Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

DNA repair protein RAD50 (mRad50) (EC 3.6.-.-)

 RAD50_MOUSE             Reviewed;        1312 AA.
P70388; Q6PEB0; Q8C2T7; Q9CU59;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
25-APR-2018, entry version 136.
RecName: Full=DNA repair protein RAD50;
Short=mRad50;
EC=3.6.-.-;
Name=Rad50;
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] (ISOFORMS 1; 3 AND 4), PROTEIN SEQUENCE OF
113-120; 132-140; 175-202; 230-248; 295-310; 815-832; 840-845;
1012-1026 AND 1079-1089, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=8910585; DOI=10.1074/jbc.271.46.29255;
Kim K.K., Daud A.I., Wong S.C., Pajak L., Tsai S.-C., Wang H.,
Henzel W.J., Field L.J.;
"Mouse RAD50 has limited epitopic homology to p53 and is expressed in
the adult myocardium.";
J. Biol. Chem. 271:29255-29264(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-214 AND 443-743 (ISOFORM
1).
STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-722 (ISOFORM 2).
STRAIN=NMRI; TISSUE=Mammary tumor;
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).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=10377422; DOI=10.1073/pnas.96.13.7376;
Luo G., Yao M.S., Bender C.F., Mills M., Bladl A.R., Bradley A.,
Petrini J.H.J.;
"Disruption of mRad50 causes embryonic stem cell lethality, abnormal
embryonic development, and sensitivity to ionizing radiation.";
Proc. Natl. Acad. Sci. U.S.A. 96:7376-7381(1999).
[5]
FUNCTION, AND MUTAGENESIS OF LYS-22.
PubMed=12208847; DOI=10.1101/gad.1007902;
Bender C.F., Sikes M.L., Sullivan R., Huye L.E., Le Beau M.M.,
Roth D.B., Mirzoeva O.K., Oltz E.M., Petrini J.H.J.;
"Cancer predisposition and hematopoietic failure in Rad50(S/S) mice.";
Genes Dev. 16:2237-2251(2002).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635 AND THR-690, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
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).
-!- FUNCTION: Component of the MRN complex, which plays a central role
in double-strand break (DSB) repair, DNA recombination,
maintenance of telomere integrity and meiosis. The complex
possesses single-strand endonuclease activity and double-strand-
specific 3'-5' exonuclease activity, which are provided by MRE11.
RAD50 may be required to bind DNA ends and hold them in close
proximity. This could facilitate searches for short or long
regions of sequence homology in the recombining DNA templates, and
may also stimulate the activity of DNA ligases and/or restrict the
nuclease activity of MRE11 to prevent nucleolytic degradation past
a given point. The complex may also be required for DNA damage
signaling via activation of the ATM kinase. In telomeres the MRN
complex may modulate t-loop formation (By similarity).
{ECO:0000250, ECO:0000269|PubMed:10377422,
ECO:0000269|PubMed:12208847}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per homodimer. {ECO:0000250};
-!- SUBUNIT: Component of the MRN complex composed of two heterodimers
RAD50/MRE11 associated with a single NBN. Component of the BASC
complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM,
RAD50, MRE11 and NBN. Found in a complex with TERF2. Interacts
with RINT1. Interacts with BRCA1 via its N-terminal domain.
Interacts with DCLRE1C/Artemis. Interacts with MRNIP.
{ECO:0000250|UniProtKB:Q92878}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere
{ECO:0000250}. Note=Localizes to discrete nuclear foci after
treatment with genotoxic agents. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P70388-1; Sequence=Displayed;
Name=2;
IsoId=P70388-2; Sequence=VSP_012593;
Note=No experimental confirmation available.;
Name=3; Synonyms=3.1 kb splice variant;
IsoId=P70388-3; Sequence=VSP_012592;
Name=4; Synonyms=1.6 kb splice variant;
IsoId=P70388-4; Sequence=VSP_012594, VSP_012595;
-!- TISSUE SPECIFICITY: In adult, it is expressed at very low level in
most tissues, except in heart, lung and aorta. Expressed at high
level in testis. {ECO:0000269|PubMed:8910585}.
-!- DEVELOPMENTAL STAGE: Widely expressed. Expressed at higher level
in heart, liver and thymus from E18. By neonatal day 1.5, it
decreases in brain, liver, gut and skin, while it is expressed in
spleen. {ECO:0000269|PubMed:8910585}.
