protein

Recombinant Human Replication protein A 70 kDa DNA-binding subunit

MBS967200

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Recombinant Protein

Recombinant Human Replication protein A 70 kDa DNA-binding subunit

Replication protein A 70 kDa DNA-binding subunit

Replication factor A protein 1; RF-A protein 1; Single-stranded DNA-binding protein

replication protein A 70 kDa DNA-binding subunit; Replication protein A 70 kDa DNA-binding subunit; replication protein A 70 kDa DNA-binding subunit; replication protein A1; Replication factor A protein 1; RF-A protein 1

RPA1

RPA1; RPA1; HSSB; RF-A; RP-A; REPA1; RPA70; MST075; REPA1; RPA70; RP-A p70; RF-A protein 1

RFA1_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

2-616, Full length

616

VGQLSEGAIAAIMQKGDTNIKPILQVINIRPITTGNSPP
RYRLLMSDGLNTLSSFMLATQLNPLVEEEQLSSNCVCQI
HRFIVNTLKDGRRVVILMELEVLKSAEAVGVKIGNPVPY
NEGLGQPQVAPPAPAASPAASSRPQPQNGSSGMGSTVSK
AYGASKTFGKAAGPSLSHTSGGTQSKVVPIASLTPYQSK
WTICARVTNKSQIRTWSNSRGEGKLFSLELVDESGEIRA
TAFNEQVDKFFPLIEVNKVYYFSKGTLKIANKQFTAVKN
DYEMTFNNETSVMPCEDDHHLPTVQFDFTGIDDLENKSK
DSLVDIIGICKSYEDATKITVRSNNREVAKRNIYLMDTS
GKVVTATLWGEDADKFDGSRQPVLAIKGARVSDFGGRSL
SVLSSSTIIANPDIPEAYKLRGWFDAEGQALDGVSISDL
KSGGVGGSNTNWKTLYEVKSENLGQGDKPDYFSSVATVV
YLRKENCMYQACPTQDCNKKVIDQQNGLYRCEKCDTEFP
NFKYRMILSVNIADFQENQWVTCFQESAEAILGQNAAYL
GELKDKNEQAFEEVFQNANFRSFIFRVRVKVETYNDESR
IKATVMDVKPVDYREYGRRLVMSIRRSALM

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Epigenetics and Nuclear Signaling

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

Characterization of a cDNA encoding the 70-kDa single-stranded DNA-binding subunit of human replication protein A and the role of the protein in DNA replication.Erdile L.F., Heyer W.-D., Kolodner R., Kelly T.J.J. Biol. Chem. 266:12090-12098(1991) Type I human complement C2 deficiency. A 28-base pair gene deletion causes skipping of exon 6 during RNA splicing.Erdile L.F., Heyer W.-D., Kolodner R., Kelly T.J.J. Biol. Chem. 268:2268-2268(1993) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. NIEHS SNPs program

4506583

NP_002936.1

NM_002945.3

P27694

84kD

Activation Of ATR In Response To Replication Stress Pathway (1269757); Activation Of The Pre-replicative Complex Pathway (1269773); Base Excision Repair Pathway (1270351); Cell Cycle Pathway (1269741); Cell Cycle Checkpoints Pathway (1269742); Cell Cycle, Mitotic Pathway (1269763); Cellular Response To Heat Stress Pathway (1270421); Cellular Responses To Stress Pathway (1270414); Chromosome Maintenance Pathway (1269853); DNA Damage Bypass Pathway (1270367)

RPA1: Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing. Heterotrimer composed of RPA1, RPA2 and RPA3 (canonical replication protein A complex). Component of the alternative replication protein A complex (aRPA) composed of RPA1, RPA3 and RPA4. The DNA-binding activity may reside exclusively on the RPA1 subunit. Interacts with RIPK1 and XPA. Interacts with RPA4. Interacts with the polymerase alpha subunit POLA1/p180; this interaction stabilizes the replicative complex and reduces the misincorporation rate of DNA polymerase alpha by acting as a fidelity clamp. Interact with RAD51 and SENP6 to regulate DNA repair. Interacts with HELB; this interaction promotes HELB recruitement to chromatin following DNA damage. Belongs to the replication factor A protein 1 family. Protein type: DNA-binding. Chromosomal Location of Human Ortholog: 17p13.3. Cellular Component: DNA replication factor A complex; lateral element; male germ cell nucleus; nuclear chromosome, telomeric region; nucleoplasm; nucleus; PML body. Molecular Function: chromatin binding; damaged DNA binding; metal ion binding; protein binding; single-stranded DNA binding. Biological Process: base-excision repair; bypass DNA synthesis; cellular protein metabolic process; DNA damage response, detection of DNA damage; DNA recombination; DNA repair; DNA replication; DNA strand elongation during DNA replication; DNA-dependent DNA replication; double-strand break repair; double-strand break repair via homologous recombination; error-prone postreplication DNA repair; G1/S transition of mitotic cell cycle; hemopoiesis; homeostasis of number of cells within a tissue; in utero embryonic development; meiosis; mismatch repair; mitotic cell cycle; nucleotide-excision repair; nucleotide-excision repair, DNA gap filling; nucleotide-excision repair, DNA incision; positive regulation of cell proliferation; post-translational protein modification; protein sumoylation; telomere maintenance; telomere maintenance via recombination; telomere maintenance via semi-conservative replication; transcription-coupled nucleotide-excision repair

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