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ELISA Kit for Mouse Breast cancer type 1 susceptibility protein homolog

SKU : BHE13801661

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EIAAB SCIENCE INC, WUHAN

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Mfr.No.	E0939m
Alternative Names	RING-type E3 ubiquitin transferase BRCA1
Categories	Elisa
Function	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. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The E3 ubiquitin-protein ligase activity is required for its tumor suppressor function. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Regulates centrosomal microtubule nucleation. Required for normal cell cycle progression from G2 to mitosis. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Involved in transcriptional regulation of P21 in response to DNA damage. Required for FANCD2 targeting to sites of DNA damage. May function as a transcriptional regulator. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation. 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.
Specificity	Natural and recombinant Mouse Breast cancer type 1 susceptibility protein homolog
Subcellular Location	Nucleus Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex.
Detection Range	0.312-20ng/mL
Entryname	BRCA1_MOUSE
Method Type	Sandwich
Platform	PF00533
Protein Name	Breast cancer type 1 susceptibility protein homolog
Sensitivity	0.072ng/mL
Sequence	50: MDLSAVQIQE ; VQNVLHAMQK ; ILECPICLEL ; IKEPVSTKCD ; HIFCKFCMLK ; 100: LLNQKKGPSQ ; CPLCKNEITK ; RSLQGSTRFS ; QLAEELLRIM ; AAFELDTGMQ ; 150: LTNGFSFSKK ; RNNSCERLNE ; EASIIQSVGY ; RNRVRRLPQV ; EPGNATLKDS ; 200: LGVQLSNLGI ; VRSVKKNRQT ; QPRKKSVYIE ; LDSDSSEETV ; TKPGDCSVRD ; 250: QELLQTAPQE ; AGDEGKLHSA ; EEAACEFSEG ; IRNIEHHQCS ; DDLNPTENHA ; 300: TERHPEKCQS ; ISISNVCVEP ; CGTDAHASSL ; QPETSSLLLI ; EDRMNAEKAE ; 350: FCNKTKQPGI ; AVSQQSRWPA ; SKGTCNDRQV ; PSTGEKVGPN ; ADSLSDREKW ; 400: THPQSLCPEN ; SGATTDVPWI ; TLNSSVQKVN ; EWFSRTGEML ; TSDSASARRH ; 450: ESNAEAAVVL ; EVSNEVDGGF ; SSSRKTDLVT ; PDPHHTLMCK ; SGRDFSKPVE ; 500: DNISDKIFGK ; SYQRKGSRPH ; LNHVTEIIGT ; FITEPQITQE ; QPFTNKLKRK ; 550: RSTSLQPEDF ; IKKADSAGVQ ; RTPDNINQGT ; DLMEPNEQAV ; STTSNCQENK ; 600: IAGSNLQKEK ; SAHPTESLRK ; EPASTAGAKS ; ISNSVSDLEV ; ELNVHSSKAP ; 650: KKNRLRRKSS ; IRCALPLEPI ; SRNPSPPTCA ; ELQIDSCGSS ; EETKKNHSNQ ; 700: QAAGHLREPQ ; LIEDTEPAAD ; AKKNEPNEHI ; RKRRASDAFP ; EEKLMNKAGL ; 750: LTSCSSPRKS ; QGPVNPSPQR ; TGTEQLETRQ ; MSDSAKELGD ; RVLGGEPSGK ; 800: TTDRSEESTS ; VSLVSDTDYD ; TQNSVSVLDA ; HTVRYARTGS ; AQCMTQFVAS ; 850: ENPKELVHGS ; NNAGSGTEGL ; KPPLRHALNL ; SQEKVEMEDS ; ELDTQYLQNT ; 900: FQVSKRQSFA ; LFSKPRSPQK ; DCAHSVPSKE ; LSPKVTAKGK ; QKERQGQEEF ; 950: EISHVQAVAA ; TVGLPVPCQE ; GKLAADTMCD ; RGCRLCPSSH ; YRSGENGLSA ; 1000: TGKSGISQNS ; HFKQSVSPIR ; SSIKTDNRKP ; LTEGRFERHT ; SSTEMAVGNE ; 1050: NILQSTVHTV ; SLNNRGNACQ ; EAGSGSIHEV ; CSTGDSFPGQ ; LGRNRGPKVN ; 1100: TVPPLDSMQP ; GVCQQSVPVS ; DKYLEIKKQE ; GEAVCADFSP ; CLFSDHLEQS ; 1150: MSGKVFQVCS ; ETPDDLLDDV ; EKQGHTSFGE ; GDIMERSAVF ; NGSILRRESS ; 1200: RSPSPVTHAS ; KSQSLHRASR ; KLESSEESDS ; TEDEDLPCFQ ; HLLSRISNTP ; 1250: ELTRCSSAVT ; QRMPEKAEGT ; QAPWKGSSSD ; CNNEVIMIEA ; SQEHQFSEDP ; 1300: RCSGSMFSSQ ; HSAVQGSTPN ; ANSQDSNFIP ; PSTQRSHQCG ; NEEAFLSDKE ; 1350: LISDNEEMAT ; CLEEDNDQEE ; DSIIPDSEAS ; GYESETTLSE ; DCSQSDILPT ; 1400: QEGATMKYNL ; IKLQQEMAHL ; EAVLEQRGNQ ; SSGHSPSLLG ; DPCALEDLPV ; 1450: LEPNMSGAAI ; LTSKNINENP ; VSQNLKSACD ; DKFQLQHLEG ; PTSGDDESGM ; 1500: GRPSPFKSPL ; AGSRGSAHGC ; SRHLQKRNSP ; SQEELLQPAG ; SEASSEPHNS ; 1550: TGESCLPRRE ; LEGTPYLGSG ; ISLFSSRDPE ; SESPKEPAHI ; GTTPASTSVL ; 1600: KIPQGQVAFR ; SAAAAGADKA ; VVGIVSKIKP ; ELTSSEERAD ; RDISMVVSGL ; 1650: TPKEVMTVQK ; FAEKYRLTLT ; DAITEETTHV ; IIKTDAEFVC ; ERTLKYFLGI ; 1700: AGGKWIVSYS ; WVVRSIQERR ; LLNVHEFEVT ; GDVVTGRNHQ ; GPRRSRESRE ; 1750: KLFKGLQVYC ; CDPFTNMPKD ; DLERMLQLCG ; ASVVKELPSL ; THDTGAHLVV ; 1800: IVQPSAWTED ; SNCPDIGQLC ; KARLVMWDWV ; LDSLSSYRCR ; DLDAYLVQNI ; 1812: TCDSSEPQDS ; ND
Sequence Length	1812
String	P48754
Sub Unit	Heterodimer with BARD1. Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBN protein complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. Component of the BRCA1-A complex, at least composed of the BRCA1, BARD1, UIMC1/RAP80, FAM175A/Abraxas, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/NBA1. Interacts (via BRCT domains) with FAM175A/Abraxas and RBBP8. Associates with RNA polymerase II holoenzyme. Interacts with SMC1A and COBRA1/NELFB. Interacts (via BRCT domains) with phosphorylated BRIP1. Interacts with FANCD2 (ubiquitinated). Interacts with BAP1. Interacts with DCLRE1C/Artemis and CLSPN. Interacts with H2AFX (phosphorylated on 'Ser-140'). Interacts with CHEK1/CHK1. Interacts with BRCC3. Interacts (via BRCT domains) with ACACA (phosphorylated); the interaction prevents dephosphorylation of ACACA. Interacts with AURKA. Interacts with UBXN1. Part of a trimeric complex containing BRCA1, BRCA2 and PALB2. Interacts with PALB2 and this interaction is essential for its function in HRR. Interacts with BRCA2 only in the presence of PALB2 which serves as the bridging protein.

Uniprot	P48754
Gene Name	Brca1
Immunogen Species	Mus musculus (Mouse)
Kegg	mmu:12189
Unigene	Mm.244975

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