-!- DOMAIN: The zinc-hook, which separates the large intramolecular
coiled coil regions, contains 2 Cys residues that coordinate one
molecule of zinc with the help of the 2 Cys residues of the zinc-
hook of another RAD50 molecule, thereby forming a V-shaped
homodimer. The two heads of the homodimer, which constitute the
ATP-binding domain, interact with the MRE11 homodimer (By
similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Defects cause embryonic stem cell lethality,
abnormal embryonic development and sensitivity to ionizing
radiation. {ECO:0000269|PubMed:10377422}.
-!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U66887; AAC52894.1; -; mRNA.
EMBL; AK018001; BAB31030.1; -; mRNA.
EMBL; AK087982; BAC40074.1; -; mRNA.
EMBL; BC058180; AAH58180.1; -; mRNA.
CCDS; CCDS24684.1; -. [P70388-1]
PIR; T30845; T30845.
UniGene; Mm.4888; -.
ProteinModelPortal; P70388; -.
SMR; P70388; -.
DIP; DIP-46805N; -.
IntAct; P70388; 5.
MINT; P70388; -.
STRING; 10090.ENSMUSP00000020649; -.
iPTMnet; P70388; -.
PhosphoSitePlus; P70388; -.
EPD; P70388; -.
MaxQB; P70388; -.
PaxDb; P70388; -.
PeptideAtlas; P70388; -.
PRIDE; P70388; -.
UCSC; uc011xus.1; mouse. [P70388-2]
MGI; MGI:109292; Rad50.
eggNOG; KOG0962; Eukaryota.
eggNOG; COG0419; LUCA.
HOGENOM; HOG000090195; -.
HOVERGEN; HBG058033; -.
InParanoid; P70388; -.
PhylomeDB; P70388; -.
ChiTaRS; Rad50; mouse.
PRO; PR:P70388; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_RAD50; -.
GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
GO; GO:0030870; C:Mre11 complex; ISO:MGI.
GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
GO; GO:0000784; C:nuclear chromosome, telomeric region; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0045120; C:pronucleus; IDA:MGI.
GO; GO:0035861; C:site of double-strand break; ISO:MGI.
GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IEA:InterPro.
GO; GO:0003677; F:DNA binding; ISO:MGI.
GO; GO:0003691; F:double-stranded telomeric DNA binding; IBA:GO_Central.
GO; GO:0051880; F:G-quadruplex DNA binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030674; F:protein binding, bridging; ISO:MGI.
GO; GO:0043047; F:single-stranded telomeric DNA binding; IBA:GO_Central.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
GO; GO:0051276; P:chromosome organization; IMP:MGI.
GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IMP:MGI.
GO; GO:0032508; P:DNA duplex unwinding; ISO:MGI.
GO; GO:0006310; P:DNA recombination; ISO:MGI.
GO; GO:0006281; P:DNA repair; ISO:MGI.
GO; GO:0006302; P:double-strand break repair; ISO:MGI.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
GO; GO:1904354; P:negative regulation of telomere capping; ISO:MGI.
GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IBA:GO_Central.
GO; GO:0033674; P:positive regulation of kinase activity; ISO:MGI.
GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISO:MGI.
GO; GO:0032206; P:positive regulation of telomere maintenance; ISO:MGI.
GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:MGI.
GO; GO:0000019; P:regulation of mitotic recombination; ISO:MGI.
GO; GO:0016233; P:telomere capping; IBA:GO_Central.
GO; GO:0000722; P:telomere maintenance via recombination; IBA:GO_Central.
GO; GO:0007004; P:telomere maintenance via telomerase; ISO:MGI.
GO; GO:0031860; P:telomeric 3' overhang formation; ISO:MGI.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR038729; Rad50/SbcC_AAA.
InterPro; IPR004584; Rad50_eukaryotes.
InterPro; IPR013134; Zn_hook_RAD50.
Pfam; PF13476; AAA_23; 1.
Pfam; PF04423; Rad50_zn_hook; 1.
SUPFAM; SSF52540; SSF52540; 3.
TIGRFAMs; TIGR00606; rad50; 1.
PROSITE; PS51131; ZN_HOOK; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Cell cycle;
Chromosome; Coiled coil; Complete proteome; Direct protein sequencing;
DNA damage; DNA repair; Hydrolase; Meiosis; Metal-binding;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Telomere; Zinc.
