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Orf Virus VEGF-E, Heparin-binding
Orf Virus VEGF-E, Heparin-binding
- 中文名称：
- Orf Virus VEGF-E, Heparin-binding
- 英文名称：
- Orf Virus VEGF-E, Heparin-binding
- 品牌：
- AAA Biotech
- 品牌介绍：
- AAA Biotech专注于为全球生命科学研究提供高品质的蛋白质研究工具，核心产品包括经严格验证的抗体、重组蛋白及ELISA试剂盒。
- 货号：
- AAA79256
- 规格：
- 0.005 mg|2x0.005 mg|3x0.005 mg|5x0.005 mg|4x0.005 mg
- 保存建议：
- Lyophilized samples are stable for greater than six months at -20 degree C to -70 degree C. Reconstituted HB-VEGF-E should be stored in working aliquots at -20 degree C.
- 货期：
- 6-8周
- 纯度：
- > 90% by SDS-PAGE & silver stain
- 产品形式：
- Lyophilized
- 免责声明：
- *本产品仅供科研实验使用，不得用于临床诊断。*
- 说明书：
A DNA sequence encoding the first 116 amino acid residue of Orf virus VEGF-E isolate D1701 (Dehio et al., 1999 EMBO J. 18:363-374; GenBank accession No. AF106020) was fused with a DNA sequence encoding to the C-terminal heparin binding domain of human VEGF165. The chimeric protein was expressed in insect cells using a baculovirus expression system. Based on sequence similarity to VEGF-A, a gene encoding a VEGF homologue has recently been discovered in the genome of Orf virus (OV) (Lyttle et al., 1994 J. Virol 68:84-92). Different isolates of orf virus show significant amino acid sequence similarity to VEGF-A and described as a viral virulence factor that appear to be derived from captured host genes. All eight cysteine residues of the central cysteine knot motif characteristic of members of the VEGF family are conserved among other residues in the VEGF-E proteins (Dehio et al., 1999 EMBO J. 18:363-374; Wise et al., 1999 Proc. Natl. Acad. Sci USA 96:3071-3076). Alignment of all mammalian VEGF sequences indicated that VEGF-E is distinct from the previously described VEGFs but most closely related to VEGF-A. Like VEGF-A, VEGF-E was found to bind with high affinity to VEGF receptor-2 (KDR) resulting in receptor autophosphorylation, whilst in contrast to VEGF-A, VEGF-E and hb-VEGF-E can not bind to VEGF receptor-1 (Flt-1). Therefore VEGF-E is a potent angiogenic factor selectively binding to VEGF receptor -2/ KDR. Compared to human VEGF165 this virus form has no heparin-binding domain and seems to be a freely secreted protein comparable to VEGF121. In order to compare this form with human VEGF165, an additional heparin-binding domain was engineered at the C-terminus to allow interaction with proteo-aminoglycans and heparan sulfate. These form is also able to interact with neuropillin -1.
