RPA 32 kDa subunit Antibody (G-3): sc-166886

RPA 32 kDa subunit Antibody (G-3) is a mouse monoclonal IgG1 antibody that detects RPA 32 kDa subunit in mouse, rat, and human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). RPA 32 kDa subunit is a critical component of the heterotrimeric replication protein A complex, which serves as a single-stranded DNA-binding protein essential for DNA replication, repair, and recombination processes. RPA 32 kDa subunit′s ability to bind to single-stranded DNA is crucial for maintaining genomic stability, as RPA 32 kDa subunit facilitates the recruitment of various repair factors to sites of DNA damage. Notably, the C-terminus of RPA 32 kDa subunit specifically interacts with the DNA repair enzyme uracil-DNA glycosylase 2 (UNG2) and repair factors such as XPA and Rad52, each of which plays a distinct role in different DNA repair pathways. This interaction underscores RPA 32 kDa subunit′s importance in orchestrating the cellular response to DNA damage, thereby preventing mutations and maintaining cellular integrity. Additionally, RPA 32 kDa subunit′s binding to the SH2 domain of Stat3 highlights RPA 32 kDa subunit′s involvement in signaling pathways that regulate cell growth and survival, making RPA 32 kDa subunit a significant player in both DNA repair and cellular signaling.

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RPA 32 kDa subunit Antibody (G-3) References:

1. The phosphorylation domain of the 32-kDa subunit of replication protein A (RPA) modulates RPA-DNA interactions. Evidence for an intersubunit interaction.  |  Binz, SK., et al. 2003. J Biol Chem. 278: 35584-91. PMID: 12819197
2. Heparin-binding properties of vitronectin are linked to complex formation as illustrated by in vitro polymerization and binding to the terminal complement complex.  |  Høgåsen, K., et al. 1992. J Biol Chem. 267: 23076-82. PMID: 1385412
3. A mechanism for assembly of complexes of vitronectin and plasminogen activator inhibitor-1 from sedimentation velocity analysis.  |  Minor, KH., et al. 2005. J Biol Chem. 280: 28711-20. PMID: 15905170
4. The presence of methionine or threonine at position 381 in vitronectin is correlated with proteolytic cleavage at arginine 379.  |  Tollefsen, DM., et al. 1990. J Biol Chem. 265: 9778-81. PMID: 1693616
5. The phosphorylation of the two-chain form of vitronectin by protein kinase A is heparin dependent.  |  Chain, D., et al. 1990. FEBS Lett. 269: 221-5. PMID: 1696913
6. Endogenous cleavage of the Arg-379-Ala-380 bond in vitronectin results in a distinct conformational change which 'buries' Ser-378, its site of phosphorylation by protein kinase A.  |  Chain, D., et al. 1991. Biochem J. 274 (Pt 2): 387-94. PMID: 1706595
7. The 32 kDa subunit of replication protein A (RPA) participates in the DNA replication of Mung bean yellow mosaic India virus (MYMIV) by interacting with the viral Rep protein.  |  Singh, DK., et al. 2007. Nucleic Acids Res. 35: 755-70. PMID: 17182628
8. Impact of vitronectin concentration and surface properties on the stable propagation of human embryonic stem cells.  |  Li, J., et al. 2010. Biointerphases. 5: FA132-42. PMID: 21171706
9. Evaluation of Vitronectin Expression in Prostate Cancer and the Clinical Significance of the Association of Vitronectin Expression with Prostate Specific Antigen in Detecting Prostate Cancer.  |  Niu, Y., et al. 2016. Urol J. 13: 2527-32. PMID: 26945657
10. Electron microscopic immunohistochemistry of ocular and extraocular pseudoexfoliative material.  |  Amari, F., et al. 1997. Exp Eye Res. 65: 51-6. PMID: 9237864

The preferred RPA 32 kDa subunit antibody is RPA 32 kDa subunit Antibody (9H8): sc-56770.