Anti-RPA32/RPA2 Antibody Picoband™ (monoclonal, 3B2E9)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC, IF, ICC, FC |
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Primary Accession | P15927 |
Host | Mouse |
Isotype | Mouse IgG2a |
Reactivity | Human |
Clonality | Monoclonal |
Format | Lyophilized |
Description | Anti-RPA32/RPA2 Antibody Picoband™ (monoclonal, 3B2E9) . Tested in Flow Cytometry, IF, IHC, ICC, WB applications. This antibody reacts with Human. |
Reconstitution | Adding 0.2 ml of distilled water will yield a concentration of 500 µg/ml. |
Gene ID | 6118 |
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Other Names | 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 |
Calculated MW | 32 kDa |
Application Details | Western blot, 0.25-0.5 µg/ml, Human Immunohistochemistry(Paraffin-embedded Section), 2-5 µg/ml, Human Immunocytochemistry/Immunofluorescence, 5 µg/ml, Human Flow Cytometry, 1-3 µg/1x10^6 cells, Human |
Contents | Each vial contains 4 mg Trehalose, 0.9 mg NaCl and 0.2 mg Na2HPO4. |
Clone Names | Clone: 3B2E9 |
Immunogen | E.coli-derived human RPA32/RPA2 recombinant protein (Position: Q34-H254). |
Purification | Immunogen affinity purified. |
Storage | At -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freezing and thawing. |
Name | RPA2 |
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Synonyms | REPA2, RPA32, RPA34 |
Function | As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Also plays a role in base excision repair (BER) probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. RPA stimulates 5'-3' helicase activity of BRIP1/FANCJ (PubMed:17596542). |
Cellular Location | Nucleus. Nucleus, PML body. Note=Redistributes to discrete nuclear foci upon DNA damage in an ATR-dependent manner |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes a subunit of the heterotrimeric Replication Protein A (RPA) complex, which binds to single-stranded DNA (ssDNA), forming a nucleoprotein complex that plays an important role in DNA metabolism, being involved in DNA replication, repair, recombination, telomere maintenance, and co-ordinating the cellular response to DNA damage through activation of the ataxia telangiectasia and Rad3-related protein (ATR) kinase. The RPA complex protects single-stranded DNA from nucleases, prevents formation of secondary structures that would interfere with repair, and co-ordinates the recruitment and departure of different genome maintenance factors. The heterotrimeric complex has two different modes of ssDNA binding, a low-affinity and high-affinity mode, determined by which oligonucleotide/oligosaccharide-binding (OB) domains of the complex are utilized, and differing in the length of DNA bound. This subunit contains a single OB domain that participates in high-affinity DNA binding and also contains a winged helix domain at its carboxy terminus, which interacts with many genome maintenance protein. Post-translational modifications of the RPA complex also plays a role in co-ordinating different damage response pathways.
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