Recombinant Mouse Breast cancer type 2 susceptibility protein homolog (Brca2), partial

Product Details

Purity
>85% (SDS-PAGE)
Target Names
Brca2
Uniprot NO.
Alternative Names
Brca2; Fancd1; Breast cancer type 2 susceptibility protein homolog; Fanconi anemia group D1 protein homolog
Species
Mus musculus (Mouse)
Source
Yeast
Expression Region
1-3329
Target Protein Sequence
MPVEYKRRPT FWEIFKARCS TADLGPISLN WFEELSSEAP PYNSEPPEES EYKPHGYEPQ LFKTPQRNPP YHQFASTPIM FKERSQTLPL DQSPFRELGK VVASSKHKTH SKKKTKVDPV VDVASPPLKS CLSESPLTLR CTQAVLQREK PVVSGSLFYT PKLKEGQTPK PISESLGVEV DPDMSWTSSL ATPPTLSSTV LIARDEEARS SVTPADSPAT LKSCFSNHNE SPQKNDRSVP SVIDSENKNQ QEAFSQGLGK MLGDSSGKRN SFKDCLRKPI PNILEDGETA VDTSEEDSFS LCFPKRRTRN LQKMRMGKTR KKIFSETRTD ELSEEARRQT DDKNSFVFEM ELRESDPLDP GVTSQKPFYS QNEEICNEAV QCSDSRWSQS NLSGLNETQT GKITLPHISS HSQNISEDFI DMKKEGTGSI TSEKSLPHIS SLPEPEKMFS EETVVDKEHE GQHFESLEDS IAGKQMVSRT SQAACLSPSI RKSIFKMREP LDETLGTVFS DSMTNSTFTE EHEASACGLG ILTACSQRED SICPSSVDTG SWPTTLTDTS ATVKNAGLIS TLKNKKRKFI YSVSDDASLQ GKKLQTHRQL ELTNLSAQLE ASAFEVPLTF TNVNSGIPDS SDKKRCLPND PEEPSLTNSF GTATSKEISY IHALISQDLN DKEAIVIEEK PQPYTAREAD FLLCLPERTC ENDQKSPKVS NGKEKVLVSA CLPSAVQLSS ISFESQENPL GDHNGTSTLK LTPSSKLPLS KADMVSREKM CKMPEKLQCE SCKVNIELSK NILEVNEICI LSENSKTPGL LPPGENIIEV ASSMKSQFNQ NAKIVIQKDQ KGSPFISEVA VNMNSEELFP DSGNNFAFQV TNKCNKPDLG SSVELQEEDL SHTQGPSLKN SPMAVDEDVD DAHAAQVLIT KDSDSLAVVH DYTEKSRNNI EQHQKGTEDK DFKSNSSLNM KSDGNSDCSD KWSEFLDPVL NHNFGGSFRT ASNKEIKLSE HNVKKSKMFF KDIEEQYPTR LACIDIVNTL PLANQKKLSE PHIFDLKSVT TVSTQSHNQS SVSHEDTDTA PQMLSSKQDF HSNNLTTSQK AEITELSTIL EESGSQFEFT QFRKPSHIAQ NTSEVPGNQM VVLSTASKEW KDTDLHLPVD PSVGQTDHSK QFEGSAGVKQ SFPHLLEDTC NKNTSCFLPN INEMEFGGFC SALGTKLSVS NEALRKAMKL FSDIENSEEP SAKVGPRGFS SSAHHDSVAS VFKIKKQNTE KSFDEKSSKC QVTLQNNIEM TTCIFVGRNP EKYIKNTKHE DSYTSSQRNN LENSDGSMSS TSGPVYIHKG DSDLPADQGS KCPESCTQYA REENTQIKEN ISDLTCLEIM KAEETCMKSS DKKQLPSDKM EQNIKEFNIS FQTASGKNTR VSKESLNKSV NIFNRETDEL TVISDSLNSK ILHGINKDKM HTSCHKKAIS IKKVFEDHFP IVTVSQLPAQ QHPEYEIEST KEPTLLSFHT ASGKKVKIMQ ESLDKVKNLF DETQYVRKTA SFSQGSKPLK DSKKELTLAY EKIEVTASKC EEMQNFVSKE TEMLPQQNYH MYRQTENLKT SNGTSSKVQE