VEGF Mouse

Vascular Endothelial Growth Factor Mouse Recombinant

Vascular Endothelial Growth Factor Mouse Recombinant produced in E.Coli is a disulfide-linked homodimeric, double polypeptide chains containing 165 amino acids and having a molecular mass of 38.8kDa.

Shipped with Ice Packs
Cat. No.
BT7818
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

VEGF Mouse (121 a.a.), Yeast

Vascular Endothelial Growth Factor (121 a.a.) Mouse Recombinant, Yeast

Vascular Endothelial Growth Factor (121 a.a.) Mouse Recombinant produced in yeast is a disulfide-linked homodimer consisting of 2x121 amino acid polypeptide chains, having a molecular mass of approximately 20.7kDa each.
VEGF (121 a.a.) is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT7913
Source

Saccharomyces cerevisiae

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

VEGF Mouse, His

Vascular Endothelial Growth Factor Mouse Recombinant, His Tag

VEGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids (205-324 a.a.) and having a total molecular mass of 16.3kDa.
Mouse VEGF is fused to 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8030
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

VEGF Mouse, Sf9

Vascular Endothelial Growth Factor Mouse Recombinant, Sf9

Vascular Endothelial Growth Factor Mouse Recombinant produced in Sf9 insect cells is a double, glycosylated, polypeptide chain containing 164 amino acids and having a molecular mass of 48 kDa.
The VEGF is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8124
Source
Baculovirus Sf9 cells.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

VEGF Mouse, Yeast

Vascular Endothelial Growth Factor Mouse Recombinant, Yeast

Vascular Endothelial Growth Factor Mouse Recombinant produced in yeast is a disulfide-linked homodimer consisting of 2x165 amino acid polypeptide chains, having a molecular mass of approximately 40.0kDa each.
VEGF is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT8190
Source

Saccharomyces cerevisiae

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

VEGF Rat

Vascular Endothelial Growth Factor Rat Recombinant

Vascular Endothelial Growth Factor Rat Recombinant produced in E.Coli is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 38,750 Dalton.
The VEGF is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8266
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

VEGF Rat (120a.a.), Yeast

Vascular Endothelial Growth Factor (120a.a.) Rat Recombinant, Yeast

Vascular Endothelial Growth Factor(120a.a.) Rat Recombinant produced in yeast is a disulfide-linked homodimer consisting of 2x121 amino acid polypeptide chains, having a molecular mass of approximately 18.5kDa each.
VEGF is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT8393
Source

Saccharomyces cerevisiae

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

VEGF Rat, His

Vascular Endothelial Growth Factor Rat Recombinant, His Tag

VEGF Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (206-325 a.a) and having a molecular mass of 16.7kDa.
VEGF is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8454
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

VEGF Rat, Yeast

Vascular Endothelial Growth Factor Rat Recombinant, Yeast

Vascular Endothelial Growth Factor Rat Recombinant produced in yeast is a disulfide-linked homodimer consisting of 2x165 amino acid polypeptide chains, having a molecular mass of approximately 25.7kDa each.
VEGF is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT8548
Source

Saccharomyces cerevisiae

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

VEGFC Human HEK

Vascular Endothelial Growth Factor C Human Recombinant HEK

VEGFC Human Recombinant produced by transfected human cells is a single polypeptide chain containing 204 amino acids (32-227). VEGFC is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8635
Source
HEK293 cells.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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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