Recombinant Human Replication protein A 70 kDa DNA-binding subunit (RPA1)

Code CSB-YP020088HU
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Source Yeast
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Code CSB-EP020088HU-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-BP020088HU
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Source Baculovirus
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Code CSB-MP020088HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
RPA1
Uniprot No.
Alternative Names
Dmrpa1; Drosophila Replication Protein A; DRPA; HSSB; Human single stranded DNA binding protein ; MST075; MSTP075; p70; REPA1; Replication factor A; Replication factor A protein 1; Replication protein A 70 kDa DNA-binding subunit; Replication protein A 70kDa DNA binding subunit; Replication protein A1 70kDa; Replication protein A1; RF A; RF-A protein 1; RFA; RFA1_HUMAN; RP A; RP-A p70; RPA 70; RPA; rpa1; Single stranded binding protein 70; Single-stranded DNA-binding protein
Species
Homo sapiens (Human)
Expression Region
2-616
Target Protein Sequence
VGQLSEGAIAAIMQKGDTNIKPILQVINIRPITTGNSPPRYRLLMSDGLNTLSSFMLATQLNPLVEEEQLSSNCVCQIHRFIVNTLKDGRRVVILMELEVLKSAEAVGVKIGNPVPYNEGLGQPQVAPPAPAASPAASSRPQPQNGSSGMGSTVSKAYGASKTFGKAAGPSLSHTSGGTQSKVVPIASLTPYQSKWTICARVTNKSQIRTWSNSRGEGKLFSLELVDESGEIRATAFNEQVDKFFPLIEVNKVYYFSKGTLKIANKQFTAVKNDYEMTFNNETSVMPCEDDHHLPTVQFDFTGIDDLENKSKDSLVDIIGICKSYEDATKITVRSNNREVAKRNIYLMDTSGKVVTATLWGEDADKFDGSRQPVLAIKGARVSDFGGRSLSVLSSSTIIANPDIPEAYKLRGWFDAEGQALDGVSISDLKSGGVGGSNTNWKTLYEVKSENLGQGDKPDYFSSVATVVYLRKENCMYQACPTQDCNKKVIDQQNGLYRCEKCDTEFPNFKYRMILSVNIADFQENQWVTCFQESAEAILGQNAAYLGELKDKNEQAFEEVFQNANFRSFIFRVRVKVETYNDESRIKATVMDVKPVDYREYGRRLVMSIRRSALM
Protein Length
Full Length of Mature 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.