NIENNVEKNP RICCICQSSY PVTEDSALAY YTEDSRKTCV RESSLSKGRK WLREQGDKLG TRNTIKIECV KEHTEDFAGN ASYEHSLVII RTEIDTNHVS ENQVSTLLSD PNVCHSYLSQ SSFCHCDDMH NDSGYFLKNK IDSDVPPDMK NAEGNTISPR VSATKERNLH PQTINEYCVQ KLETNTSPHA NKDVAIDPSL LDSRNCKVGS LVFITAHSQE TERTKEIVTD NCYKIVEQNR QSKPDTCQTS CHKVLDDSKD FICPSSSGDV CINSRKDSFC PHNEQILQHN QSMSGLKKAA TPPVGLETWD TSKSIREPPQ AAHPSRTYGI FSTASGKAIQ VSDASLEKAR QVFSEMDGDA KQLSSMVSLE GNEKPHHSVK RENSVVHSTQ GVLSLPKPLP GNVNSSVFSG FSTAGGKLVT VSESALHKVK GMLEEFDLIR TEHTLQHSPI PEDVSKILPQ PCAEIRTPEY PVNSKLQKTY NDKSSLPSNY KESGSSGNTQ SIEVSLQLSQ MERNQDTQLV LGTKVSHSKA NLLGKEQTLP QNIKVKTDEM KTFSDVPVKT NVGEYYSKES ENYFETEAVE SAKAFMEDDE LTDSEQTHAK CSLFTCPQNE TLFNSRTRKR GGVTVDAVGQ PPIKRSLLNE FDRIIESKGK SLTPSKSTPD GTVKDRSLFT HHMSLEPVTC GPFCSSKERQ GAQRPHLTSP AQELLSKGHP WRHSALEKSP SSPIVSILPA HDVSATRTER TRHSGKSTKV FVPPFKMKSQ FHGDEHFNSK NVNLEGKNQK STDGDREDGN DSHVRQFNKD LMSSLQSARD LQDMRIKNKE RRHLRLQPGS LYLTKSSTLP RISLQAAVGD RAPSACSPKQ LYIYGVSKEC INVNSKNAEY FQFDIQDHFG KEDLCAGKGF QLADGGWLIP SNDGKAGKEE FYRALCDTPG VDPKLISSIW VANHYRWIVW KLAAMEFAFP KEFANRCLNP ERVLLQLKYR YDVEIDNSRR SALKKILERD DTAAKTLVLC ISDIISPSTK VSETSGGKTS GEDANKVDTI ELTDGWYAVR AQLDPPLMAL VKSGKLTVGQ KIITQGAELV GSPDACAPLE APDSLRLKIS ANSTRPARWH SRLGFFRDPR PFPLPLSSLF SDGGNVGCVD IIVQRVYPLQ WVEKTVSGLY IFRSEREEEK EALRFAEAQQ KKLEALFTKV HTEFKDHEED TTQRCVLSRT LTRQQVHALQ DGAELYAAVQ YASDPDHLEA CFSEEQLRAL NNYRQMLNDK KQARIQSEFR KALESAEKEE GLSRDVTTVW KLRVTSYKKK EKSALLSIWR PSSDLSSLLT EGKRYRIYHL AVSKSKSKFE RPSIQLTATK RTQYQQLPVS SETLLQVYQP RESLHFSRLS DPAFQPPCSE VDVVGVVVSV VKPIGLAPLV YLSDECLNLL VVKFGIDLNE DIKPRVLIAA SNLQCQPEST SGVPTLFAGH FSIFSASPKE AYFQEKVNNL KHAIENIDTF YKEAEKKLIH VLEGDSPKWS TPNKDPTREP HAASTCCASD LLGSGGQFLR ISPTGQQSYQ SPLSHCTLKG KSMPLAHSAQ MAAKSWSGEN EIDDPKTCRK RRALDFLSRL PLPSPVSPIC TFVSPAAQKA FQPPRSCGTK YATPIKKEPS SPRRRTPFQK TSGVSLPDCD SVADEELALL STQALTPDSV GGNEQAFPGD STRNPQPAQR PDQQVGPRSR KESLRDCRGD SSEKLAVES
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
Protein Length
Partial
Tag Info
N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Storage Condition
Store at -20°C, for extended storage, conserve at -20°C or -80°C.
