HIV integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. It is one of three enzymes of HIV, the others being the Reverse Transcriptase and the Protease. The enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The full length HIV-1 integrase (288aa) has three domains: the N-terminal domain has a His2Cys2 motif which chelates zinc, the core domain has the catalytic DDE motif which is required for its enzymatic activity, and the C-terminal domain has an SH3-like fold which binds DNA nonspecifically. Although all three domains are required for integration, it is thought that the catalytic core domain contains the active site responsible for catalysis of all the reactions of integration/disintegration. The C-terminal domain confers the capacity to bind both viral and host DNA. The structure and function of the N-terminal domain are presently unknown, but it contains a His2Cys2 zinc binding motif, suggesting a possible interaction with nucleic acid. HIV integrase is a 32kD protein produced from the C-terminal portion of the Pol gene product, and is an attractive target for anti-HIV drugs.
Source:Recombinant protein corresponding to Immunodeficiency Virus Integrase (Pol) Protein, fused to GST-Tag at N-terminal, expressed in E. coli.
Applications:Suitable for use in Western Blot and ELISA. Other applications not tested.
Recommended Dilution:Optimal dilutions to be determined by the researcher.
Storage and Stability:Aliquot to avoid repeated freezing and thawing and store at -70°C. Aliquots are stable for 6 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
仕様
Size:100ug
Source Antigen:Recombinant, E. coli
Grade:Highly Purified
Purity:≥95% (SDS-PAGE and method of Bradford et al)
Form:Supplied as a liquid in 25mM Tris-HCl, pH 8.0, 0.2% Tween-20, 1.5M urea, 50% glycerol.