
Description: Receptor tyrosine Kinase VEGFR-3, also known as FLT4, together with VEGFR1 (Flt1) and VEGFR2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides which remain linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelial cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system.

Anti-Human VEGFR-3/FLT-4 Antibody

102-PA22 200 µg
EUR 147
Description: Receptor tyrosine Kinase VEGFR-3, also known as FLT4, together with VEGFR1 (FIT1) and VEGFR2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides remain linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelia cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system.

Anti-Human VEGFR-3/FLT-4 Antibody

102-PABi22 50 µg
EUR 157.5
Description: Receptor tyrosine Kinase VEGFR-3, also known as FLT4, together with VEGFR1 (FIT1) and VEGFR2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides remain linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelia cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system.

Peptide YY (PYY) (1-36)-Gly (Human)

059-07 100 μg
EUR 295.92

GnRH Associated Peptide (GAP) (1-13) / GnRH Precursor Peptide (14-26) (Human)

029-03 500 μg
EUR 114.48

GnRH Associated Peptide (GAP) (1-24) / GnRH Precursor Peptide (14-37) (Human)

029-04 100 μg
EUR 114.48

GnRH Associated Peptide (GAP) (1-53) / GnRH Precursor Peptide (14-66) (Human)

029-05 20 μg
EUR 267.84

[Tyr0]-RFamide-Related Peptide 1 (RFRP-1) (Human)

048-43 200 μg
EUR 177.12

Mouse FLK-1/VEGFR-2 control/blocking peptide # 1

FLK11-P 100 ug
EUR 196.8

Nesfatin-1-Like Peptide (NLP) (Human)

009-83 100 μg
EUR 469.8

Human VEGFR-1/Flt-1 (D3)-His, soluble Recombinant Protein

S01-080 50 µg
EUR 378
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

TCAP-1 / Teneurin C-terminal Associated Peptide-1 (Human)

020-16 100 μg
EUR 317.52

Mouse Monoclonal Anti-human FLT-1/VEGFR-1 IgG, aff pure

FLT12-M 100 ug
EUR 578.4

Mouse Monoclonal Anti-human FLT-1/VEGFR-1 IgG, aff pure

FLT14-M 100 ug
EUR 578.4

SHLP1 / Small Humanin-Like Peptide 1 (Human)

018-75 100 μg
EUR 263.52

prepro-Endothelin-1 (ET-1) Like Peptide (109-130) amide (Human)

023-11 100 μg
EUR 355.32

Gastrin Releasing Peptide (GRP) (1-16) (Human)

027-08 1 mg
EUR 177.12

Gastrin Releasing Peptide (GRP) (1-17) (Human)

027-42 200 μg
EUR 189

RFamide-Related Peptide 1 (RFRP-1) (Human) - FAM Labeled

FG-048-42A 1 nmol
EUR 336.96

VEGFR-3/Flt-4

JP27779 96
EUR 611

RFamide-Related Peptide 1 (RFRP-1) (Human) - Rhodamine Labeled

FR-048-42 1 nmol
EUR 336.96

NGR Peptide 1

025-74 200 μg
EUR 184.68

Nesfatin-1-Like Peptide(NLP) (Human) - RIA Kit

RK-009-83 125 tubes
EUR 980.64

Anti-Mouse VEGFR-3/FLT-4 Antibody

103-M36 100 µg
EUR 246.75
Description: VEGFR-3, also known as FLT4, is a member of the Tyr protein kinase family. The extracellular portion of VEGFR-3 contains 7 immunoglobulin (Ig)-like domains and the cytoplasmic portion contains a protein kinase domain. FLT4 regulates angiogenesis and lymphangiogenesis, its ligands are VEGF-C and D and its binding is mediated by the 2nd and 3rd Ig-like domains of FLT4. During fetal development VEGFR-3 is expressed on endothelial cells, however, in the adult mice, the vascular endothelial cells lose VEGFR-3 expression, but the lymphatic endothelium expresses it constitutively. In addition, VEGFR-3 expression can be induced in tumors with active angiogenesis.

Anti-Mouse VEGFR-3/FLT-4 Antibody

103-M38 100 µg
EUR 399
Description: Receptor tyrosine kinase VEGFR-3, also known as Flt-4, together with VEGFR-1 (Flt-1) and VEGFR-2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides remaining linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelial cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system.