Shelf Life
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 -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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 Customer Reviews

Target Background

Function(From Uniprot)
Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and SEM1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability, independently of its known role in homologous recombination.
Gene References into Functions
  1. BRCA2-proficient and deficient cells are radiosensitised by HT, indicating that HT does not exclusively act by inhibition of HR. PMID:28540821
  2. Results suggest that the greater reliance on homology-directed repair (HDR) in the proliferating mammary gland, rather than a specific dependence on breast cancer 2 protein (BRCA2), may increase its susceptibility to tumorigenesis incurred by BRCA2 mutation. PMID:27779185
  3. The functional consequence of Parp1 heterozygosity on BRCA2 loss is demonstrated by a significant increase in tumorigenesis in Brca2 knockout mice. PMID:27498558
  4. we generated a Brca2 knock-in mouse model lacking exons 4-7 and demonstrated that these exons are dispensable for viability as well as tumor-free survival. This study provides the first in vivo evidence of the functional significance of a minor transcript of BRCA2 that can play a major role in the survival of humans who are homozygous for a clearly pathogenic mutation. PMID:26920070
  5. we describe a genetic approach to examine the functional significance of the interaction between BRCA2 and PALB2 by generating a knock-in mouse model of Brca2 carrying a single amino acid change (Gly25Arg, Brca2G25R) that disrupts this interaction. In addition, we have combined Brca2G25R homozygosity as well as hemizygosity with Palb2 and Trp53 heterozygosity . PMID:27490902
  6. Merit40 mutation exacerbated ICL-induced chromosome instability in the context of concomitant Brca2 deficiency but not in conjunction with Fancd2 mutation. PMID:26338419
  7. Heterozygous and homozygous Brca2 mutation may lead to dysfunction in T cell populations. PMID:25666348
  8. BRCA2 exon 27 domain maintains chromosomal integrity at both stalled and collapsed replication forks consistent with involvement in both replication fork maintenance and double strand break repair. PMID:25773776
  9. we use a genetically engineered mouse model of BRCA2-associated hereditary breast cancer to study drug resistance to several types of chemotherapy and PARP inhibition. PMID:25511378
  10. BRCA2-mediated sequestration of nuclear RAD51 serves to prevent inappropriate DNA interactions. PMID:25488918
  11. BRCA2 directly represses the expression of IFN-related genes PMID:25043256
  12. the models reveal novel aspects of cancer evolution in carriers of germline BRCA2 mutations, provide new insights into the tumour suppressive role of BRCA2 PMID:24268522
  13. genetic stability, and hematopoietic differentiation potential of gene-corrected Brca2(Delta) (27/) (Delta) (27) iPSCs, achievements and limitations in the application of current reprogramming approaches in hematopoietic stem cell therapy are also discussed. PMID:24420904
  14. Results suggest that cellular levels of Brca2 and Rad51 are mutually dependent on each other, and that low levels of these proteins provide selective pressure for reduction of p53, which permits cell growth PMID:24210700
  15. BRCA2 accumulates DNA damage, which triggers checkpoint signalling and ARF activation PMID:24162189
  16. data showed that silencing of BRCA2 promoted cell proliferation, migration and invasion in vitro; data reported here demonstrate that BRCA2 may be a promising therapeutic targets for pancreatic ductal adenocarcinoma progression PMID:22934697
  17. BRCA2 is required for telomere homeostasis and may be particularly important for the replication of G-rich telomeric lagging strands. PMID:22187435
  18. Loss of Brca2 function predisposes the exocrine pancreas to profound DNA damage, and the frequency of invasive neoplasia is accentuated by the concomitant deregulation of p53 PMID:21455033
