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DNA repair protein RAD51 homolog 1 (RAD51 homolog A)

 RAD51_MOUSE             Reviewed;         339 AA.
Q08297; Q3UAY5;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 1.
22-NOV-2017, entry version 178.
RecName: Full=DNA repair protein RAD51 homolog 1;
AltName: Full=RAD51 homolog A;
Name=Rad51; Synonyms=Rad51a, Reca;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8358431; DOI=10.1038/ng0793-239;
Shinohara A., Ogawa H., Matsuda Y., Ushio N., Ikeo K., Ogawa T.;
"Cloning of human, mouse and fission yeast recombination genes
homologous to RAD51 and recA.";
Nat. Genet. 4:239-243(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
PubMed=8341671; DOI=10.1073/pnas.90.14.6577;
Morita T., Yoshimura Y., Yamamoto A., Murata K., Mori M., Yamamoto H.,
Matsushiro A.;
"A mouse homolog of the Escherichia coli recA and Saccharomyces
cerevisiae RAD51 genes.";
Proc. Natl. Acad. Sci. U.S.A. 90:6577-6580(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
LEVEL OF PROTEIN EXPRESSION.
PubMed=12531026; DOI=10.1016/S1568-7864(02)00110-6;
Essers J., Hendriks R.W., Wesoly J., Beerens C.E.M.T., Smit B.,
Hoeijmakers J.H.J., Wyman C., Dronkert M.L.G., Kanaar R.;
"Analysis of mouse Rad54 expression and its implications for
homologous recombination.";
DNA Repair 1:779-793(2002).
[6]
FUNCTION, AND INTERACTION WITH MND1-PSMC3IP HETERODIMER.
PubMed=15834424; DOI=10.1038/nsmb923;
Petukhova G.V., Pezza R.J., Vanevski F., Ploquin M., Masson J.-Y.,
Camerini-Otero R.D.;
"The Hop2 and Mnd1 proteins act in concert with Rad51 and Dmc1 in
meiotic recombination.";
Nat. Struct. Mol. Biol. 12:449-453(2005).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
INTERACTION WITH SWI5.
PubMed=20976249; DOI=10.1371/journal.pgen.1001160;
Akamatsu Y., Jasin M.;
"Role for the mammalian Swi5-Sfr1 complex in DNA strand break repair
through homologous recombination.";
PLoS Genet. 6:E1001160-E1001160(2010).
[9]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=22305526; DOI=10.1016/j.ajhg.2011.12.002;
Depienne C., Bouteiller D., Meneret A., Billot S., Groppa S.,
Klebe S., Charbonnier-Beaupel F., Corvol J.C., Saraiva J.P.,
Brueggemann N., Bhatia K., Cincotta M., Brochard V., Flamand-Roze C.,
Carpentier W., Meunier S., Marie Y., Gaussen M., Stevanin G.,
Wehrle R., Vidailhet M., Klein C., Dusart I., Brice A., Roze E.;
"RAD51 haploinsufficiency causes congenital mirror movements in
humans.";
Am. J. Hum. Genet. 90:301-307(2012).
[10]
INTERACTION WITH FBXO18.
PubMed=24108124; DOI=10.1074/jbc.M113.484493;
Simandlova J., Zagelbaum J., Payne M.J., Chu W.K., Shevelev I.,
Hanada K., Chatterjee S., Reid D.A., Liu Y., Janscak P.,
Rothenberg E., Hickson I.D.;
"FBH1 helicase disrupts RAD51 filaments in vitro and modulates
homologous recombination in mammalian cells.";
J. Biol. Chem. 288:34168-34180(2013).
-!- FUNCTION: Plays an important role in homologous strand exchange, a
key step in DNA repair through homologous recombination (HR)
(PubMed:15834424). Binds to single and double-stranded DNA and
exhibits DNA-dependent ATPase activity. Catalyzes the recognition
of homology and strand exchange between homologous DNA partners to
form a joint molecule between a processed DNA break and the repair
template. Binds to single-stranded DNA in an ATP-dependent manner
to form nucleoprotein filaments which are essential for the
homology search and strand exchange. Part of a PALB2-scaffolded HR
complex containing BRCA2 and RAD51C and which is thought to play a
role in DNA repair by HR. Plays a role in regulating mitochondrial
DNA copy number under conditions of oxidative stress in the
presence of RAD51C and XRCC3. Also involved in interstrand cross-
link repair (By similarity). {ECO:0000250|UniProtKB:Q06609,
ECO:0000269|PubMed:15834424}.
