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AB82204

重组人BRCA1蛋白

Recombinant Human BRCA1 protein

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(2 Publications)

Recombinant Human BRCA1 protein is a Human Full Length protein, in the 1 to 1863 aa range, expressed in Baculovirus infected insect cells, with >95%, suitable for SDS-PAGE.

查看别名

RNF53, BRCA1, Breast cancer type 1 susceptibility protein, RING finger protein 53, RING-type E3 ubiquitin transferase BRCA1

1 Images
SDS-PAGE - Recombinant Human BRCA1 protein (AB82204)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human BRCA1 protein (AB82204)

SDS-PAGE analysis of ab82204.

关键信息

纯度

>95% SDS-PAGE

表达系统

Baculovirus infected insect cells

标签

6x His tag C-Terminus

应用

SDS-PAGE

applications

生物活性

No

访问

P38398

不含动物源

No

不含载体蛋白

No

种属

Human

存储溶液

pH: 7.9 Constituents: 20% Glycerol (glycerin, glycerine), 0.75% Potassium chloride, 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.00584% EDTA

storage-buffer

反应性数据

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

序列信息

[{"sequence":"MDLSALRVEEVQNVINAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNDITKRSLQESTRFSQLVEELLKIICAFQLDTGLEYANSYNFAKKENNSPEHLKDEVSIIQSMGYRNRAKRLLQSEPENPSLQETSLSVQLSNLGTVRTLRTKQRIQPQKTSVYIELGSDSSEDTVNKATYCSVGDQELLQITPQGTRDEISLDSAKKAACEFSETDVTNTEHHQPSNNDLNTTEKRAAERHPEKYQGSSVSNLHVEPCGTNTHASSLQHENSSLLLTKDRMNVEKAEFCNKSKQPGLARSQHNRWAGSKETCNDRRTPSTEKKVDLNADPLCERKEWNKQKLPCSENPRDTEDVPWITLNSSIQKVNEWFSRSDELLGSDDSHDGESESNAKVADVLDVLNEVDEYSGSSEKIDLLASDPHEALICKSERVHSKSVESNIEDKIFGKTYRKKASLPNLSHVTENLIIGAFVTEPQIIQERPLTNKLKRKRRPTSGLHPEDFIKKADLAVQKTPEMINQGTNQTEQNGQVMNITNSGHENKTKGDSIQNEKNPNPIESLEKESAFKTKAEPISSSISNMELELNIHNSKAPKKNRLRRKSSTRHIHALELVVSRNLSPPNCTELQIDSCSSSEEIKKKKYNQMPVRHSRNLQLMEGKEPATGAKKSNKPNEQTSKRHDSDTFPELKLTNAPGSFTKCSNTSELKEFVNPSLPREEKEEKLETVKVSNNAEDPKDLMLSGERVLQTERSVESSSISLVPGTDYGTQESISLLEVSTLGKAKTEPNKCVSQCAAFENPKGLIHGCSKDNRNDTEGFKYPLGHEVNHSRETSIEMEESELDAQYLQNTFKVSKRQSFAPFSNPGNAEEECATFSAHSGSLKKQSPKVTFECEQKEENQGKNESNIKPVQTVNITAGFPVVGQKDKPVDNAKCSIKGGSRFCLSSQFRGNETGLITPNKHGLLQNPYRIPPLFPIKSFVKTKCKKNLLEENFEEHSMSPEREMGNENIPSTVSTISRNNIRENVFKEASSSNINEVGSSTNEVGSSINEIGSSDENIQAELGRNRGPKLNAMLRLGVLQPEVYKQSLPGSNCKHPEIKKQEYEEVVQTVNTDFSPYLISDNLEQPMGSSHASQVCSETPDDLLDDGEIKEDTSFAENDIKESSAVFSKSVQKGELSRSPSPFTHTHLAQGYRRGAKKLESSEENLSSEDEELPCFQHLLFGKVNNIPSQSTRHSTVATECLSKNTEENLLSLKNSLNDCSNQVILAKASQEHHLSEETKCSASLFSSQCSELEDLTANTNTQDPFLIGSSKQMRHQSESQGVGLSDKELVSDDEERGTGLEENNQEEQSMDSNLGEAASGCESETSVSEDCSGLSSQSDILTTQQRDTMQHNLIKLQQEMAELEAVLEQHGSQPSNSYPSIISDSSALEDLRNPEQSTSEKAVLTSQKSSEYPISQNPEGLSADKFEVSADSSTSKNKEPGVERSSPSKCPSLDDRWYMHSCSGSLQNRNYPSQEELIKVVDVEEQQLEESGPHDLTETSYLPRQDLEGTPYLESGISLFSDDPESDPSEDRAPESARVGNIPSSTSALKVPQLKVAESAQSPAAAHTTDTAGYNAMEESVSREKPELTASTERVNKRMSMVVSGLTPEEFMLVYKFARKHHITLTNLITEETTHVVMKTDAEFVCERTLKYFLGIAGGKWVVSYFWVTQSIKERKMLNEHDFEVRGDVVNGRNHQGPKRARESQDRKIFRGLEICCYGPFTNMPTDQLEWMVQLCGASVVKELSSFTLGTGVHPIVVVQPDAWTEDNGFHAIGQMCEAPVVTREWVLDSVALYQCQELDTYLIPQIPHSHY","proteinLength":"Full Length","predictedMolecularWeight":"209.1 kDa","actualMolecularWeight":null,"aminoAcidEnd":1863,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Baculovirus infected insect cells","accessionNumber":"P38398","tags":[{"tag":"6x His","terminus":"C-Terminus"}]}]