Customer Reviews and Q&A

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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. As part of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2-containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA synthesis by polymerase delta in presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange.
Gene References into Functions
  1. RPA serves to stimulate the primase activity of PrimPol. PMID: 28534480
  2. These new findings supports the existence of a functional PrimPol/RPA association that allows repriming at the exposed ssDNA regions formed in the leading strand upon replicase stalling. PMID: 28396594
  3. regulatory pathway based on casein kinase 2-G9a-RPA permits homologous recombination in cancer cells PMID: 28698370
  4. RPA1 serves as an oncogene during gastrointestinal cancers progression PMID: 29601890
  5. RPA1 is significantly up-regulated in hepatocellular carcinoma and correlates with poor prognosis. RPA1 influences cell cycle through CDK4/Cyclin-D pathway. PMID: 29477843
  6. PCAF/GCN5-mediated lysine 163 acetylation of RPA1 is crucial for nucleotide excision repair. PMID: 28854354
  7. the acetylation status of RPA1 played a crucial role in repair of DNA damage via nucleotide excision repair. PMID: 28854355
  8. data obtained allow us to suggest that XPA can be involved in the post-incision NER stages via its interaction with RPA PMID: 29320546
  9. The results suggest that RPA phosphorylation enhances the recruitment of PRP19 to RPA-ssDNA and stimulates RPA ubiquitylation through a process requiring both PRP19 and RFWD3, thereby triggering a phosphorylation-ubiquitylation circuitry that promotes ATR activation and homologous recombination. PMID: 28666352
  10. RPA recruits HIRA to promoters and enhancers and regulates deposition of newly synthesized H3.3 to these regulatory elements for gene regulation. PMID: 28107649
  11. RPA is a sensor of R loops and a regulator of RNaseH1, extending the versatile role of RPA in suppression of genomic instability. PMID: 28257700
  12. Results suggest that the UNG2 N-terminus may serve as a flexible scaffold to tether PCNA and RPA at the replication fork, and that post-translational modifications on the UNG2 N-terminus disrupt formation of the PCNA-UNG2-RPA protein complex. PMID: 28746850
  13. Data suggest that, during human DNA replication, restricting PCNA (proliferating cell nuclear antigen) to the vicinity of its DNA target site is important; PCNA can be maintained at or near primer/template junctions during DNA synthesis by RPA (replication protein A) or SSB (single-stranded DNA-binding protein); here, the SSB used was from Escherichia coli. PMID: 28590137
  14. Strikingly, the addition of the single-stranded DNA (ssDNA)-binding replication protein A (RPA) selectively restores XPF-ERCC1 endonuclease activity on this structure. The 5'-3' exonuclease SNM1A can load from the XPF-ERCC1-RPA-induced incisions and digest past the crosslink to quantitatively complete the unhooking reaction. PMID: 28607004
  15. RPA deficiency induces activation of the Fanconi anemia pathway in an ATR-dependent manner, which may play a role in the genome maintenance. PMID: 27398742
  16. Force regulated dynamics of RPA1 on a DNA fork during DNA replication has been reported. PMID: 27016742
  17. By monitoring DNA double-strand breaks mis-repair using a sensitive bioassay, it was found that depletion of homologous recombination proteins, including BRCA2, BRCA1 or RPA1, resulted in a distinct mutational signature associated with significant increases in break-induced mutation frequencies. PMID: 27131361
  18. results reveal that ETAA1 is a novel RPA-interacting protein that promotes restart of stalled replication forks. PMID: 27601467
  19. miR-30a targets the DNA replication protein RPA1, hinders the replication of DNA and induces DNA fragmentation. PMID: 27208176
  20. show that RPA can bind on each side of the G-quadruplex but it unwinds the G4 only from 5' toward 3'. PMID: 27440048
  21. Replication protein A binds tightly to the single-stranded DNA adjacent to a blocked primer/template junction and restricts PCNA to the upstream duplex region by physically blocking diffusion of PCNA along ssDNA. PMID: 28177605
  22. CTF18 forms a complex with RPA when replication stress is elicited by hydroxyurea treatment or UV exposure during S phase. The interaction kinetics between CTF18 and RPA is positively associated with the phosphorylation status of Chk1. PMID: 27175616
  23. ATRIP deacetylation by SIRT2 promotes ATR-ATRIP binding to replication protein A-single-stranded DNA to drive ATR activation and thus facilitate recovery from replication stress. PMID: 26854234
  24. radiation induced the excessive expression RPA1 in TE-1 cells, and the radiosensitivity of TE-1R cells was less than that of TE-1 cells PMID: 26824734