CHAIN 1 1312 DNA repair protein RAD50.
/FTId=PRO_0000138642.
DOMAIN 635 734 Zinc-hook. {ECO:0000255|PROSITE-
ProRule:PRU00471}.
NP_BIND 36 43 ATP. {ECO:0000255}.
COILED 200 532 {ECO:0000255}.
COILED 635 673 {ECO:0000255}.
COILED 706 734 {ECO:0000255}.
COILED 776 942 {ECO:0000255}.
COILED 1043 1075 {ECO:0000255}.
COMPBIAS 1201 1238 Ala/Asp-rich (DA-box).
METAL 681 681 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00471}.
METAL 684 684 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00471}.
MOD_RES 635 635 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 690 690 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 959 959 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q92878}.
VAR_SEQ 1 886 Missing (in isoform 3).
{ECO:0000303|PubMed:8910585}.
/FTId=VSP_012592.
VAR_SEQ 485 545 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012593.
VAR_SEQ 485 496 ERELSKAEKNSS -> IYFLELVRWLSG (in isoform
4). {ECO:0000303|PubMed:8910585}.
/FTId=VSP_012594.
VAR_SEQ 497 1312 Missing (in isoform 4).
{ECO:0000303|PubMed:8910585}.
/FTId=VSP_012595.
MUTAGEN 22 22 K->M: In Rad50S; hypomorphic allele that
induces growth defects and cancer
predisposition. Homozygous individuals
die with complete bone marrow depletion
as a result of progressive hematopoietic
stem cell failure.
{ECO:0000269|PubMed:12208847}.
CONFLICT 97 97 H -> Q (in Ref. 2; BAB31030).
{ECO:0000305}.
CONFLICT 200 200 G -> V (in Ref. 3; AAH58180).
{ECO:0000305}.
CONFLICT 474 474 I -> V (in Ref. 2; BAC40074).
{ECO:0000305}.
CONFLICT 718 718 E -> A (in Ref. 2; BAC40074).
{ECO:0000305}.
CONFLICT 719 719 L -> K (in Ref. 3; AAH58180).
{ECO:0000305}.
SEQUENCE 1312 AA; 153488 MW; 4AF9AF9AD9E1D7A2 CRC64;
MSRIEKMSIL GVRSFGIEDK DKQIISFFSP LTILVGPNGA GKTTIIECLK YICTGDFPPG
TKGNTFVHDP KVAQETDVRA QIRLQFRDVN GEMVAVHRSM LCSQKNKKTE FKTLEGVITR
MKHGEKVSLS SKCAEIDREM ISCLGVSKSV LNNVIFCHQE DSNWPLSEGK ALKQKFDEIF
SATRYIKALD TLRQVRQTQG QKVKECQTEL KYLKQNKEKA CEIRDQITSK EAQLASSQEI
VRSYEDELEP LKNRLKEIEH NLSKIMKLDN EIKALESRKK QMEKDNSELE QKMEKVFQGT
DEQLNDLYHN HQRTVREKER RLVDCQRELE KLNKEARLLN QEKAELLVEQ GRLQLQADRH
QEHIRARDSL IQSLATHLEL DGFERGPFSE RQIKNFHELV KERQEREAKT ASQLLSDLTD
KEALKQRQLD ELRDRKSGLG RTIELKTEIL TKKQSELRHV RSELQQLEGS SDRILELDQE
LTKAERELSK AEKNSSIETL KAEVMSLQNE KADLDRSLRK LDQEMEQLNH HTTTRTQMEM
LTKDKTDKDE QIRKIKSRHS DELTSLLGYF PNKKQLEDWL HSKSKEINQT RDRLAKLNKE
LASAEQNKNH INNELKKKEE QLSSYEDKLF DVCGSQDLES DLGRLKEEIE KSSKQRAMLA
GATAVYSQFI TQLTDENQSC CPVCQRVFQT EAELQEVISD LQSKLRLAPD KLKSTESELK
KKERRRDEML GLVPVRQSII DLKEKEIPEL RNRLQSVNRD IQRLKNDIEE QETLLGTIMP
EEESAKVCLT DVTIMERFQM ELKDVERKIA QQAAKLQGVD LDRTVQQVNQ EKQEKQHRLD
TVTSKIELNR KLIQDQQEQI QHLKSKTNEL KSEKLQIATN LQRRQQMEEQ SVELSTEVQS
