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SDS-Page (3ug by SDS-PAGE under reducing condition and visualized by coomassie blue stain.)

RPA2 recombinant protein

RPA2, 1-270aa, Human, His tag, E Coli

Gene Names
RPA2; REPA2; RPA32; RP-A p32; RP-A p34
Applications
SDS-Page
Purity
> 90% by SDS-PAGE
Synonyms
RPA2; 1-270aa; Human; His tag; E Coli; Replication protein A 32 kDa subunit; REPA2; RPA32; RP-A p32; RP-A p34; RPA2 recombinant protein
Ordering
For Research Use Only!
Host
E Coli
Purity/Purification
> 90% by SDS-PAGE
Form/Format
Liquid in 20mM Tris-HCl Buffer (pH 8.0) containing 20% glycerol, 2mM DTT, 0.1M NaCl.
Concentration
0.5 mg/ml (determined by Bradford assay) (varies by lot)
Sequence
< MGSSHHHHHH SSGLVPRGSH MGSMWNSGFE SYGSSSYGGA GGYTQSPGGF GSPAPSQAEK KSRARAQHIV PCTISQLLSA TLVDEVFRIG NVEISQVTIV GIIRHAEKAP TNIVYKIDDM TAAPMDVRQW VDTDDTSSEN TVVPPETYVK VAGHLRSFQN KKSLVAFKIM PLEDMNEFTT HILEVINAHM VLSKANSQPS AGRAPISNPG MSEAGNFGGN SFMPANGLTV AQNQVLNLIK ACPRPEGLNF QDLKNQLKHM SVSSIKQAVD FLSNEGHIYS TVDDDHFKST DAE
Sequence Length
270
Applicable Applications for RPA2 recombinant protein
SDS-PAGE
Antigen Species
Human
Tag
His-tag
Domain
1-270aa
Preparation and Storage
Can be stored at +2°C to +8°C for 1 week.
For long term storage, aliquot and store at -20°C or -80°C.
Avoid repeated freezing and thawing cycles.

SDS-Page

(3ug by SDS-PAGE under reducing condition and visualized by coomassie blue stain.)

SDS-Page (3ug by SDS-PAGE under reducing condition and visualized by coomassie blue stain.)
Related Product Information for RPA2 recombinant protein
Replication Protein A (RPA) is a single stranded DNA binding protein. Human RPA is a heterotrimeric protein containing subunits of 14, 32 and 70kDa. This protein complex is highly conserved in eukaryotes and is essential in DNA replication, homologous recombination and nucleotide excision repair. The C-terminus of RPA2 can specfically intereact with the DNA repair enzyme uNG2 and repair factors XPA and Rad52, each of which functions in a different repair pathway. In addition, this protein binds specifically to the SH2 domain of Stat3 in vivo, and overexpression of RPA2 corresponds to the augmented growth factor-stimulated tyrosine phosphorylation and transcription activities of Stat3. Recombinant human RPA2 protein, fused to His-tag at N-terminus, was expressed in E Coli and purified by using conventional chromatography techniques.
Product Categories/Family for RPA2 recombinant protein
References
Wang M., et al. (2000) Biochemistry. 39 (21):6433-9. ; Mer G., et al. (2000) Cell. 103 (3):449-56.;

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
31.7 kDa (293aa) confirmed by MALDI-TOF
NCBI Official Full Name
replication protein A 32 kDa subunit isoform 1
NCBI Official Synonym Full Names
replication protein A2
NCBI Official Symbol
RPA2
NCBI Official Synonym Symbols
REPA2; RPA32; RP-A p32; RP-A p34
NCBI Protein Information
replication protein A 32 kDa subunit
UniProt Protein Name
Replication protein A 32 kDa subunit
Protein Family
UniProt Gene Name
RPA2
UniProt Synonym Gene Names
REPA2; RPA32; RPA34; RP-A p32; RF-A protein 2; RP-A p34

NCBI Description

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. [provided by RefSeq, Sep 2017]

Uniprot Description

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.

Research Articles on RPA2

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Product Notes

The RPA2 rpa2 (Catalog #AAA203846) is a Recombinant Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. AAA Biotech's RPA2 can be used in a range of immunoassay formats including, but not limited to, SDS-PAGE. Researchers should empirically determine the suitability of the RPA2 rpa2 for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. The amino acid sequence is listed below: < MGSSHHHHHH SSGLVPRGSH MGSMWNSGFE SYGSSSYGGA GGYTQSPGGF GSPAPSQAEK KSRARAQHIV PCTISQLLSA TLVDEVFRIG NVEISQVTIV GIIRHAEKAP TNIVYKIDDM TAAPMDVRQW VDTDDTSSEN TVVPPETYVK VAGHLRSFQN KKSLVAFKIM PLEDMNEFTT HILEVINAHM VLSKANSQPS AGRAPISNPG MSEAGNFGGN SFMPANGLTV AQNQVLNLIK ACPRPEGLNF QDLKNQLKHM SVSSIKQAVD FLSNEGHIYS TVDDDHFKST DAE. It is sometimes possible for the material contained within the vial of "RPA2, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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