Recombinant Human Replication Protein A2
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| Amount : | 10 µg |
| Purification : | Greater than 85.0% as determined by SDS-PAGE. |
| Content : | The RPA2 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl. |
| Storage condition : | RPA2 should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles. |
| AA sequence : | MGSSHHHHHH SSGLVPRGSH MGSMWNSGFE SYGSSSYGGA GGYTQSPGGF GSPAPSQAEK KSRARAQHIV PCTISQLLSA TLVDEVFRIG NVEISQVTIV GIIRHAEKAP TNIVYKIDDM TAAPMDVRQW VDTDDTSSEN TVVPPETYVK VAGHLRSFQN KKSLVAFKIM PLEDMNEFTT HILEVINAHM VLSKANSQPS AGRAPISNPG MSEAGNFGGN SFMPANGLTV AQNQVLNLIK ACPRPEGLNF QDLKNQLKHM SVSSIKQAVD FLSNEGHIYS TVDDDHFKST DAE. |
| Alternative Name : | Replication protein A 32 kDa subunit, RP-A p32, Replication factor A protein 2, RF-A protein 2, Replication protein A 34 kDa subunit, RP-A p34, RPA2, REPA2, RPA32, RPA34. |
Source : Escherichia Coli.
RPA2 Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 293 amino acids (1-270 a.a.) and having a molecular mass of 31.7kDa. The RPA2 is purified by proprietary chromatographic techniques.
Replication Protein A2 (RPA2) is a single stranded DNA binding protein. Human RPA2 is a heterotrimeric protein containing subunits of 14, 32 and 70kDa. The RPA2 protein complex is highly conserved in eukaryotes and is crucial in DNA replication, homologous recombination and nucleotide excision repair. RPA2 C-terminus specifically interacts with the DNA repair enzyme UNG2 and repair factors XPA and Rad52, each of which functions in a different repair pathway. Additionally, RPA2 binds specifically to the SH2 domain of Stat3 in vivo, and overexpression of RPA2 corresponds to the augmented growth factor-stimulated tyrosine phosphorylation and transcription activities of Stat3.
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
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