Human VEGFR-3 / Flt-4 GENLISA ELISA

KBH0215 1 x 96 wells
EUR 286

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein

SFC-005 10 µg
EUR 57.75
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1(D7)) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1(D7)/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1(D7)/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein

SFC-006 50 µg
EUR 168
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1(D7)) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1(D7)/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1(D7)/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Neuroendocrine Regulatory Peptide 1 (NERP-1) / prepro-VGF (281-306) (Human) - Antibody

H-076-89 100 μl
EUR 336.96

Bone Forming Peptide 1 (BFP-1) (Human, Rat, Mouse, Bovine, Feline)

080-57 100ug
EUR 196.56

[Tyr0]-RFamide-Related Peptide 1 (RFRP-1) (Human) - I-125 Labeled

T-048-43 10 μCi
EUR 1145.88

Rabbit Anti-Mouse FLT-1/VEGFR-1 (279-299aa) IgG, aff pure

FLT15-A 100 ul
EUR 578.4

[Biotinyl-Gln1]-TCAP-1 / Teneurin C-terminal Associated Peptide-1 (Human)

B-020-16 20 μg
EUR 336.96

Neuroendocrine Regulatory Peptide 1 (NERP-1) / prepro-VGF (281-306) (Human)

076-89 100 μg
EUR 214.92

VEGF receptor Flt-1 (F56), Peptide Aptamer, unlabeled

AP-334-U 5 mg Ask for price

Growth Hormone-Releasing Peptide-Related Peptide-1 (fGRP-RP-1) (Frog)

048-80 500 μg
EUR 177.12

[Tyr0]-Neuroendocrine Regulatory Peptide 1 (NERP-1) (Human) - I-125 Labeled

T-076-93 10 μCi
EUR 1145.88

Peptide F 1 (Lobster)

047-62 500 μg
EUR 73.44

Peptide Lv (Human)

008-71 100 μg
EUR 405

Peptide YY (PYY) (Human) - Antibody

H-059-01 100 μl
EUR 469.8

VEGF receptor Flt-1 (F56), Peptide Aptamer, Biotinylated

AP-334-B 1 mg Ask for price

Neuroendocrine Regulatory Peptide 1 (NERP-1) / prepro-VGF (281-306) (Human) - Purified IgG Antibody

G-076-89 100 μg
EUR 370.44

Calmodulin Binding Peptide 1

070-17 20 μg
EUR 214.92

Human VEGFR-3/FLT-4/Fc Chimera, soluble

SFC-010 50ug
EUR 378

Rabbit Anti-Mouse FLT-4/VEGFR-3 IgG #1, aff pure

FLT41-A 100 ug
EUR 578.4

Neuroendocrine Regulatory Peptide 1 (NERP-1) / prepro-VGF (281-306) (Human) - EIA Kit

EK-076-89 96 wells
EUR 645.84

Neuroendocrine Regulatory Peptide 1 (NERP-1) / prepro-VGF (281-306) (Human) - RIA Kit

RK-076-89 125 tubes
EUR 932.04

Peptide YY (PYY) (Human)

059-01 200 μg
EUR 119.88

Erythropoietin-Mimetic Peptide 1 (EMP-1)

070-27 100 μg
EUR 160.92

Anti-Inflammatory Peptide 2

004-02 200 μg
EUR 27

Anti-Inflammatory Peptide 3

004-03 200 μg
EUR 27

Neuroendocrine Regulatory Peptide 1 (NERP-1) / prepro-VGF (281-306) (Human) - FAM Labeled

FG-076-89A 1 nmol
EUR 336.96

Neuroendocrine Regulatory Peptide 1 (NERP-1) / prepro-VGF (281-306) (Human) - FITC Labeled

FG-076-89B 1 nmol
EUR 336.96

[Ser3(Des-Octanoyl)]-Ghrelin (1-18) / Motlin-Related Peptide (Human)

031-47 100 μg
EUR 199.8

Peptide YY (PYY) (3-36) (Human) - Antibody

H-059-02 100 μl
EUR 604.8

VEGF receptor Flt-1 (F56), Peptide Aptamer, FITC labelled

AP-334-F 1 mg Ask for price

Neuroendocrine Regulatory Peptide 1 (NERP-1) / prepro-VGF (281-306) (Human) - Biotin Labeled

B-076-89 20 μg
EUR 336.96

Anti-Angiogenic Peptide Library

L-008A 88 peptides
EUR 6067.44

GnRH Associated Peptide (GAP) (25-53) / GnRH Precursor Peptide (38-66) (Human)

029-06 100 μg
EUR 114.48

prepro-IGFBP-5 (98-122) peptide 1 (Human, Rat, Mouse, Bovine, Porcine)

