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

Specification
Organism Homo sapiens (Human)
Expression Host E.coli
Tag Info N-terminal 6xHis-SUMO-tagged
Purity Greater than 85% by SDS-PAGE
Uniprot ID P27694
Gene Names RPA1
Alternative Names Replication factor A protein 1 ;RF-A protein 1Single-stranded DNA-binding protein
Expression Region Full Length of Mature Protein(2-616aa )
Molecular Weight 84 kDa
Protein Sequence VGQLSEGAIAAIMQKGDTNIKPILQVINIRPITTGNSPPRYRLLMSDGLNTLSSFMLATQLNPLVEEEQLSSNCVCQIHRFIVNTLKDGRRVVILMELEVLKSAEAVGVKIGNPVPYNEGLGQPQVAPPAPAASPAASSRPQPQNGSSGMGSTVSKAYGASKTFGKAAGPSLSHTSGGTQSKVVPIASLTPYQSKWTICARVTNKSQIRTWSNSRGEGKLFSLELVDESGEIRATAFNEQVDKFFPLIEVNKVYYFSKGTLKIANKQFTAVKNDYEMTFNNETSVMPCEDDHHLPTVQFDFTGIDDLENKSKDSLVDIIGICKSYEDATKITVRSNNREVAKRNIYLMDTSGKVVTATLWGEDADKFDGSRQPVLAIKGARVSDFGGRSLSVLSSSTIIANPDIPEAYKLRGWFDAEGQALDGVSISDLKSGGVGGSNTNWKTLYEVKSENLGQGDKPDYFSSVATVVYLRKENCMYQACPTQDCNKKVIDQQNGLYRCEKCDTEFPNFKYRMILSVNIADFQENQWVTCFQESAEAILGQNAAYLGELKDKNEQAFEEVFQNANFRSFIFRVRVKVETYNDESRIKATVMDVKPVDYREYGRRLVMSIRRSALM
Form Liquid or Lyophilization
Buffer The default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol if the delivery form is liquid. The lyophilization buffer is Tris/PBS-based buffer, 6% Trehalose, pH 8.0 if the delivery form is lyophilized powder. Please contact us if you have any special requirment.
Reconstitution Please reconstitute protein in deionized sterile water and we recommend that briefly centrifuge thevial prior to opening the vial .We recommend aliquot for long-term storage at -20℃/-80℃.
Background
Relevance 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 . Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. 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
Involvement in Disease
Subcellular Location Nucleus, Nucleus, PML body
Protein Families Replication factor A protein 1 family
Tissue Specificity RPA1
QC Data
Note Please contact us for QC Data
Product Image (Reference Only) Product via image
$202.00
In stock
SKU
EB-PE8HU20213

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

Question / Bulk Inquiry
Please leave us a message if you have any questions or have bulk order inquiry, we will get back to you in 24 hours.
Please type the letters and numbers below

 

Reviews

Write Your Own Review
You're reviewing:Recombinant Human Replication protein A 70kDa DNA-binding subunit(RPA1)
Copyright © 2021-present Echo Biosystems. All rights reserved.