Recombinant Human Replication protein A 32 kDa subunit (RPA2)

Code CSB-YP020089HU
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Source Yeast
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Code CSB-EP020089HU
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Source E.coli
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Code CSB-EP020089HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP020089HU
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Source Baculovirus
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Code CSB-MP020089HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
RPA2
Uniprot No.
Alternative Names
60S acidic ribosomal protein P1; AA409079; AI325195; AU020965; ik:tdsubc_2g1; M(2)21C; MGC137236; OTTHUMP00000004008 ; p32; p34; RCJMB04_6d17 replication protein A2; 32kDa ; REPA2; Replication factor A protein 2; Replication protein A 32 kDa subunit; Replication protein A 32kDa subunit; Replication protein A 34 kDa subunit; Replication protein A; Replication Protein A2 (32kDa); Replication protein A2; Replication protein A2; 32kDa ; RF-A protein 2; Rf-A2; RFA; RFA2_HUMAN; RP-A p32; RP-A p34; RP21C; RPA 2; RPA 32; RPA; Rpa2; RPA32 ; RPA34; RpLP1; RpP2; xx:tdsubc_2g1; zgc:109822
Species
Homo sapiens (Human)
Expression Region
1-270
Target Protein Sequence
MWNSGFESYG SSSYGGAGGY TQSPGGFGSP APSQAEKKSR ARAQHIVPCT ISQLLSATLV DEVFRIGNVE ISQVTIVGII RHAEKAPTNI VYKIDDMTAA PMDVRQWVDT DDTSSENTVV PPETYVKVAG HLRSFQNKKS LVAFKIMPLE DMNEFTTHIL EVINAHMVLS KANSQPSAGR APISNPGMSE AGNFGGNSFM PANGLTVAQN QVLNLIKACP RPEGLNFQDL KNQLKHMSVS SIKQAVDFLS NEGHIYSTVD DDHFKSTDAE
Protein Length
Full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

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. Plays also 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.
Gene References into Functions
  1. RPA, best known for its role in DNA replication and repair, recruits HIRA to promoters and enhancers and regulates deposition of newly synthesized H3.3 to these regulatory elements for gene regulation. PMID: 28107649
  2. Single point mutations in the RPA32 subunit of RPA that abolish interaction with RFWD3 also inhibit interstrand crossling repair, demonstrating that RPA-mediated RFWD3 recruitment to stalled replication forks is important for ICL repair. PMID: 28575657
  3. The authors show that Vpr can form a trimolecular complex with UNG2 and RPA32 and the positive effect of UNG2 and RPA32 on the reverse transcription process leading to optimal virus replication and dissemination between the primary target cells of HIV-1. PMID: 27068393
  4. RPA32 phosphorylation regulates replication arrest, recombination, late origin firing, and mitotic catastrophe PMID: 24819595
  5. Expression of mutant RPA2 or loss of PALB2 expression led to significant DNA damage after replication stress, a defect accentuated by poly-ADP (adenosine diphosphate) ribose polymerase inhibitors. PMID: 25113031
  6. Conserved motifs are required for RPA32 binding the the N-terminus of SMARCAL1. PMID: 24910198
  7. study reports the characterization of the RPA32C-SMARCAL1 interface at the molecular level; implications of results are discussed with respect to the recruitment of SMARCAL1 and other DNA damage response and repair proteins to stalled replication forks PMID: 24730652
  8. study concludes RPA2 expression is translationally regulated via internal ribosome entry site and by eIF3a and that this regulation is partly accountable for cellular response to DNA damage and survival. PMID: 23393223
  9. this study has explored the role of RPA32 phosphorylation at CDK and ATR sites and propose that phosphorylation of the RPA32 subunit is dispensable for checkpoint activation induced by replication stress with aphidicolin. PMID: 23047005
  10. 4E-BP3 regulates eIF4E-mediated nuclear mRNA export and interacts with replication protein A2 PMID: 22684010
  11. Data show that the R88C variant impairs binding of the R88C variant impairs binding of uracil-DNA glycosylase UNG2 to replication protein A RPA2. PMID: 22521144
  12. Replication protein A1, replication protein A2, and cyclins D2 and D3 seem to have a parallel role in the promotion of cell cycle in astrocytic tumors being implicated in the malignant progression of these neoplasms. PMID: 21496876
  13. RPA2 up-regulation may be involved in the growth and/or survival of BRCA1 tumor cells and useful in immunohistochemical discrimination of triple-negative BRCA1 tumors. PMID: 21137066
  14. At the subunit level, 13 proteins out of 30 examined may interact with RPA2. PMID: 20679368
  15. data suggest that RPA2 hyperphosphorylation plays a critical role in maintenance of genomic stability and cell survival after a DNA replication block via promotion of homologus recombination PMID: 20130019
  16. Data suggest that PP4-mediated dephosphorylation of RPA2 is necessary for an efficient DNA-damage response. PMID: 20154705
  17. RPA32, critical for cell proliferation and maintenance of genome stability, are markedly down-regulated, Data hypothesized that their DNA-related functions could be partially limited in TRAIL-resistant HL-60 cells. PMID: 19834905
  18. Phosphorylation of the RPA2 subunit is observed after exposure of cells to ionizing radiation (IR) and other DNA-damaging agents, which implicates the modified protein in the regulation of DNA replication after DNA damage or in DNA repair. PMID: 11731442
  19. RPA2 binds to menin and has a role in multiple endocrine neoplasia PMID: 12509449
  20. C-terminal domain of hRPA32 subunit (RPA32C) facilitates initiation of SV40 replication. PMID: 15793585
  21. in response to UV-induced DNA damage, ATR rapidly phosphorylates RPA2, disrupting its association with replication centers in the S-phase and contributing to the inhibition of DNA replication PMID: 17035231
  22. Determination at single-nucleotide resolution the relative positions of the single-stranded DNA with interacting intrinsic tryptophans of RPA32. PMID: 17583916
  23. RPA phosphorylation facilitates chromosomal DNA repair. PMID: 17928296
  24. RPA32 is extensively phosphorylated after the induction of EBV lytic replication. Rad51 and RPA32 are necessary for the completion of EBV lytic infection. PMID: 19386720
  25. The N-terminus of RPA1 and phosphorylation of RPA2 regulate RPA interactions with the MRE11-RAD50-NBS1 (MRN) complex and are important in the response to DNA damage. PMID: 19586055
  26. mitotic phosphorylation of RPA2 starts at the onset of mitosis, and dephosphorylation occurs during late cytokinesis. PMID: 19671522

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Subcellular Location
Nucleus. Nucleus, PML body.
Protein Families
Replication factor A protein 2 family
Database Links

HGNC: 10290

OMIM: 179836

KEGG: hsa:6118

STRING: 9606.ENSP00000363021

UniGene: Hs.79411

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