VEGF Mouse (121 a.a.), Yeast

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

Recombinant Mouse Vascular Endothelial Growth Factor (121 a.a.), produced in yeast, is a disulfide-linked homodimer comprising two 121 amino acid polypeptide chains, each with a molecular mass of approximately 20.7kDa. Purification is achieved through 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

Recombinant Mouse VEGF, produced in E. coli bacteria, is a single, non-glycosylated polypeptide chain comprising 141 amino acids (corresponding to amino acids 205-324 of the full-length protein). It has a molecular weight of 16.3 kDa. This Mouse VEGF variant is fused to a 20 amino acid Histidine (His) tag at its N-terminus to facilitate purification, which is carried out using specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT8030
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

VEGF Rat

Vascular Endothelial Growth Factor Rat Recombinant

Recombinant Rat Vascular Endothelial Growth Factor, produced in E. coli, is a non-glycosylated polypeptide chain comprising 165 amino acids. It forms a dimer with a molecular weight of 38,750 Daltons. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8266
Source
Escherichia Coli.
Appearance
Sterile, white, lyophilized powder.

VEGF Rat (120a.a.), Yeast

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

Recombinant Rat Vascular Endothelial Growth Factor (120a.a.), produced in yeast, is a homodimer protein consisting of two identical polypeptide chains, each comprising 121 amino acids. The two chains are linked together by disulfide bonds, resulting in a total molecular weight of approximately 18.5 kDa per chain. The purification process involves proprietary chromatographic techniques to ensure high purity.

Shipped with Ice Packs
Cat. No.
BT8393
Source

Saccharomyces cerevisiae

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

EG VEGF Human

Endocrine Gland Vascular Endothelial Growth Factor Human Recombinant

This product consists of a single, non-glycosylated polypeptide chain of EG-VEGF, produced in E. coli bacteria. Containing 86 amino acids, it has a molecular weight of 9.7kDa. The EG-VEGF is purified using specialized chromatographic techniques to ensure its high quality.
Shipped with Ice Packs
Cat. No.
BT5323
Source
Escherichia Coli.
Appearance
The product appears as a white powder, sterilized by filtration and freeze-dried.

VEGF (121 a.a.) Mouse

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

Recombinant Mouse VEGF-121, produced in E. coli, is a non-glycosylated, homodimeric polypeptide chain comprising 121 amino acids. This truncated version of Murine VEGF-165 has a molecular mass of 28.4 kDa. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6238
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder.

VEGF (121a.a.) Human, HEK

Vascular Endothelial Growth Factor (121) Human Recombinant, HEK

Recombinant Human VEGF, encompassing 121 amino acids and produced in HEK cells, is a glycosylated protein. It exists in two forms: a homodimer with a molecular weight of 37kDa and a homotrimer with a molecular weight of 50kDa. The VEGF protein undergoes a purification process using specialized chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6314
Source
HEK.
Appearance
Sterile Filtered White lyophilized powder.

VEGF Human, Baculovirus

Vascular Endothelial Growth Factor Human Recombinant, Baculovirus

Produced in Sf9 Baculovirus cells, this recombinant VEGF protein is a single, glycosylated polypeptide chain. It consists of 171 amino acids (specifically, amino acids 27-191), resulting in a molecular mass of 19.9 kDa. For purification and detection purposes, a 6 amino acid His tag is present at the C-terminus. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7335
Source
Sf9, Baculovirus cells.
Appearance
The product is a sterile, colorless solution that has been filtered for sterility.

VEGF Human, CHO

Vascular Endothelial Growth Factor Human Recombinant, CHO

Recombinant Human Vascular Endothelial Growth Factor, produced in CHO cells, is a glycosylated polypeptide chain dimer comprising 165 amino acids per monomer. It exhibits a molecular weight of approximately 44 kDa under non-reducing conditions in SDS-PAGE. The purification process utilizes proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7407
Source
Chinese Hamster Ovarian Cell.
Appearance
Sterile, white lyophilized powder.

VEGF Human, HEK

Vascular Endothelial Growth Factor Human Recombinant, HEK

Recombinant Human Vascular Endothelial Growth Factor, produced in HEK293 cells, is a glycosylated polypeptide chain dimer. It comprises 165 amino acids (27-191) and has a molecular weight of 40 kDa. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7517
Source
HEK293 (Human Embryonic Kidney cell line).
Appearance
Sterile, white lyophilized 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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