DIATHEVA - Biomanufacturing of innovative diagnostics and reagents

Recombinant Integrase

Description: Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. 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 (288 amino acids) has three domains: the catalytic core, the C-terminal, and the N-terminal domains. 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.

Product type: Recombinant protein

Expression system: E.coli

Tested by: SDS Page, Western Blotting Reacts with all DIATHEVA mouse anti HIV-1 integrase antibodies.

Purity: >95% pure estimated by SDS-PAGE (EU Ph. 5.0 § 2.5.31)


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Form: Liquid

Storage buffer: 20mM phosphate buffer pH 7.5, 1M NaCl, 10μM Zinc acetate, 1mM DTT, 0.1mM EDTA; 10%(v/v) glycerol.


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