VEGF-F antibody

Catalog No. ABIN1589914

The Rabbit Polyclonal anti-VEGF-F antibody (ABIN1589914) specifically detects VEGF-F in WB. The antibody is reactive with Bothrops insularis samples.

Quick Overview for VEGF-F antibody (ABIN1589914)

Target: VEGF-F

Reactivity: Bothrops insularis

Host: Rabbit

Clonality: Polyclonal

Application: Western Blotting (WB)

Product Details

Purpose: VEGF-F (Bothrops insularis) antibody

Specificity: Recombinant snake-venom VEGF-F

Purification: Protein A purified

Immunogen: Recombinant snake-venom VEGF-F (ABIN1589540 and ABIN1589541)

Isotype: IgG

Application Details

Application Notes: Western Blot: Use 2-5 μg/mL

Restrictions: For Research Use only

Handling

Format: Lyophilized

Reconstitution: Centrifuge vial prior to opening. Reconstitute in sterile water to a concentration of 0.1-1.0 mg/mL.

Buffer: PBS

Handling Advice: Centrifuge vial prior to opening.

Storage: 4 °C,-20 °C

Storage Comment: The lyophilized antibody is stable for at least 2 years at -20°C. After sterile reconstitution the antibody is stable at 2-8°C for up to 6 months. Frozen aliquots are stable for at least 6 months when stored at -20°C. Addition of a carrier protein or 50% glycerol is recommended for frozen aliquots.

Expiry Date: 24 months

Target Details

Target: VEGF-F

Background: Vascular Endothelial Growth Factor-F,Vascular endothelial growth factor (VEGF-A) and its family proteins are crucial regulators of blood vessel formation and vascular permeability. Snake venom has recently been shown to be an exogenous source of unique VEGF (known as VEGF-F), and now, two types of VEGF-F with distinct biochemical properties have been reported. VEGF-Fs (venom type VEGFs) are highly variable in structure and function among species, in contrast to endogenous tissue-type VEGFs (VEGF-As) of snakes. Although the structures of tissue-type VEGFs are highly conserved among venomous snake species and even among all vertebrates, including humans, those of venom-type VEGFs are extensively variegated, especially in the regions around receptor-binding loops and C-terminal putative coreceptor-binding regions, indicating that highly frequent variations are located around functionally key regions of the proteins. Genetic analyses suggest that venom-type VEGF gene may have developed from a tissue-type gene and that the unique sequence of its C-terminal region was generated by an alteration in the translation frame in the corresponding exons. The svVEGF-F was identified during the generation of abundant expressed sequence tags from the Viperidae snake Bothrops insularis venom glands. The deduced primary sequence, after complete sequencing of the longest snake venom VEGF (svVEGF) cDNA, displayed similarity with vertebrate VEGFs and with the hypotensive factor from Vipera aspis venom. The mature svVEGF appears to be ubiquitously distributed throughout snake venoms and was also confirmed by Northern blot studies of other related Viperidae species and by cDNA cloning of svVEGF from Bothrops jararaca pit viper. The produced recombinant protein dimerizes after refolding processes and was biologically characterized, showing ability to increase vascular permeability. These results established that svVEGF is a novel and important active toxin during the early stages of bothropic snake bite envenoming and represents a new member of the VEGF family of proteins.

UniProt: Q90X24