-!- SUBUNIT: Forms linear homooligomers, giving rise to a RAD51
nucleoprotein filament, which is essential for strand-pairing
reactions during DNA recombination. Interacts with BRCA1 and
either directly or indirectly with p53. Interacts with XRCC3,
RAD54L and RAD54B. Interacts with the BCDX2 subcomplex
RAD51C:RAD51B. Interacts directly with PALB2 which may serve as a
scaffold for a HR complex containing PALB2, BRCA2, RAD51C, RAD51
and XRCC3. Interacts with RAD51AP1 and RAD51AP2. Interacts with
CHEK1, and this may require prior phosphorylation of CHEK1 (By
similarity). Interacts with the MND1-PSMC3IP heterodimer
(PubMed:15834424). Found in a complex, at least composed of BLM,
RAD51 and SPIDR; the complex formation is mediated by SPIDR.
Interacts with SPIDR; the interaction is direct and recruits RAD51
to DNA damage sites. Interacts with FIGNL1 (via N-terminal one-
half region); the interaction is direct. Interacts with RAD51AP1
(via C-terminal region); the interaction is direct (By
similarity). Interacts with NABP2, RPA1, PALB2 and RAD51.
Interacts with SWI5/C9orf119, and at lower level with SFR1/MEIR5
(PubMed:20976249). Interacts with hyperphosphorylated RPA2; this
interaction is necessary for efficient recruitment to chromatin in
response to DNA damage. Interacts with SWSAP1; involved in
homologous recombination repair. Interacts with PARPBP, BRCA2 and
RECQL5; these interactions interfere with the formation of the
RAD51-DNA homologous recombination structure. Interacts with POLQ;
POLQ acts as an inhibitor of homology-recombination repair (HR)
pathway by limiting RAD51 accumulation at resected ends. Interacts
with POLN (By similarity). Interacts with FBXO18/FBH1
(PubMed:24108124). Interacts with RFWD3 (By similarity).
{ECO:0000250|UniProtKB:Q06609, ECO:0000269|PubMed:15834424,
ECO:0000269|PubMed:20976249, ECO:0000269|PubMed:24108124}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q06609}.
Cytoplasm {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, perinuclear
region {ECO:0000250|UniProtKB:Q06609}. Mitochondrion matrix
{ECO:0000250|UniProtKB:Q06609}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:Q06609}. Note=Colocalizes with RAD51AP1 and
RPA2 to multiple nuclear foci upon induction of DNA damage. DNA
damage induces an increase in nuclear levels. Together with
FIGNL1, redistributed in discrete nuclear DNA damage-induced foci
after ionizing radiation (IR) or camptothecin (CPT) treatment.
Accumulated at sites of DNA damage in a SPIDR-dependent manner.
{ECO:0000250|UniProtKB:Q06609}.
-!- TISSUE SPECIFICITY: Expressed in ovary and testis. Expressed in
the brain. {ECO:0000269|PubMed:22305526}.
-!- DEVELOPMENTAL STAGE: Expression in the brain is strongest at day
E12, particularly in the cortical ventricular zone. In the cortex
of newborn mice (P0), RAD51 is mainly present in the subplate and,
in lesser amounts, in layer V. It is detected in a subpopulation
of corticospinal axons at the pyramidal decussation in 2-day-old
(P2) mice. {ECO:0000269|PubMed:22305526}.
-!- PTM: Ubiquitinated by the SCF(FBXO18) E3 ubiquitin ligase complex,
regulating RAD51 subcellular location and preventing its
association with DNA. Ubiquitinated by RFWD3 in response to DNA
damage: ubiquitination leads to degradation by the proteasome,
promoting homologous recombination.
{ECO:0000250|UniProtKB:Q06609}.
-!- PTM: Phosphorylated. Phosphorylation of Thr-309 by CHEK1 may
enhance association with chromatin at sites of DNA damage and
promote DNA repair by homologous recombination. Phosphorylation by
ABL1 inhibits function. {ECO:0000250|UniProtKB:Q06609}.
