EG VEGF Mouse

Endocrine Gland Vascular Endothelial Growth Factor Mouse Recombinant

This product consists of a single, non-glycosylated polypeptide chain of EG-VEGF, with 86 amino acids and a molecular weight of 9.6kDa. It is produced through recombinant DNA technology in E. coli bacteria.
Shipped with Ice Packs
Cat. No.
BT5987
Source
Escherichia Coli.
Appearance
This product is provided as a white powder that has been freeze-dried and sterilized.

VEGF (121 a.a.) Human

Vascular Endothelial Growth Factor (121 a.a.) Human Recombinant

Recombinant Human Vascular Endothelial Growth Factor-121, produced in E. coli, is a non-glycosylated polypeptide chain dimer. Each monomer contains 121 amino acids, resulting in a molecular weight of 28.4 kDa for the dimer. Compared to other VEGF isoforms that bind strongly to vascular heparin sulfates, VEGF121 exhibits higher circulatory freedom.

Shipped with Ice Packs
Cat. No.
BT6039
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder.

VEGF (121 a.a.) Human, Sf9

Vascular Endothelial Growth Factor (121 a.a.) Human Recombinant, Sf9

Recombinant Human Vascular Endothelial Growth Factor-121, produced in insect cells, is a glycosylated homodimer with a molecular weight of approximately 36kDa. It comprises two 18kDa polypeptide chains, each containing 121 amino acids. VEGF121 exhibits greater circulatory freedom compared to other VEGF forms due to its weaker binding affinity to vascular heparin sulfates. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6134
Source
Sf9, Insect Cells.
Appearance
Sterile Filtered White lyophilized powder.

VEGF Equine

Vascular Endothelial Growth Factor Equine Recombinant

Recombinant Equine VEGF, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 2 x 165 amino acids, resulting in a total molecular mass of 38.6 kDa. The purification process involves proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT6974
Source

Escherichia Coli.

Appearance
Sterile Filtered White lyophilized powder.

VEGF Human

Vascular Endothelial Growth Factor Human Recombinant

Recombinant Human Vascular Endothelial Growth Factor, produced in E. coli, is a non-glycosylated polypeptide chain consisting of two identical chains. Each chain contains 165 amino acids, resulting in a total molecular mass of 38.2 kDa. The purification of VEGF is achieved through specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT7088
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder.

VEGF Human (121 a.a.), His

Vascular Endothelial Growth Factor-121 Human Recombinant, His Tag

Recombinant Human Vascular Endothelial Growth Factor-121, expressed in E. coli, is a non-glycosylated polypeptide chain comprising amino acids 207-327. This 142-amino acid protein, with a molecular weight of 16.3 kDa, consists of two identical polypeptide chains. A 20-amino acid His tag is fused to the N-terminus of VEGF-121. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7236
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

VEGF Rat, His

Vascular Endothelial Growth Factor Rat Recombinant, His Tag

Recombinant Rat VEGF, expressed in E. coli, is a single-chain polypeptide that lacks glycosylation. It comprises 145 amino acids (spanning positions 206 to 325) and has a molecular weight of 16.7 kDa. The protein includes a 25 amino acid His-tag at its N-terminus to facilitate purification, which is achieved through specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT8454
Source
Escherichia Coli.
Appearance
A clear and colorless solution that has been sterilized by filtration.

VEGF Rat, Yeast

Vascular Endothelial Growth Factor Rat Recombinant, Yeast

Recombinant Rat Vascular Endothelial Growth Factor, produced in yeast, is a homodimeric protein linked by disulfide bonds. It comprises two polypeptide chains, each containing 165 amino acids, resulting in a molecular mass of approximately 25.7 kDa per chain. The purification process of VEGF involves proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT8548
Source

Saccharomyces cerevisiae

Appearance

Sterile Filtered White lyophilized powder.

VEGFC Human HEK

Vascular Endothelial Growth Factor C Human Recombinant HEK

Recombinant Human VEGFC, produced in transfected human cells, is a single polypeptide chain comprising 204 amino acids (residues 32-227). The protein includes an 8 amino acid His-tag fused at the C-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT8635
Source
HEK293 cells.
Appearance
White, lyophilized (freeze-dried) powder, sterile-filtered.

VEGFC Human, Sf9

Vascular Endothelial Growth Factor C Human Recombinant, Sf9

Recombinant Human VEGFC, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain comprising 125 amino acids (spanning positions 112 to 227). It has a molecular mass of 14.2 kDa. On SDS-PAGE, the apparent molecular size will appear between 18-28 kDa due to glycosylation. This protein is engineered with a 6-amino acid His tag located at the C-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8705
Source
Sf9, Baculovirus cells.
Appearance
A clear and colorless solution that has been sterilized by filtration.
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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