Comparison

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

Manufacturer Cusabio
Category
Type Proteins
Specific against other
Amount 100ug
Host E.coli
Item no. CSB-EP020088HU-100
Eclass 6.1 34160400
Eclass 9.0 42020190
Available
Alternative Name(s)
Replication factor A protein 1 ; RF-A protein 1Single-stranded DNA-binding protein
AA Sequence
VGQLSEGAIAAIMQKGDTNIKPILQVINIRPITTG NSPPRYRLLMSDGLNTLSSFMLATQLNPLVEEEQL SSNCVCQIHRFIVNTLKDGRRVVILMELEVLKSAE AVGVKIGNPVPYNEGLGQPQVAPPAPAASPAASSR PQPQNGSSGMGSTVSKAYGASKTFGKAAGPSLSHT SGGTQSKVVPIASLTPYQSKWTICARVTNKSQIRT WSNSRGEGKLFSLELVDESGEIRATAFNEQVDKFF PLIEVNKVYYFSKGTLKIANKQFTAVKNDYEMTFN NETSVMPCEDDHHLPTVQFDFTGIDDLENKSKDSL VDIIGICKSYEDATKITVRSNNREVAKRNIYLMDT SGKVVTATLWGEDADKFDGSRQPVLAIKGARVSDF GGRSLSVLSSSTIIANPDIPEAYKLRGWFDAEGQA LDGVSISDLKSGGVGGSNTNWKTLYEVKSENLGQG DKPDYFSSVATVVYLRKENCMYQACPTQDCNKKVI DQQNGLYRCEKCDTEFPNFKYRMILSVNIADFQEN QWVTCFQESAEAILGQNAAYLGELKDKNEQAFEEV FQNANFRSFIFRVRVKVETYNDESRIKATVMDVKP VDYREYGRRLVMSIRRSALM
Research Topic
Epigenetics and Nuclear Signaling
Uniprot ID
P27694
Gene Names
RPA1
Tag Info
N-terminal 6xHis-SUMO-tagged
Expression Region
2-616aa
MW of Fusion Proten
84
Sequence Info
Full Length
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
Reference
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)
Purity
Greater than 90% as determined by SDS-PAGE.
Storage Buffer
Tris-based buffer, 50% glycerol
Storage
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 -20C/-80C. The shelf life of lyophilized form is 12 months at -20C/-80C.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4C for up to one week.
Species
Homo sapiens (Human)
Amount: 100ug
Available: In stock
Listprice: €353.57
Price: €353.57
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