  19. FANCD1/BRCA2 played notably important roles in the repair of TMZ-induced DNA damage. PMID:21573016
  20. Data suggest that the growth-suppressive effect of CHK1 inhibition in BRCA2-mutant tumors can be opposed by concurrent KRAS activation and TP53 mutations. PMID:21289082
  21. Trp53 signaling must be modified before inactivation of the Brca2 wild-type allele, irrespective of Kras status, for Brca2-deficient cells to form pancreatic tumors PMID:21199651
  22. BRCA2 associates with telomeres during the S and G2 phases of the cell cycle and facilitates the loading of RAD51 onto telomeres. PMID:21076401
  23. Germline heterozygosity for a pathogenic Brca2 truncation suffices to promote pancreatic ductal adenocarcinomas driven by Kras(G12D), irrespective of Trp53 status. PMID:21056012
  24. Simultaneous deletion of Brca2 and the tumour suppressor Trp53 in prostate epithelia gave rise to focal hyperplasia and atypical cells PMID:20585617
  25. Loss of Brca2 increases in vivo somatic mutation acquisition and synergizes with ionizing radiation exposure. PMID:11850397
  26. Genomic organization and expression of the mouse Brca2 gene PMID:12140683
  27. crystal structure of a COOH terminal BRCA2 domain bound to DSS1; demonstrate that this BRCA2 domain binds single-stranded DNA and show that BRCA2 stimulates RAD51-mediated recombination in vitro PMID:12228710
  28. The extreme carboxy-terminal region encoded by exon 27 is vital for BRCA2 function in mice, perhaps because it is required for a fully functional interaction between BRCA2 and RAD51, though it is less severe than truncations that delete some BRC motifs. PMID:12619154
  29. BRCA2 has a role in modulating M phase progression PMID:12815053
  30. interplay between Brca2 and mitotic checkpoint has been suggested in the maintenance of genetic fidelity PMID:14646599
  31. BRCA2-deficient spermatocytes fail to progress beyond the early prophase I stage of meiosis. PMID:14660434
  32. Brca2 knockout mouse is less susceptible to chemically indeced tumorigenesis. PMID:14981540
  33. results show that BRCA2 deficiency impairs the completion of cell division by cytokinesis PMID:15375219
  34. Brca2 plays an important role in the response to DNA damage in the small intestine. PMID:15735671
  35. In the small intestine, deletion of cells lacking Brca2 is necessary to avoid the development of potentially tumorigenic clones in this tissue. PMID:16042582
  36. Homozygous germ-line mutation in exon 27 of Brca2 disrupts the Fancd2-Brca2 pathway in the homologous recombination-mediated DNA interstrand cross-links' repair, but does not affect meiosis. PMID:16127665
  37. These findings include extensive in vivo data demonstrating that germline Brca2 and p53 mutations cooperatively affect animal survivals, tumor susceptibilities, and tumor onsets. PMID:16546942
  38. These results identify a novel role for FoxM1 in the transcriptional response during DNA damage/checkpoint signaling and show a novel mechanism by which Chk2 protein regulates expression of DNA repair enzymes. PMID:17101782
  39. Brca2 has roles in DNA repair and recombination PMID:17336596
  40. BRCA2 is required for neurogenesis and suppression of medulloblastoma. PMID:17476307
  41. Loss of Rad51 function as a critical underlying factor in the homologous recombination defect in the Brca2-depleted cells. PMID:18992372
  42. Article describes the involvement of BRCA2 in O6-alkylguanine DNA alkyltransferase (AGT)-mediated repair of O6-methylguanine adducts. PMID:19047179
  43. Murine Brca2 shares multiple properties with human BRCA2 including its regulation during the cell cycle, localization to nuclear foci, and interaction with Brca1 and Rad51. PMID:11477095

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Subcellular Location
Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Tissue Specificity
Widely expressed. Highest expression in cerebellum, testis, ileum, appendix, epididymis, ovary and mammary gland. No expression in lung.
Database Links
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