  25. Our study predicted that UBC and RPA had potential as target genes for the diagnosis and treatment of osteosarcoma PMID: 26782416
  26. FAN1 efficiently promoted DNA incision at the proper site of RPA-coated 5'-flapped DNA. Therefore, FAN1 possesses the ability to promote the ICL repair of 5'-flapped DNA covered by RPA. PMID: 25922199
  27. a significant increase in DKC1, RAD50, MRE11 and RPA1 expression in MM cases with high bone marrow infiltration (pPMID: 26366868
  28. Here, we introduce a number of key characteristics and concepts, including the modularity of the proteins, linkage of weak binding sites, direct competition between sites, and allostery, using the protein replication protein A (RPA). [review] PMID: 25542993
  29. RFWD3-dependent ubiquitination of RPA regulates repair at stalled replication forks. PMID: 26474068
  30. RPA70 is an intrinsically highly dynamic single-stranded DNA-binding complex during both replication and distinct steps of nucleotide excision repair. PMID: 25453469
  31. by targeting RPA and mimicking DNA, DSS1 functions with BRCA2 in a two-component homologous recombination mediator complex in genome maintenance and tumor suppression PMID: 26145171
  32. The D228Y mutation in human RPA1 affects its DNA-binding activity to telomeric DNA. PMID: 26041456
  33. RPA plays an important maintaining genome integrity. [Review] PMID: 25400143
  34. RPA by itself does not affect pol eta dependent lesion bypass fidelity when copying either 8-oxoG or T-T CPD lesions. PMID: 24824831
  35. Both human RPA and hepatitis C virus NS5A(S25-C447), but not NS5A(S25-K215), enabled the NS5BDelta21-NS3 helicase complex to be stably associated with the template and synthesize RNA product in a highly processive manner in vitro. PMID: 25320291
  36. In addition to its annealing helicase activity, which eliminates the natural binding substrate for RPA, HARP blocks the phosphorylation of RPA by DNA-PK. PMID: 24565939
  37. Fanconi anemia group J (FANCJ) helicase partners with the single-stranded DNA-binding protein replication protein A (RPA) to displace BamHI-E111A bound to duplex DNA in a specific manner. PMID: 24895130
  38. LT prevents recruitment of RPA to nuclear foci after DNA damage. This leads to failure to recruit repair proteins such as Rad51 or Rad9, explaining why LT prevents repair of double strand DNA breaks by homologous recombination. PMID: 24204272
  39. these results suggest that the PSO4 complex functionally interacts with RPA and plays an important role in the DNA damage response. PMID: 24443570
  40. the current understanding of RPA's roles in replication by reviewing the available structural data, DNA-binding properties, interactions with various replication proteins, and interactions with DNA repair proteins when DNA replication is stalled. PMID: 22918586
  41. ATR-mediated suppression of dormant origins shields active forks against irreversible breakage via preventing exhaustion of nuclear RPA. This study elucidates how replicating genomes avoid destabilizing DNA damage. PMID: 24267891
  42. Data suggest that replication protein A (RPA) brings a complex of SMARCAL1 and WRN to stalled forks, but that they may act in different pathways to promote fork repair and restart. PMID: 23671665
  43. Results reveal a mechanism for the crosstalk between HR repair and NHEJ through the co-regulation of p53-RPA interaction by DNA-PK, ATM and ATR. PMID: 22797063
  44. RPA is a cofactor of the BLM-Topo IIIalpha-RMI1-RMI2 complex in double holliday junction dissolution PMID: 23543748
  45. Depletion of RPA1 abolishes HSF1 access to the promoter of HSP70 in unstressed condition and delays its rapid activation in response to heat shock. PMID: 22940245
  46. In vitro analysis of the role of replication protein A (RPA) and RPA phosphorylation in ATR-mediated checkpoint signaling. PMID: 22948311
  47. The radiosensitizing effect of DPYD depletion plus CPT was the additive effect of DPYD depletion and CPT. PMID: 22510597
  48. Replication stress-induced recruitment of HDHB to chromatin is independent of checkpoint signaling but correlates with the level of replication protein A (RPA) recruited to chromatin. PMID: 22194613
  49. cells require different RPA functions in DNA replication and DNA repair. PMID: 22179778
  50. Study propose that RPA plays a role in the protection of the human genome cell from A3G and other deaminases when they are inadvertently diverged from their natural targets. PMID: 21935481

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Subcellular Location
Nucleus. Nucleus, PML body.
Protein Families
Replication factor A protein 1 family
Database Links

HGNC: 10289

OMIM: 179835

KEGG: hsa:6117

STRING: 9606.ENSP00000254719

UniGene: Hs.461925

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