VEGF E (Orf Virus)

Vascular Endothelial Growth Factor-E Recombinant (Orf Virus)

A DNA sequence encoding the mature variant of ovVEGF-E isolate D1701 (Dehio et al., 1999; GenBank accession No. AF106020) was expressed in E. coli as a 132 amino acid residue fusion protein with an N-terminal His-tag sequence and a thrombin cleavage site. Recombinant VEGF-E homodimer was dimerized in vitro and has a predicted mass of approximately 35 kDa.
Shipped with Ice Packs
Cat. No.
BT6861
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

VEGF Equine

Vascular Endothelial Growth Factor Equine Recombinant

VEGF Equine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 2 x 165 amino acids and having a total molecular mass of 38.6 kDa.
The VEGF is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT6974
Source

Escherichia Coli.

Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

VEGF Human

Vascular Endothelial Growth Factor Human Recombinant

Vascular Endothelial Growth Factor Human Recombinant produced in E.Coli is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 38.2kDa.
The VEGF is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7088
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

VEGF Human (121 a.a.), His

Vascular Endothelial Growth Factor-121 Human Recombinant, His Tag

Vascular Endothelial Growth Factor-121 Human Recombinant produced in E.Coli is a double, non-glycosylated, polypeptide chain (aa 207-327) containing a total of 142 amino acids and having a molecular mass of 16.3 kDa.
The VEGF-121 is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7236
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

VEGF Human, Baculovirus

Vascular Endothelial Growth Factor Human Recombinant, Baculovirus

VEGF produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 171 amino acids (27-191 a.a.) and having a molecular mass of 19.9 kDa.

VEGF is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT7335
Source
Sf9, Baculovirus cells.
Appearance
Sterile filtered colorless solution.

VEGF Human, CHO

Vascular Endothelial Growth Factor Human Recombinant, CHO

Vascular Endothelial Growth Factor Human Recombinant produced in CHO cells is a double, glycosylated, polypeptide chain containing 165 amino acids and migrates as 44 kDa in SDS-PAGE under non-reducing conditions.
The VEGF is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7407
Source
Chinese Hamster Ovarian Cell.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

VEGF Human, HEK

Vascular Endothelial Growth Factor Human Recombinant, HEK

Vascular Endothelial Growth Factor Human Recombinant produced in HEK293 cells is a double, glycosylated, polypeptide chain containing 165 amino acids (27-191) and having a molecular mass of 40 kDa. The VEGF is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7517
Source
HEK293 (Human Embryonic Kidney cell line).
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

VEGF Human, His

Vascular Endothelial Growth Factor Human Recombinant, His

Vascular Endothelial Growth Factor Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain (aa 207-371) containing a total of 185 amino acids and having a molecular mass of 21.3 kDa (corresponding to Isoform L-VEGF165 UniProt acc#P15692-11).
The VEGF is fused to a 20 a.a His-tag at N-terminus and is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7614
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

VEGF Human, Plant

Vascular Endothelial Growth Factor Human Recombinant, Plant

Vascular Endothelial Growth Factor Human Recombinant produced in Oryza Sativa has a molecular mass of 19.2kDa. The VEGF is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT7677
Source

Rice Grain

Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

VEGF Human, Yeast

Vascular Endothelial Growth Factor Human Recombinant, Yeast

Vascular Endothelial Growth Factor Human Recombinant produced in Yeast is a double, glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 42 kDa.
Shipped with Ice Packs
Cat. No.
BT7754
Source
Pichia Pastoris.
Appearance
Sterile Filtered colorless liquid formulation.
Definition and Classification

Vascular Endothelial Growth Factor (VEGF) is a signal protein produced by many cells that stimulates the formation of blood vessels. It is a sub-family of growth factors, specifically the platelet-derived growth factor family of cystine-knot growth factors . The VEGF family in mammals comprises five members: VEGF-A, VEGF-B, VEGF-C, VEGF-D, and Placenta Growth Factor (PGF) . Additionally, VEGF-related proteins encoded by viruses (VEGF-E) and in the venom of some snakes (VEGF-F) have also been discovered .

Biological Properties

VEGF proteins are crucial signaling molecules involved in vasculogenesis (the formation of the embryonic circulatory system) and angiogenesis (the growth of blood vessels from pre-existing vasculature) . They are expressed in various tissues, particularly in vascularized tissues . VEGF is also involved in the formation of new blood vessels during embryonic development, after injury, and in muscles following exercise . The expression of VEGF is regulated by factors such as oxygen tension, cytokines, and differentiation .

Biological Functions

The primary function of VEGF is to promote the growth of new blood vessels. It plays a critical role in embryonic development, wound healing, and the formation of collateral circulation to bypass blocked vessels . VEGF is also involved in immune responses by being chemotactic for granulocytes and macrophages . It contributes to pathological conditions such as tumor growth and metastasis, as well as vascular diseases in the retina .

Modes of Action

VEGF exerts its effects by binding to tyrosine kinase receptors (VEGFRs) on the cell surface, leading to receptor dimerization and activation through transphosphorylation . The primary receptors for VEGF are VEGFR-1 (Flt-1) and VEGFR-2 (KDR/Flk-1) . These receptors activate downstream signaling cascades that promote endothelial cell proliferation, migration, and survival . VEGF also interacts with co-receptors such as neuropilins, which modulate its activity .

Regulatory Mechanisms

The expression and activity of VEGF are tightly regulated at multiple levels. Transcriptional regulation is influenced by oxygen levels, with hypoxia being a major inducer of VEGF gene transcription . Other regulatory factors include growth factors, hormones, and oncogenes . Post-translational modifications, such as phosphorylation, also play a role in modulating VEGF activity . Additionally, VEGF signaling is regulated by the availability of its receptors and the presence of co-receptors .

Applications

VEGF has significant applications in biomedical research, diagnostics, and therapeutics. In research, recombinant VEGF proteins are used to study angiogenesis and related signaling pathways . Clinically, VEGF inhibitors such as bevacizumab (Avastin) are used to treat cancers by inhibiting tumor angiogenesis . VEGF is also targeted in therapies for age-related macular degeneration and diabetic retinopathy . Diagnostic tools measuring VEGF levels can help in assessing disease progression and treatment efficacy .

Role in the Life Cycle

VEGF plays a vital role throughout the life cycle, from development to aging and disease. During embryogenesis, VEGF is essential for the formation of the vascular system . In adults, it is involved in physiological processes such as wound healing, menstrual cycles, and pregnancy . VEGF also contributes to pathological conditions, including cancer, retinopathy, and inflammatory diseases . Its role in promoting angiogenesis makes it a critical factor in both normal physiology and disease states .

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