Product Details

Purity

Greater than 90% as determined by SDS-PAGE.

Target Names

RPA2

Uniprot No.

P15927

Research Area

Epigenetics and Nuclear Signaling

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)

Source

E.coli

Expression Region

1-267aa

Target Protein Sequence

MWNSGFESYGSSSYGGAGGYTQSPGGFGSPAPSQAEKKSRARAQHIVPCTISQLLSATLVDEVFRIGNVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAAPMDVRQWVDTDDTSSENTVVPPETYVKVAGHLRSFQNKKSLVAFKIMPLEDMNEFTTHILEVINAHMVLSKANSQPSAGRAPISNPGMSEAGNFGGNSFMPANGLTVAQNQVLNLIKACPRPEGLNFQDLKNQLKHMSVSSIKQAVDFLSNEGHIYSTVDDDHFKST
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Mol. Weight

55.9kDa

Protein Length

Partial

Tag Info

N-terminal GST-tagged

Form

Liquid or 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

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.

Troubleshooting and FAQs

Protein 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

3-7 business days

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Description

This high-quality Recombinant Human RPA2 protein is an essential component for research in epigenetics and nuclear signaling. RPA2, also known as Replication protein A 32 kDa subunit (RP-A p32), is a vital subunit of the heterotrimeric Replication protein A complex, which plays a key role in DNA replication, repair, and recombination processes.

Our Recombinant Human RPA2 protein is expressed in E.coli, ensuring a partial protein length (1-267aa) that retains functionality. The N-terminal GST-tag facilitates efficient purification, while maintaining the protein's integrity and activity. With a purity greater than 90% as determined by SDS-PAGE, our RPA2 protein guarantees reliable and reproducible results in your research projects. Available in both liquid and lyophilized powder forms, our Recombinant Human RPA2 protein is poised to support your scientific discoveries.

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

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
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
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
RPA32 phosphorylation regulates replication arrest, recombination, late origin firing, and mitotic catastrophe PMID: 24819595
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
Conserved motifs are required for RPA32 binding the the N-terminus of SMARCAL1. PMID: 24910198
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
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
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
4E-BP3 regulates eIF4E-mediated nuclear mRNA export and interacts with replication protein A2 PMID: 22684010
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
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
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
At the subunit level, 13 proteins out of 30 examined may interact with RPA2. PMID: 20679368
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
Data suggest that PP4-mediated dephosphorylation of RPA2 is necessary for an efficient DNA-damage response. PMID: 20154705
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
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
RPA2 binds to menin and has a role in multiple endocrine neoplasia PMID: 12509449
C-terminal domain of hRPA32 subunit (RPA32C) facilitates initiation of SV40 replication. PMID: 15793585
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
Determination at single-nucleotide resolution the relative positions of the single-stranded DNA with interacting intrinsic tryptophans of RPA32. PMID: 17583916
RPA phosphorylation facilitates chromosomal DNA repair. PMID: 17928296
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
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
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

Code	CSB-EP020089HU1
Abbreviation	Recombinant Human RPA2 protein, partial
MSDS	MSDS Datasheet
Size	$224
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Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Recombinant Human Replication protein A 32 kDa subunit (RPA2), partial

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