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p75-CTR [C-terminal region of p75 (LEDGF)]

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Description:

10ug His tagged recombinant p75 C terminal region was purified from a bacterial system. NM_033222. gene_synonym: DFS70; LEDGF; MGC74712; p52; p75; PAIP;PSIP2.

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P1061-01 $283.80
 

Lens epithelium-derived growth factor (LEDGF, also called as p75) has been shown to enhance survival of lens epithelial cells (LECs) against stress (1). LEDGF is a transcriptional activator. It protects the cells by binding to cis-stress response ((A/T)GGGG(T/A)), and heat shock (HSE; nGAAn) elements in the stress genes and activating their transcription (2). Originally, it was isolated as a co-activator required for transcriptional activation in human cell-free systems containing RNA polymerase II and general initiation factors (3). LEDGF is expressed at all stages of development in a variety of organs and tissues (4). A second protein product, p52, can be produced from the same gene due to alternative splicing of pre-mRNA. In vitro, p52 was found to be more general and stronger transcriptional co-activator than LEDGF/p75 (3,5). HIV-1 integrase (IN) forms a specific nuclear complex with p75 but not with p52, suggesting a role for p75’s C-terminal region in retroviral integration (6).
Recombinant His tagged p75 CTR is isolated from an E. coli strain that carries the C-terminal coding sequence of the human LEDGF/p75 (amino acid 322-530) under the control of a T7 promoter.
p75 has been applied in in vitro transcription assays, splicing assays, DNA and protein-protein interaction assays.
Purified protein is greater than 95% homogeneous based on SDS-PAGE analysis.
1 unit equals 1 nanogram of purified protein. 20-100 units are sufficient for a ligand binding assay and 100 units are sufficient for a protein-protein interaction assay.
variable in different lots
1x dilution buffer A: 20 mM Tris-Cl (pH 8.0), 20% Glycerol, 100 mM KCl, 1 mM DTT and 0.2 mM EDTA
 
References:
1. Fatma et al., (2001) J. Biol. Chem. 276, 48899-48907
2. Singh et. Al., (2001) Biochem. Biophys. Res. Commun. 283, 943-955
3. Ge et al., (1998) EMBO J. 17, 6723-6729
4. Cherapanov et al., (2003) J. Biol. Chem. 278, 372-381
5. Ge et al., (1998) Mol. Cell 2, 751-759
6. Maertens et al., (2003) J. Biol. Chem. June 9 Epub ahead of print

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