Recombinant Human Replication Protein A 32 Kda Subunit (RPA2) Protein (GST)

Name: Recombinant Human Replication Protein A 32 Kda Subunit (RPA2) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-04617P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Replication Protein A 32 Kda Subunit (RPA2) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P15927
Target Symbol	RPA2
Synonyms	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 System	E.coli
Tag	N-GST
Target Protein Sequence	MWNSGFESYGSSSYGGAGGYTQSPGGFGSPAPSQAEKKSRARAQHIVPCTISQLLSATLVDEVFRIGNVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAAPMDVRQWVDTDDTSSENTVVPPETYVKVAGHLRSFQNKKSLVAFKIMPLEDMNEFTTHILEVINAHMVLSKANSQPSAGRAPISNPGMSEAGNFGGNSFMPANGLTVAQNQVLNLIKACPRPEGLNFQDLKNQLKHMSVSSIKQAVDFLSNEGHIYSTVDDDHFKST
Expression Range	1-267aa
Protein Length	Partial
Mol. Weight	55.9kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location	Nucleus. Nucleus, PML body.
Protein Families	Replication factor A protein 2 family
Database References	HGNC: 10290 OMIM: 179836 KEGG: hsa:6118 STRING: 9606.ENSP00000363021 UniGene: 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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.