033-73 100 μg
EUR 267.84

Anti-Human VEGFR1-14/Flt1-14 (peptide), soluble Antibody

101-M29 100 µg
EUR 199.5
Description: A human-specific splicing variant of vascular endothelial growth factor (VEGF) receptor 1 (Flt1) was discovered, producing a soluble receptor (designated sFlt1-14) that is qualitatively different from the previously described soluble receptor (sFlt1) and functioning as a potent VEGF inhibitor. sFlt1-14 is generated in a cell type-specific fashion, primarily in non-endothelial cells. Notably, in vascular smooth muscle cells, all Flt1 messenger RNA is converted to sFlt1-14, whereas endothelial cells of the same human vessel express sFlt1. sFlt1-14 expression by vascular smooth muscle cells is dynamically regulated as evidenced by its upregulation on coculture with endothelial cells or by direct exposure to VEGF. Increased production of soluble VEGF receptors during pregnancy is entirely attributable to induced expression of placental sFlt1-14 starting by the end of the first trimester. Expression is dramatically elevated in the placenta of women with preeclampsia, specifically induced in abnormal clusters of degenerative syncytiotrophoblasts known as syncytial knots, where it may undergo further messenger RNA editing. sFlt1-14 is the predominant VEGF-inhibiting protein produced by the preeclamptic placenta, accumulates in the circulation, and hence is capable of neutralizing VEGF in distant organs affected in preeclampsia. Together, these findings revealed a new natural VEGF inhibitor that has evolved in humans, possibly to protect non-endothelial cells from adverse VEGF signaling. Furthermore, the study uncovered the identity of a VEGF-blocking protein implicated in preeclampsia.

Active Recombinant Human VEGFR-3/FLT-4 Protein

RP00123 10 μg
EUR 175.5

Peptide Histidine Methionine 27 (PHM-27) / Peptide Histidine Isoleucine (PHI) (Human) - Antibody

H-064-07 50 μl
EUR 238.68

Human VEGFR-3/FLT-4, soluble Recombinant Protein

S01-017 10 µg
EUR 103.95
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.

Human VEGFR-3/FLT-4, soluble Recombinant Protein

S01-017S 5 µg
EUR 63
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.

Human VEGFR-3/FLT-4, soluble Recombinant Protein

S01-018 50 µg
EUR 210
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23 aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751 aa residue extracellular domain, a 22 aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.

Peptide YY (PYY) (3-36)-Gly (Human) - Antibody

H-059-08 100 μl
EUR 469.8

Galanin-Like Peptide (GALP) (Human) - Antibody

H-026-51 50 μl
EUR 604.8

Neuroendocrine Regulatory Peptide 1 (NERP-1) (Rat)

076-90 100 μg
EUR 214.92

[Cys0]-Peptide YY (PYY) (3-19) (Human) - Antibody

H-059-16 100 μl
EUR 469.8

[Cys20]-Peptide YY (PYY) (3-19) (Human) - Antibody

H-059-17 100 μl
EUR 469.8

Peptide-Depleted Plasma (Human)

MB-099-01 2 ml
EUR 119.88

Angiotensin II - constrained peptide 1

004-09 500 μg
EUR 165.24

Peptide YY (PYY) (Human) - Purified IgG Antibody

G-059-01 400 μg
EUR 438.48

Peptide YY (PYY) (3-36) (Human)

059-02 200 μg
EUR 102.6

Gastrin Releasing Peptide (GRP) (Human) - Antibody

H-027-07 50 μl
EUR 238.68

RFamide-Related Peptide 1 (RFRP-1) (Rat, Mouse)

048-48 500 μg
EUR 177.12

GnRH Associated Peptide (GAP) (1-13) / Gn-RH Precursor Peptide (14-26) (Rat)

029-08 200 μg
EUR 64.8

FLT-1/VEGFR1 Human, Antibody

GWB-BE9645 0.1 mg Ask for price

Stresscopin Related Peptide (SRP) (Human) - Antibody

H-019-27 50 μl
EUR 604.8

C28 optimized peptide 6 (Human)

073-82 100 μg
EUR 235.44

Peptide YY (PYY) (Human) - EIA Kit

EK-059-01 96 wells
EUR 617.76

Peptide YY (PYY) (Human) - RIA Kit

RK-059-01 125 tubes
EUR 814.32

Neuroendocrine Regulatory Peptide 1 (NERP-1) / prepro-VGF (281-306) (Human) - Cy3 Labeled Purified IgG

FC3-G-076-89 100 μl
EUR 756

Neuroendocrine Regulatory Peptide 1 (NERP-1) / prepro-VGF (281-306) (Human) - Cy5 Labeled Purified IgG

FC5-G-076-89 100 μl
EUR 756

Neuroendocrine Regulatory Peptide 1 (NERP-1) / prepro-VGF (281-306) (Human) - FAM Labeled Purified IgG

FG-G-076-89A 100 μl
EUR 469.8

Nesfatin-1-Like Peptide (NLP) (Rat)

009-85 100 μg
EUR 461.16

Galanin-Like Peptide (GALP) (Human)

026-51 100 μg
EUR 230.04

PACAP-Related Peptide (PRP) (Human)

052-10 200 μg
EUR 86.4

Peptide Histidine Methionine 27 (PHM-27) / Peptide Histidine Isoleucine (PHI) (Human)

064-07 200 μg
EUR 114.48

Neuroendocrine Regulatory Peptide 1 (NERP-1) / prepro-VGF (281-306) (Human) - FITC Labeled Purified IgG

FG-G-076-89B 100 μl
EUR 469.8

Human Vascular Endothelial Growth Factor Receptor 1 / VEGFR1 (FLT1) Peptide (OVA)

abx165607-100g 100 µg
EUR 1800

Human Vascular Endothelial Growth Factor Receptor 1 / VEGFR1 (FLT1) Peptide (OVA)

abx165607-10g 10 µg
EUR 475

Human Vascular Endothelial Growth Factor Receptor 1 / VEGFR1 (FLT1) Peptide (OVA)

abx165607-50g 50 µg
EUR 575

Nesfatin-1-Like Peptide (NLP) (Mouse)

009-81 100 μg
EUR 469.8

T3 Peptide / Tumstatin (69-88) (Human)

016-50 100 μg
EUR 255.96

T7 Peptide / Tumstatin (74-98) (Human)

016-51 100 μg
EUR 255.96

VEGF receptor KDR and Flt-1 (v107), Peptide Aptamer, unlabeled

AP-335-U 5 mg Ask for price

Galanin-Like Peptide (GALP) (36-60) (Human) - Antibody

H-026-55 50 μl
EUR 604.8

Peptide Histidine Methionine 27 (PHM-27) / Peptide Histidine Isoleucine (PHI) (Human) - Purified IgG Antibody

G-064-07 400 μg
EUR 438.48

Peptide YY (PYY) (3-36)-Gly (Human)

059-08 100 μg
EUR 282.96

Peptide YY (PYY) (2-36)-Gly (Human)

059-11 100 μg
EUR 267.84

Peptide YY (PYY) (4-36)-Gly (Human)

059-12 100 μg
EUR 267.84

Gastrin Releasing Peptide (GRP) (Human)

027-07 200 μg
EUR 119.88

Neuroendocrine Regulatory Peptide 1 (NERP-1) / prepro-VGF (281-306) (Human) - Biotin Labeled Purified IgG

B-G-076-89 100 μl
EUR 672.84

Peptide I / pro-Histine-Rich Basic Peptide (HRBP) (1-26) (Aplysia brasiliana)

047-39 200 μg
EUR 444.96

Peptide I / pro-Histine-Rich Basic Peptide (HRBP) (1-26) (Aplysia californica)

047-42 200 μg
EUR 444.96

JAG-1 Protein Active Peptide Fragment

080-11 100 μg
EUR 129.6

Peptide YY (PYY) (3-36) (Human) - Purified IgG Antibody

G-059-02 200 μg
EUR 604.8

Prolactin-Releasing Peptide-31 (PrRP-31) (Human) - Antibody

H-008-50 50 μl
EUR 604.8

Bombinin-Like Peptide 1 amide / prepro-Bombinin-Like Peptide (44-70) amide / prepro-Bombinin-Like Peptide (107-133) amide

007-60 100 μg
EUR 214.92

[Tyr0]-RFamide-Related Peptide 1 (RFRP-1) (Rat, Mouse)

048-49 200 μg
EUR 177.12

Gastrin Releasing Peptide (GRP) (1-16) (Porcine) - Antibody

H-027-15 50 μl
EUR 238.68

SHAAG Peptide / Chemokine (46-63) (Human)

072-32 100 μg
EUR 160.92

Stresscopin Related Peptide (SRP) (Human)

019-27 100 μg
EUR 214.92

Rat Monoclonal anti-Mouse VEGFR-3 (FLT-4) Antibody

xAP-0836 100ug
EUR 280

Achatina Cardio-Excitatory Peptide-1 (ACEP-1) (Achatina fulica)

047-02 500 μg
EUR 114.48

Fractalkine Chemokine Domain peptide (41-52) (Human)

026-82 200 μg
EUR 160.92

Fractalkine Chemokine Domain peptide (53-60) (Human)

026-83 200 μg
EUR 135

The particular procedures reported right here complement various protocols for AAV manufacturing described by others and us earlier than, and, collectively, ought to allow any laboratory to generate these vectors on a small-to-medium scale for ex vivo or in vivo expression of optogenetic parts.

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