性能和储存信息

运输条件
Dry Ice
推荐的短期储存条件
-80°C
推荐的长期储存条件
-80°C
分装信息
Upon delivery aliquot
储存信息
Avoid freeze / thaw cycle
False

特殊说明

形式

Liquid

附加说明

Purified by affinity and FPLC chromatography.

常规信息

功能

E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage (PubMed : 10500182, PubMed : 12887909, PubMed : 12890688, PubMed : 14976165, PubMed : 16818604, PubMed : 17525340, PubMed : 19261748). It is unclear whether it also mediates the formation of other types of polyubiquitin chains (PubMed : 12890688). The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability (PubMed : 12890688, PubMed : 14976165, PubMed : 20351172). Regulates centrosomal microtubule nucleation (PubMed : 18056443). Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle (PubMed : 10724175, PubMed : 11836499, PubMed : 12183412, PubMed : 19261748). Required for FANCD2 targeting to sites of DNA damage (PubMed : 12887909). Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation (PubMed : 16326698). Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks (PubMed : 19369211). Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8 (PubMed : 16818604). Acts as a transcriptional activator (PubMed : 20160719).

翻译后修饰

Phosphorylated in response to IR, UV, and various stimuli that cause checkpoint activation, probably by ATM or ATR (PubMed:11114888, PubMed:12183412, PubMed:21144835). Phosphorylation at Ser-988 by CHEK2 regulates mitotic spindle assembly (PubMed:10724175, PubMed:20364141). Phosphorylation by AURKA regulates centrosomal microtubule nucleation (PubMed:18056443).. Autoubiquitinated, undergoes 'Lys-6'-linked polyubiquitination. 'Lys-6'-linked polyubiquitination does not promote degradation. Ubiquitinated in a FBXO44-dependent manner; leading to proteasomal degradation (PubMed:23086937).

产品实验方案

靶点信息

E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage (PubMed : 10500182, PubMed : 12887909, PubMed : 12890688, PubMed : 14976165, PubMed : 16818604, PubMed : 17525340, PubMed : 19261748). It is unclear whether it also mediates the formation of other types of polyubiquitin chains (PubMed : 12890688). The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability (PubMed : 12890688, PubMed : 14976165, PubMed : 20351172). Regulates centrosomal microtubule nucleation (PubMed : 18056443). Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle (PubMed : 10724175, PubMed : 11836499, PubMed : 12183412, PubMed : 19261748). Required for FANCD2 targeting to sites of DNA damage (PubMed : 12887909). Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation (PubMed : 16326698). Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks (PubMed : 19369211). Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8 (PubMed : 16818604). Acts as a transcriptional activator (PubMed : 20160719).
See full target information BRCA1

文献 (2)

Recent publications for all applications. Explore the full list and refine your search

Cell reports 24:3262-3273.e4 PubMed30232007

2018

The Helicase PIF1 Facilitates Resection over Sequences Prone to Forming G4 Structures.

Applications

Unspecified application

Species

Unspecified reactive species

Sonia Jimeno,Rosa Camarillo,Fernando Mejías-Navarro,Maria Jesús Fernández-Ávila,Isabel Soria-Bretones,Rosario Prados-Carvajal,Pablo Huertas

PloS one 8:e66801 PubMed23826138

2013

Interaction between DNA Polymerase β and BRCA1.

Applications

Unspecified application

Species

Unspecified reactive species

Aya Masaoka,Natalie R Gassman,Julie K Horton,Padmini S Kedar,Kristine L Witt,Cheryl A Hobbs,Grace E Kissling,Keizo Tano,Kenjiro Asagoshi,Samuel H Wilson
View all publications

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