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V6012

Vascular Endothelial Growth Factor D human

recombinant, expressed in baculovirus infected Sf21 cells, powder, suitable for cell culture

Synonym(s):

VEGF-D, c-fos-induced growth factor (FIGF)

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About This Item

UNSPSC Code:
12352200
MDL number:
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biological source

human

recombinant

expressed in baculovirus infected Sf21 cells

assay

≥95% (SDS-PAGE)

form

powder

potency

8-500 ng/mL

mol wt

13 kDa

storage condition

avoid repeated freeze/thaw cycles

technique(s)

cell culture | mammalian: suitable

impurities

endotoxin, tested

UniProt accession no.

storage temp.

−20°C

Gene Information

Application

VEGF-D is involved in the regulation of the growth and/or differentiation of lymphatic endothelium and thus, a mitogen for endothelial cells

Biochem/physiol Actions

Vascular Endothelial Growth Factor D (VEGF-D), also known as c-fos-induced growth factor (FIGF), is a member of the VEGF family of growth factors. Vascular endothelial growth factor (VEGF) family consists of closely related growth factors having a conserved pattern of eight cysteine residues and sharing common VEGF receptors. VEGF is a dimeric glycoprotein that stimulates endothelial cells, induces angiogenesis, promotes cell migration, increases vascular permeability and inhibits apoptosis. VEGF-D is most closely related to VEGF-C (23.3% amino acid sequence identity) and has similar VEGF homology domain that spans the middle third of the precursor protein, and long N- and C-terminal extensions.

In adults, VEGF-D is highly expressed in lung, heart, muscle and small intestine. VEGF-D has special relevance in the vascularization of lung tissue during the last trimester of fetal development. Recombinant human VEGF-D is a ligand for the tyrosine kinases, VEGF receptor 2 (Flk1) and VEGF receptor 3 (Flt4). VEGF R3 is strongly expressed in lymphatic endothelial cells and it is postulated that VEGF-D is involved in the regulation of the growth and/or differentiation of lymphatic endothelium and thus, a mitogen for endothelial cells.

Physical form

Lyophilized in phosphate buffered saline containing 1.25 mg bovine serum albumin.

Preparation Note

Recombinant Human Vascular Endothelial Growth Factor D (VEGF-D) is produced from the DNA sequence encoding the VEGF domain of human VEGFD and fused to the signal peptide of CD33 at the N-terminus and to a 6X histidine tag at the C-terminus. The chimeric protein is expressed in Sf 21 cells using a baculovirus expression system. Based on N-terminal sequencing, Met 17 from the CD33 signal peptide is retained in the recombinant protein. This methionyl form contains 115 amino acid residues with a calculated molecular mass of approximately 13 kDa. As a result of glycosylation, the recombinant protein migrates as a 20 and 22 kDa protein in SDS-PAGE under reducing and non-reducing conditions. This recombinant VEGF-D also contains a small amount of disulfide-linked homodimeric VEGF-D.

Analysis Note

The biological activity of VEGF-D is measured by its ability to bind to recombinant human FLT-4/Fc in a ELISA assay.


Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

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Related Content


M G Achen et al.
Proceedings of the National Academy of Sciences of the United States of America, 95(2), 548-553 (1998-01-22)
We have identified a member of the VEGF family by computer-based homology searching and have designated it VEGF-D. VEGF-D is most closely related to VEGF-C by virtue of the presence of N- and C-terminal extensions that are not found in
F Farnebo et al.
Biochemical and biophysical research communications, 257(3), 891-894 (1999-04-20)
Endothelial growth factors have become the target of intense research since the initial discovery of vascular endothelial growth factor (VEGF/VPF). At present, VEGF is established as a major inducer of angiogenesis in normal and pathological conditions. Recently several new members
Structure, expression and receptor-binding properties of novel vascular endothelial growth factors.
U Eriksson et al.
Current topics in microbiology and immunology, 237, 41-57 (1999-01-20)