In Western blot against the HPV16-E7 bacterially derived fusion protein, the antibody detects a 52 kD band which is composed of the HPV16-E7 protein (15 kDa) and the trpE protein (37 kDa). Positive reactivity for the 15 kDa HPV16-E7 expressed protein was shown with CaSki (HPV16 DNA-containing cell line) cells by Western blot. The antibody has also been shown to immunoprecipitate and immunocytochemically stain the HPV16-E7 expressed protein from the CaSki cell line. Negative reactivity by Western blot was shown with a series of other HPV fusion proteins including: HPV16-E2, HPV16-E4, HPV16-E6, HPV18-E7, HPV6-E7, HPV6-E4, and HPV6-L1. The antibody failed to react with HeLa (HPV18 DNA-containing cell line) cells and other HPV DNA negative cervical carcinoma cell lines, HT-3 and C-33A, by Western blot, by immunoprecipitation or by immunocytochemical staining analyses.
Reconstitute the lyophilized material with 1 mL of deionized or distilled water for a final concentration of 50 µg/mL.
The HPV E7 proteins are small (HPV16 E7 comprising 98 amino acids, 15kDa), zinc binding phosphoproteins which are localised in the nucleus. They are structurally and functionally similar to the E1A protein of subgenus C adenoviruses. The first 16 amino-terminal amino acids of HPV16 E7 contain a region homologous to a segment of the conserved region 1 (CR1) of the E1A protein of subgenus C adenoviruses. The next domain, up to amino acid 37, is homologous to the entire region 2 (CR2) of E1A. Genetic studies have established that these domains are required for cell transformation in vitro, suggesting similarities in the mechanism of transformation by these viruses. The CR2 homology region contains the LXCXE motif (residues 22-26) involved in binding to the tumour suppressor protein pRb.
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Protein Aliases: HPV 16-E7; HPV16E7; human papillomavirus