-!- MISCELLANEOUS: The nucleus of a mouse embryonic stem (ES) cells
contains on average 4.7 x 10(5) molecules.
-!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily.
{ECO:0000305}.
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EMBL; D13473; BAA02718.1; -; mRNA.
EMBL; D13803; BAA02961.1; -; mRNA.
EMBL; AK011242; BAB27489.1; -; mRNA.
EMBL; AK076468; BAC36357.1; -; mRNA.
EMBL; AK151157; BAE30162.1; -; mRNA.
EMBL; AK151177; BAE30179.1; -; mRNA.
EMBL; BC027384; AAH27384.1; -; mRNA.
CCDS; CCDS16590.1; -.
PIR; A48221; A48221.
RefSeq; NP_035364.1; NM_011234.4.
UniGene; Mm.330492; -.
ProteinModelPortal; Q08297; -.
SMR; Q08297; -.
BioGrid; 202564; 5.
CORUM; Q08297; -.
IntAct; Q08297; 1.
MINT; MINT-205669; -.
STRING; 10090.ENSMUSP00000028795; -.
ChEMBL; CHEMBL2034808; -.
iPTMnet; Q08297; -.
PhosphoSitePlus; Q08297; -.
EPD; Q08297; -.
MaxQB; Q08297; -.
PaxDb; Q08297; -.
PRIDE; Q08297; -.
Ensembl; ENSMUST00000028795; ENSMUSP00000028795; ENSMUSG00000027323.
GeneID; 19361; -.
KEGG; mmu:19361; -.
UCSC; uc008ltd.1; mouse.
CTD; 5888; -.
MGI; MGI:97890; Rad51.
eggNOG; KOG1433; Eukaryota.
eggNOG; COG0468; LUCA.
GeneTree; ENSGT00890000139508; -.
HOGENOM; HOG000227426; -.
HOVERGEN; HBG001504; -.
InParanoid; Q08297; -.
KO; K04482; -.
OMA; VGHTATF; -.
OrthoDB; EOG091G09QY; -.
PhylomeDB; Q08297; -.
TreeFam; TF101218; -.
Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-MMU-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
Reactome; R-MMU-5693579; Homologous DNA Pairing and Strand Exchange.
Reactome; R-MMU-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-MMU-912497; Meiotic Recombination.
PRO; PR:Q08297; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027323; -.
CleanEx; MM_RAD51; -.
ExpressionAtlas; Q08297; baseline and differential.
Genevisible; Q08297; MM.
GO; GO:0000785; C:chromatin; ISO:MGI.
GO; GO:0000793; C:condensed chromosome; IDA:MGI.
GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0000800; C:lateral element; IDA:MGI.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0000228; C:nuclear chromosome; ISS:UniProtKB.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0016605; C:PML body; ISO:MGI.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0035861; C:site of double-strand break; ISO:MGI.
GO; GO:0000795; C:synaptonemal complex; TAS:UniProtKB.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0070182; F:DNA polymerase binding; ISO:MGI.
GO; GO:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central.
GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
GO; GO:0000400; F:four-way junction DNA binding; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0000150; F:recombinase activity; IBA:GO_Central.
GO; GO:0003697; F:single-stranded DNA binding; IDA:MGI.
GO; GO:0043142; F:single-stranded DNA-dependent ATPase activity; ISS:UniProtKB.
GO; GO:0071312; P:cellular response to alkaloid; IMP:MGI.
GO; GO:0072757; P:cellular response to camptothecin; ISS:UniProtKB.
GO; GO:0072719; P:cellular response to cisplatin; IEA:Ensembl.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
GO; GO:0072711; P:cellular response to hydroxyurea; IMP:MGI.
GO; GO:0071479; P:cellular response to ionizing radiation; ISS:UniProtKB.
GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IMP:MGI.
GO; GO:0000730; P:DNA recombinase assembly; ISS:UniProtKB.
GO; GO:0006281; P:DNA repair; TAS:UniProtKB.
GO; GO:0006268; P:DNA unwinding involved in DNA replication; ISS:UniProtKB.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:MGI.
GO; GO:0036297; P:interstrand cross-link repair; ISS:UniProtKB.
GO; GO:0051321; P:meiotic cell cycle; IDA:MGI.
GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IEA:InterPro.
GO; GO:0051106; P:positive regulation of DNA ligation; ISO:MGI.
GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
GO; GO:0007131; P:reciprocal meiotic recombination; TAS:UniProtKB.
GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
GO; GO:0001932; P:regulation of protein phosphorylation; IMP:MGI.
GO; GO:0031297; P:replication fork processing; IMP:MGI.
GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IMP:MGI.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:1904631; P:response to glucoside; IEA:Ensembl.
GO; GO:0010212; P:response to ionizing radiation; IBA:GO_Central.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
GO; GO:0042148; P:strand invasion; IBA:GO_Central.
GO; GO:0000722; P:telomere maintenance via recombination; IGI:BHF-UCL.
GO; GO:0010833; P:telomere maintenance via telomere lengthening; IGI:BHF-UCL.
GO; GO:0032200; P:telomere organization; IMP:MGI.
CDD; cd01123; Rad51_DMC1_radA; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011941; DNA_recomb/repair_Rad51.
InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
InterPro; IPR016467; DNA_recomb/repair_RecA-like.
InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR033925; Rad51_DMC1_RadA.
InterPro; IPR020588; RecA_ATP-bd.
InterPro; IPR020587; RecA_monomer-monomer_interface.
Pfam; PF08423; Rad51; 1.
PIRSF; PIRSF005856; Rad51; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF47794; SSF47794; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR02239; recomb_RAD51; 1.
PROSITE; PS50162; RECA_2; 1.
PROSITE; PS50163; RECA_3; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
DNA damage; DNA recombination; DNA repair; DNA-binding;
Isopeptide bond; Mitochondrion; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q06609}.
CHAIN 2 339 DNA repair protein RAD51 homolog 1.
/FTId=PRO_0000122933.
DOMAIN 48 77 HhH.
NP_BIND 127 134 ATP. {ECO:0000250}.
REGION 184 257 Interaction with PALB2. {ECO:0000250}.
MOTIF 245 260 Nuclear export signal; masked by the
interaction with BRCA2.
{ECO:0000250|UniProtKB:Q06609}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q06609}.
MOD_RES 54 54 Phosphotyrosine; by ABL1.
{ECO:0000250|UniProtKB:Q06609}.
MOD_RES 309 309 Phosphothreonine; by CHEK1.
{ECO:0000250|UniProtKB:Q06609}.
CROSSLNK 58 58 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q06609}.
CROSSLNK 64 64 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q06609}.
SEQUENCE 339 AA; 36971 MW; CE631E2C246BA481 CRC64;
MAMQMQLEAS ADTSVEEESF GPQPISRLEQ CGINANDVKK LEEAGYHTVE AVAYAPKKEL
INIKGISEAK ADKILTEAAK LVPMGFTTAT EFHQRRSEII QITTGSKELD KLLQGGIETG
SITEMFGEFR TGKTQICHTL AVTCQLPIDR GGGEGKAMYI DTEGTFRPER LLAVAERYGL
SGSDVLDNVA YARGFNTDHQ TQLLYQASAM MVESRYALLI VDSATALYRT DYSGRGELSA
RQMHLARFLR MLLRLADEFG VAVVITNQVV AQVDGAAMFA ADPKKPIGGN IIAHASTTRL
YLRKGRGETR ICKIYDSPCL PEAEAMFAIN ADGVGDAKD


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EIAAB33657 Bos taurus,Bovine,DNA repair protein RAD51 homolog 1,RAD51
E0084Bo Bovine DNA repair protein RAD51 homolog 1(RAD51) ELISA Kit 96T
CSB-EL019263DO Dog DNA repair protein RAD51 homolog 1(RAD51) ELISA kit SpeciesDog 96T
YHB0431Mo Mouse DNA repair protein RAD51 homolog 1(RAD51) ELISA Kit 48T
CSB-EL019263BO Bovine DNA repair protein RAD51 homolog 1(RAD51) ELISA kit 96T
E1033Mo Mouse DNA repair protein RAD51 homolog 1(RAD51) ELISA Kit 48T
E0059Ch Chicken DNA repair protein RAD51 homolog 1(RAD51) ELISA Kit 96T
YHB0034Rb Rabbit DNA repair protein RAD51 homolog 1(RAD51) ELISA Kit 48T
E0050Rb Rabbit DNA repair protein RAD51 homolog 1(RAD51) ELISA Kit 48T


 

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