LNREIKDAKE QISPLETALE KLQQEKEELI HRKHTSNKMA QDKINDIKEK VKNIHGYMKD
IENYIQDGKD DYKKQKETEL NGVAVQLNEC EKHREKINKD MGTMRQDIDT QKIQERWLQD
NLTLRKRRDE LKEVEEEPKQ HLKEMGQMQV LQMKNEHQKL EENIDTIKRN HSLALGRQKG
YEDEILHFKK ELREPQFRDA EEKYREMMIV MRTTELVNKD LDIYYKTLDQ AIMKFHSMKM
EEINKIIRDL WRSTYRGQDI EYIEIRSDAD ENVSASDKRR NYNYRVVMLK GDTALDMRGR
CSAGQKVLAS LIIRLALAET FCLNCGILAL DEPTTNLDRE NIESLAHALV EIIKSRSQQR
NFQLLVITHD EDFVELLGRS EYVEKFYRVK KNMDQCSEIV KCSISSLGSY VH


Related products :

Catalog number Product name Quantity
EIAAB33654 DNA repair protein RAD50,Mouse,mRad50,Mus musculus,Rad50
DL-RAD50-Hu Human DNA Repair Protein RAD50 (RAD50) ELISA Kit 96T
DL-RAD50-Mu Mouse DNA Repair Protein RAD50 (RAD50) ELISA Kit 96T
EIAAB33656 DNA repair protein RAD50,Homo sapiens,hRAD50,Human,RAD50
RAD50_MOUSE ELISA Kit FOR DNA repair protein RAD50; organism: Mouse; gene name: Rad50 96T
RAD50_HUMAN ELISA Kit FOR DNA repair protein RAD50; organism: Human; gene name: RAD50 96T
E99111Mu ELISA Kit for DNA Repair Protein RAD50 (RAD50) Organism: Mus musculus (Mouse) 96T
SEK111Hu ELISA Kit for DNA Repair Protein RAD50 (RAD50) Homo sapiens (Human) 96T
SEK111Mu ELISA Kit for DNA Repair Protein RAD50 (RAD50) Mus musculus (Mouse) 96T
CSB-EL019262MO Mouse DNA repair protein RAD50(RAD50) ELISA kit SpeciesMouse 96T
CSB-EL019262HU Human DNA repair protein RAD50(RAD50) ELISA kit SpeciesHuman 96T
CSB-EL019262HU Human DNA repair protein RAD50(RAD50) ELISA kit 96T
CSB-EL019262MO Mouse DNA repair protein RAD50(RAD50) ELISA kit 96T
CSB-EL019262RA Rat DNA repair protein RAD50(RAD50) ELISA kit SpeciesRat 96T
EIAAB33655 DNA repair protein RAD50,Rad50,Rat,Rattus norvegicus
201-02-1074 Mouse DNA Repair Protein RAD50(RAD50)ELISA Kit 96T
P99111Hu01 DNA Repair Protein RAD50 (RAD50) Organism: Homo sapiens (Human) Source: Escherichia coli 100ug
E99111Mu ELISA Kit for DNA Repair Protein RAD50 (RAD50), Organism Mus musculus (Mouse), Detection range 0.312-20ng_mL 96T/Kit
P99111Hu01 DNA Repair Protein RAD50 (RAD50) Organism: Homo sapiens (Human) Source: Escherichia coli 50ug
P99111Hu01 DNA Repair Protein RAD50 (RAD50) Organism: Homo sapiens (Human) Source: Escherichia coli 10ug
E99111Mu ELISA Kit for DNA Repair Protein RAD50 (RAD50) 96T/Kit
CSB-EL019262RA Rat DNA repair protein RAD50(RAD50) ELISA kit 96T
A99111Hu01 Antibody to DNA Repair Protein RAD50 (RAD50) Organism: Homo sapiens (Human) Type: Polyclonal Source: Rabbit 100ug
A99111Hu01 Antibody to DNA Repair Protein RAD50 (RAD50) Organism: Homo sapiens (Human) Type: Polyclonal Source: Rabbit 50ug
A99111Hu01-B Biotin-linked Antibody to DNA Repair Protein RAD50 (RAD50); Reactivity: Homo sapiens (Human) Clonality: Polyclonal Source: Rabbit 50ug


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur