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Mast/stem cell growth factor receptor Kit (SCFR) (EC 2.7.10.1) (Proto-oncogene c-Kit) (Tyrosine-protein kinase Kit) (CD antigen CD117)

 KIT_MOUSE               Reviewed;         979 AA.
P05532; Q61415; Q61416; Q61417; Q6LEE9; Q6QJB7; Q6QJB8; Q7TS86;
Q8C8K9;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
19-OCT-2011, sequence version 3.
30-AUG-2017, entry version 192.
RecName: Full=Mast/stem cell growth factor receptor Kit;
Short=SCFR;
EC=2.7.10.1;
AltName: Full=Proto-oncogene c-Kit;
AltName: Full=Tyrosine-protein kinase Kit;
AltName: CD_antigen=CD117;
Flags: Precursor;
Name=Kit; Synonyms=Sl;
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] (ISOFORM 2), AND VARIANT GLU-207.
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=2456920;
Qiu F., Ray P., Brown K., Barker P.E., Jhanwar S., Ruddle F.H.,
Besmer P.;
"Primary structure of c-kit: relationship with the CSF-1/PDGF receptor
kinase family -- oncogenic activation of v-kit involves deletion of
extracellular domain and C-terminus.";
EMBO J. 7:1003-1011(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
PubMed=1709486; DOI=10.1093/nar/19.6.1267;
Hayashi S., Kunisada T., Ogawa M., Yamaguchi K., Nishikawa S.;
"Exon skipping by mutation of an authentic splice site of c-kit gene
in W/W mouse.";
Nucleic Acids Res. 19:1267-1271(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3), AND TISSUE
SPECIFICITY.
STRAIN=ICR;
PubMed=1378413; DOI=10.1016/0012-1606(92)90172-D;
Rossi P., Marziali G., Albanesi C., Charlesworth A., Geremia R.,
Sorrentino V.;
"A novel c-kit transcript, potentially encoding a truncated receptor,
originates within a kit gene intron in mouse spermatids.";
Dev. Biol. 152:203-207(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND MUTAGENESIS OF PHE-860.
STRAIN=C57BL/6J;
PubMed=15731517; DOI=10.1534/genetics.104.027177;
Ruan H.B., Zhang N., Gao X.;
"Identification of a novel point mutation of mouse proto-oncogene c-
kit through N-ethyl-N-nitrosourea mutagenesis.";
Genetics 169:819-831(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and 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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
STRAIN=BALB/cJ;
PubMed=7682073; DOI=10.1006/bbrc.1993.1301;
Yasuda H., Galli S.J., Geissler E.N.;
"Cloning and functional analysis of the mouse c-kit promoter.";
Biochem. Biophys. Res. Commun. 191:893-901(1993).
[8]
FUNCTION, AND SUBUNIT.
PubMed=1698611;
Tan J.C., Buck J., Levi E., Besmer P.;
"Candidate ligand for the c-kit transmembrane kinase receptor: KL, a
fibroblast derived growth factor stimulates mast cells and erythroid
progenitors.";
EMBO J. 9:3287-3294(1990).
[9]
FUNCTION IN ACTIVATION OF PLCG1, INTERACTION WITH PLCG1, ALTERNATIVE
SPLICING, PHOSPHORYLATION, GLYCOSYLATION, AND CHARACTERIZATION OF
VARIANTS W37 LYS-586 AND W41 MET-835.
PubMed=1714377;
Reith A.D., Ellis C., Lyman S.D., Anderson D.M., Williams D.E.,
Bernstein A., Pawson T.;
"Signal transduction by normal isoforms and W mutant variants of the
Kit receptor tyrosine kinase.";
EMBO J. 10:2451-2459(1991).
[10]
INTERACTION WITH PIK3R1, AND FUNCTION IN PHOSPHORYLATION OF PIK3R1.
PubMed=7509796;
Serve H., Hsu Y.C., Besmer P.;
"Tyrosine residue 719 of the c-kit receptor is essential for binding
of the P85 subunit of phosphatidylinositol (PI) 3-kinase and for c-
kit-associated PI 3-kinase activity in COS-1 cells.";
J. Biol. Chem. 269:6026-6030(1994).
[11]
UBIQUITINATION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY,
PHOSPHORYLATION AT TYR-825, INTERACTION WITH PIK3R1, CHARACTERIZATION
OF VARIANT W42 ASN-794, MUTAGENESIS OF TYR-723, AND TISSUE
SPECIFICITY.
PubMed=7527401;
Yee N.S., Hsiau C.W., Serve H., Vosseller K., Besmer P.;
"Mechanism of down-regulation of c-kit receptor. Roles of receptor
tyrosine kinase, phosphatidylinositol 3'-kinase, and protein kinase
C.";
J. Biol. Chem. 269:31991-31998(1994).
[12]
ALTERNATIVE SPLICING, AND FUNCTION IN ACTIVATION OF PLCG1.
PubMed=9722617; DOI=10.1083/jcb.142.4.1063;
Sette C., Bevilacqua A., Geremia R., Rossi P.;
"Involvement of phospholipase Cgamma1 in mouse egg activation induced
by a truncated form of the C-kit tyrosine kinase present in
spermatozoa.";
J. Cell Biol. 142:1063-1074(1998).
[13]
INTERACTION WITH PTPN6/SHP-1 AND PTPN11/SHP-2, FUNCTION IN
PHOSPHORYLATION OF PTPN6/SHP-1, AND MUTAGENESIS OF TYR-571 AND
TYR-573.
PubMed=9528781; DOI=10.1128/MCB.18.4.2089;
Kozlowski M., Larose L., Lee F., Le D.M., Rottapel R.,
Siminovitch K.A.;
"SHP-1 binds and negatively modulates the c-Kit receptor by
interaction with tyrosine 569 in the c-Kit juxtamembrane domain.";
Mol. Cell. Biol. 18:2089-2099(1998).
[14]
REVIEW ON ROLE IN SPERMATOGENESIS AND FERTILITY.
PubMed=12558531; DOI=10.1046/j.1439-0272.2003.00539.x;
Rossi P., Dolci S., Sette C., Geremia R.;
"Molecular mechanisms utilized by alternative c-kit gene products in
the control of spermatogonial proliferation and sperm-mediated egg
activation.";
Andrologia 35:71-78(2003).
[15]
INTERACTION WITH FES/FPS.
PubMed=17595334; DOI=10.1182/blood-2007-02-076471;
Voisset E., Lopez S., Dubreuil P., De Sepulveda P.;
"The tyrosine kinase FES is an essential effector of KITD816V
proliferation signal.";
Blood 110:2593-2599(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-571; TYR-573; TYR-706
AND TYR-938, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[17]
FUNCTION IN MAST CELL MIGRATION, AND IN SIGNALING VIA FYN.
PubMed=18725415; DOI=10.1074/jbc.M804077200;
Samayawardhena L.A., Pallen C.J.;
"Protein-tyrosine phosphatase alpha regulates stem cell factor-
dependent c-Kit activation and migration of mast cells.";
J. Biol. Chem. 283:29175-29185(2008).
[18]
ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=18447649; DOI=10.1089/scd.2007.0101;
Zayas J., Spassov D.S., Nachtman R.G., Jurecic R.;
"Murine hematopoietic stem cells and multipotent progenitors express
truncated intracellular form of c-kit receptor.";
Stem Cells Dev. 17:343-353(2008).
[19]
FUNCTION IN MAST CELL DEGRANULATION.
PubMed=21037083; DOI=10.2353/ajpath.2010.100369;
Chen S., Burgin S., McDaniel A., Li X., Yuan J., Chen M., Khalaf W.,
Clapp D.W., Yang F.C.;
"Nf1-/- Schwann cell-conditioned medium modulates mast cell
degranulation by c-Kit-mediated hyperactivation of
phosphatidylinositol 3-kinase.";
Am. J. Pathol. 177:3125-3132(2010).
[20]
INTERACTION WITH IL1RL1 AND IL1RAP, AND SUBUNIT.
PubMed=20200353; DOI=10.1182/blood-2009-10-247411;
Drube S., Heink S., Walter S., Loehn T., Grusser M., Gerbaulet A.,
Berod L., Schons J., Dudeck A., Freitag J., Grotha S., Reich D.,
Rudeschko O., Norgauer J., Hartmann K., Roers A., Kamradt T.;
"The receptor tyrosine kinase c-Kit controls IL-33 receptor signaling
in mast cells.";
Blood 115:3899-3906(2010).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Lung, 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).
[22]
VARIANT GLU-207.
Jawad-Alam J.;
Unpublished observations (APR-2010).
[23]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 25-314 IN COMPLEX WITH
KITLG/SCF, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-296 AND ASN-303.
PubMed=17255936; DOI=10.1038/sj.emboj.7601545;
Liu H., Chen X., Focia P.J., He X.;
"Structural basis for stem cell factor-KIT signaling and activation of
class III receptor tyrosine kinases.";
EMBO J. 26:891-901(2007).
[24]
VARIANT W42 ASN-794.
PubMed=1688471; DOI=10.1126/science.1688471;
Tan J.C., Nocka K., Ray P., Traktman P., Besmer P.;
"The dominant W42 spotting phenotype results from a missense mutation
in the c-kit receptor kinase.";
Science 247:209-212(1990).
[25]
VARIANTS W37 LYS-586; WV MET-664 AND W41 MET-835.
PubMed=1693331;
Nocka K., Tan J.C., Chiu E., Chu T.Y., Ray P., Traktman P., Besmer P.;
"Molecular bases of dominant negative and loss of function mutations
at the murine c-kit/white spotting locus: W37, Wv, W41 and W.";
EMBO J. 9:1805-1813(1990).
-!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface
receptor for the cytokine KITLG/SCF and plays an essential role in
the regulation of cell survival and proliferation, hematopoiesis,
stem cell maintenance, gametogenesis, mast cell development,
migration and function, and in melanogenesis. In response to
KITLG/SCF binding, KIT can activate several signaling pathways.
Phosphorylates PIK3R1, PLCG1, SH2B2/APS and CBL. Activates the
AKT1 signaling pathway by phosphorylation of PIK3R1, the
regulatory subunit of phosphatidylinositol 3-kinase. Activated KIT
also transmits signals via GRB2 and activation of RAS, RAF1 and
the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation
of STAT family members STAT1, STAT3, STAT5A and STAT5B. Activation
of PLCG1 leads to the production of the cellular signaling
molecules diacylglycerol and inositol 1,4,5-trisphosphate. KIT
signaling is modulated by protein phosphatases, and by rapid
internalization and degradation of the receptor. Activated KIT
promotes phosphorylation of the protein phosphatases PTPN6/SHP-1
and PTPRU, and of the transcription factors STAT1, STAT3, STAT5A
and STAT5B. Promotes phosphorylation of PIK3R1, CBL, CRK (isoform
Crk-II), LYN, MAPK1/ERK2 and/or MAPK3/ERK1, PLCG1, SRC and SHC1.
{ECO:0000269|PubMed:1698611, ECO:0000269|PubMed:1714377,
ECO:0000269|PubMed:18725415, ECO:0000269|PubMed:21037083,
ECO:0000269|PubMed:7509796, ECO:0000269|PubMed:9528781,
ECO:0000269|PubMed:9722617}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:7527401}.
-!- ENZYME REGULATION: Present in an inactive conformation in the
absence of bound ligand. KITLG/SCF binding leads to dimerization
and activation by autophosphorylation.
-!- SUBUNIT: Monomer in the absence of bound KITLG/SCF. Homodimer in
the presence of bound KITLG/SCF, forming a heterotetramer with two
KITLG/SCF molecules. Interacts (via phosphorylated tyrosine
residues) with the adapter proteins GRB2 and GRB7 (via SH2
domain), and SH2B2/APS. Interacts (via C-terminus) with MPDZ (via
the tenth PDZ domain). Interacts (via phosphorylated tyrosine
residues) with the protein phosphatases PTPN6/SHP-1 (via SH2
domain), PTPN11/SHP-2 (via SH2 domain) and PTPRU. Interacts with
DOK1 and TEC (By similarity). Interacts with the protein kinase
FES/FPS. Interacts with PLCG1. Interacts (via phosphorylated
tyrosine residues) with PIK3R1 and PIK3 catalytic subunit.
Interacts (KITLG/SCF-bound) with IL1RL1. Interacts with IL1RAP
(independent of stimulation with KITLG/SCF). A mast cell-specific
KITLG/SCF-induced interleukin-33 signaling complex contains
IL1RL1, IL1RAP, KIT and MYD88. {ECO:0000250|UniProtKB:P10721,
ECO:0000269|PubMed:1698611, ECO:0000269|PubMed:1714377,
ECO:0000269|PubMed:17255936, ECO:0000269|PubMed:17595334,
ECO:0000269|PubMed:20200353, ECO:0000269|PubMed:7509796,
ECO:0000269|PubMed:7527401, ECO:0000269|PubMed:9528781}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Single-pass type I
membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Note=Detected in the
cytoplasm of spermatozoa, especially in the equatorial and
subacrosomal region of the sperm head. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=GNNK(+), KitA(+);
IsoId=P05532-1; Sequence=Displayed;
Name=2; Synonyms=GNNK(-), Kit(+);
IsoId=P05532-2; Sequence=VSP_041870;
Name=3; Synonyms=Tr-kit, Truncated;
IsoId=P05532-3; Sequence=VSP_041868, VSP_041869;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are detected in bone
marrow cells, spermatogonia and spermatocytes, but not in round
spermatids, elongating spermatids and spermatozoa. Isoform 3 is
detected in round spermatids, elongating spermatids and
spermatozoa, but not in spermatogonia and spermatocytes (at
protein level). Isoform 1 is widely expressed and detected in
fetal liver and bone marrow. Isoform 3 is detected in bone marrow
cells enriched in hematopoietic stem cells.
{ECO:0000269|PubMed:1378413, ECO:0000269|PubMed:18447649,
ECO:0000269|PubMed:7527401}.
-!- PTM: Ubiquitinated by SOCS6. KIT is rapidly ubiquitinated after
autophosphorylation induced by KITLG/SCF binding, leading to
internalization and degradation (By similarity). {ECO:0000250}.
-!- PTM: Autophosphorylated on tyrosine residues. KITLG/SCF binding
promotes autophosphorylation of isoform 1 and isoform 2. Isoform 1
shows low levels of tyrosine phosphorylation in the absence of
added KITLG/SCF, while isoform 2 requires stimulation by KITLG/SCF
for phosphorylation (in vitro). Phosphorylation of Tyr-573 is
required for interaction with PTPN6/SHP-1. Phosphorylation of Tyr-
571 is required for interaction with PTPN11/SHP-2. Phosphorylated
tyrosine residues are important for interaction with specific
binding partners. {ECO:0000269|PubMed:1714377,
ECO:0000269|PubMed:7527401}.
-!- DISEASE: Note=Defects in Kit are the cause of the white-spotting
phenotype (W). White-spotting variants induces severe effects on
pigmentation, gametogenesis and hematopoiesis. Mice homozygous for
W42 die perinatally of macrocytic anemia.
-!- MISCELLANEOUS: Numerous proteins are phosphorylated in response to
KIT signaling, but it is not evident to determine which are
directly phosphorylated by KIT under in vivo conditions.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSF-1/PDGF receptor subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
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EMBL; Y00864; CAA68772.1; -; mRNA.
EMBL; AK046795; BAC32872.1; -; mRNA.
EMBL; X65997; CAA46798.1; -; mRNA.
EMBL; X65998; CAA46799.1; ALT_SEQ; Genomic_DNA.
EMBL; X65998; CAA46800.1; -; Genomic_DNA.
EMBL; AY536430; AAS45606.1; -; mRNA.
EMBL; AY536431; AAS45607.1; -; mRNA.
EMBL; AC013622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC115853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC052457; AAH52457.1; -; mRNA.
EMBL; BC075716; AAH75716.1; -; mRNA.
EMBL; L11358; AAA37420.1; -; Genomic_DNA.
CCDS; CCDS51525.1; -. [P05532-1]
CCDS; CCDS80302.1; -. [P05532-2]
PIR; A44876; A44876.
PIR; S00474; TVMSKT.
PIR; S24667; S24667.
PIR; S34435; S34435.
RefSeq; NP_001116205.1; NM_001122733.1. [P05532-1]
RefSeq; NP_066922.2; NM_021099.3. [P05532-2]
UniGene; Mm.247073; -.
PDB; 2O26; X-ray; 2.50 A; U/W/X/Y=25-314.
PDBsum; 2O26; -.
ProteinModelPortal; P05532; -.
SMR; P05532; -.
BioGrid; 200957; 18.
DIP; DIP-59622N; -.
IntAct; P05532; 3.
STRING; 10090.ENSMUSP00000005815; -.
BindingDB; P05532; -.
ChEMBL; CHEMBL2034798; -.
iPTMnet; P05532; -.
PhosphoSitePlus; P05532; -.
MaxQB; P05532; -.
PaxDb; P05532; -.
PRIDE; P05532; -.
Ensembl; ENSMUST00000005815; ENSMUSP00000005815; ENSMUSG00000005672. [P05532-1]
Ensembl; ENSMUST00000144270; ENSMUSP00000116465; ENSMUSG00000005672. [P05532-2]
GeneID; 16590; -.
KEGG; mmu:16590; -.
UCSC; uc008xug.2; mouse. [P05532-1]
UCSC; uc012dxj.1; mouse. [P05532-2]
CTD; 3815; -.
MGI; MGI:96677; Kit.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
HOGENOM; HOG000112008; -.
HOVERGEN; HBG004335; -.
InParanoid; P05532; -.
KO; K05091; -.
OMA; PTFKQIV; -.
TreeFam; TF325768; -.
BRENDA; 2.7.10.1; 3474.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-1433557; Signaling by SCF-KIT.
Reactome; R-MMU-1433559; Regulation of KIT signaling.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
ChiTaRS; Kit; mouse.
EvolutionaryTrace; P05532; -.
PRO; PR:P05532; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000005672; -.
CleanEx; MM_KIT; -.
Genevisible; P05532; MM.
GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0042629; C:mast cell granule; IEA:GOC.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019955; F:cytokine binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0004716; F:signal transducer, downstream of receptor, with protein tyrosine kinase activity; IEA:InterPro.
GO; GO:0005020; F:stem cell factor receptor activity; IDA:MGI.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; ISO:MGI.
GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; TAS:MGI.
GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IDA:UniProtKB.
GO; GO:0006935; P:chemotaxis; TAS:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
GO; GO:0002371; P:dendritic cell cytokine production; IMP:UniProtKB.
GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:UniProtKB.
GO; GO:0048066; P:developmental pigmentation; IMP:MGI.
GO; GO:0048565; P:digestive tract development; IMP:UniProtKB.
GO; GO:0035234; P:ectopic germ cell programmed cell death; IGI:MGI.
GO; GO:0035162; P:embryonic hemopoiesis; IMP:UniProtKB.
GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
GO; GO:0038162; P:erythropoietin-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0038093; P:Fc receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007281; P:germ cell development; TAS:MGI.
GO; GO:0008354; P:germ cell migration; IEA:Ensembl.
GO; GO:0006687; P:glycosphingolipid metabolic process; IMP:MGI.
GO; GO:0035701; P:hematopoietic stem cell migration; IMP:MGI.
GO; GO:0030097; P:hemopoiesis; IMP:MGI.
GO; GO:0002327; P:immature B cell differentiation; IMP:UniProtKB.
GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IDA:MGI.
GO; GO:0038109; P:Kit signaling pathway; ISO:MGI.
GO; GO:0030032; P:lamellipodium assembly; IDA:UniProtKB.
GO; GO:0002320; P:lymphoid progenitor cell differentiation; IGI:MGI.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0002551; P:mast cell chemotaxis; ISO:MGI.
GO; GO:0032762; P:mast cell cytokine production; ISS:UniProtKB.
GO; GO:0043303; P:mast cell degranulation; ISS:UniProtKB.
GO; GO:0060374; P:mast cell differentiation; IMP:UniProtKB.
GO; GO:0035855; P:megakaryocyte development; IMP:UniProtKB.
GO; GO:0097326; P:melanocyte adhesion; IDA:UniProtKB.
GO; GO:0030318; P:melanocyte differentiation; IMP:UniProtKB.
GO; GO:0097324; P:melanocyte migration; IMP:UniProtKB.
GO; GO:0002573; P:myeloid leukocyte differentiation; IMP:MGI.
GO; GO:0002318; P:myeloid progenitor cell differentiation; IGI:MGI.
GO; GO:0043069; P:negative regulation of programmed cell death; IMP:MGI.
GO; GO:0001541; P:ovarian follicle development; IMP:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0043473; P:pigmentation; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IGI:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
GO; GO:0046427; P:positive regulation of JAK-STAT cascade; ISO:MGI.
GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IGI:MGI.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IEA:Ensembl.
GO; GO:0031274; P:positive regulation of pseudopodium assembly; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; ISO:MGI.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
GO; GO:1905065; P:positive regulation of vascular smooth muscle cell differentiation; ISO:MGI.
GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0008360; P:regulation of cell shape; IDA:UniProtKB.
GO; GO:0048070; P:regulation of developmental pigmentation; IMP:MGI.
GO; GO:0009314; P:response to radiation; IMP:MGI.
GO; GO:0048103; P:somatic stem cell division; IEA:Ensembl.
GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
GO; GO:0007286; P:spermatid development; IMP:MGI.
GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
GO; GO:0030217; P:T cell differentiation; IMP:UniProtKB.
GO; GO:0008542; P:visual learning; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR027263; SCGF_receptor.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
Pfam; PF00047; ig; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF500951; SCGF_recepter; 1.
SMART; SM00409; IG; 4.
SMART; SM00408; IGc2; 3.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 4.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Complete proteome; Cytoplasm; Disease mutation; Disulfide bond;
Glycoprotein; Immunoglobulin domain; Kinase; Magnesium; Membrane;
Metal-binding; Nucleotide-binding; Phosphoprotein; Proto-oncogene;
Receptor; Reference proteome; Repeat; Signal; Transferase;
Transmembrane; Transmembrane helix; Tyrosine-protein kinase;
Ubl conjugation.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 979 Mast/stem cell growth factor receptor
Kit.
/FTId=PRO_0000016755.
TOPO_DOM 25 527 Extracellular. {ECO:0000255}.
TRANSMEM 528 548 Helical. {ECO:0000255}.
TOPO_DOM 549 979 Cytoplasmic. {ECO:0000255}.
DOMAIN 31 117 Ig-like C2-type 1.
DOMAIN 126 210 Ig-like C2-type 2.
DOMAIN 217 315 Ig-like C2-type 3.
DOMAIN 324 417 Ig-like C2-type 4.
DOMAIN 420 514 Ig-like C2-type 5.
DOMAIN 592 939 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 599 606 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 674 680 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 571 573 Important for interaction with
phosphotyrosine-binding proteins.
{ECO:0000250}.
ACT_SITE 794 794 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
METAL 571 571 Magnesium. {ECO:0000250}.
METAL 799 799 Magnesium. {ECO:0000250}.
METAL 812 812 Magnesium. {ECO:0000250}.
BINDING 626 626 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 798 798 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 938 938 Important for interaction with
phosphotyrosine-binding proteins.
{ECO:0000250}.
MOD_RES 550 550 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 556 556 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 571 571 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 573 573 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 706 706 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 720 720 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 723 723 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P10721}.
MOD_RES 732 732 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 743 743 Phosphoserine; by PKC/PRKCA.
{ECO:0000250|UniProtKB:P10721}.
MOD_RES 748 748 Phosphoserine; by PKC/PRKCA.
{ECO:0000250|UniProtKB:P10721}.
MOD_RES 823 823 Phosphoserine.
{ECO:0000250|UniProtKB:P10721}.
MOD_RES 825 825 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:7527401}.
MOD_RES 893 893 Phosphoserine.
{ECO:0000250|UniProtKB:P10721}.
MOD_RES 902 902 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P10721}.
MOD_RES 938 938 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 962 962 Phosphoserine.
{ECO:0000250|UniProtKB:P10721}.
CARBOHYD 146 146 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17255936}.
CARBOHYD 303 303 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17255936}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 355 355 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 370 370 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 466 466 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 489 489 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 58 98 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17255936}.
DISULFID 137 187 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17255936}.
DISULFID 152 184 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17255936}.
DISULFID 234 293 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17255936}.
DISULFID 431 494 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 1 12 MRGARGAWDLLC -> MAVAVFPFLPQQ (in isoform
3). {ECO:0000303|PubMed:1378413}.
/FTId=VSP_041868.
VAR_SEQ 13 789 Missing (in isoform 3).
{ECO:0000303|PubMed:1378413}.
/FTId=VSP_041869.
VAR_SEQ 512 515 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15731517,
ECO:0000303|PubMed:2456920}.
/FTId=VSP_041870.
VARIANT 207 207 A -> E (loss-of-function mutation
abolishing ligand binding).
{ECO:0000269|PubMed:2456920,
ECO:0000269|Ref.22}.
VARIANT 586 586 E -> K (in W37 spotting; impaired protein
stability and loss of kinase activity).
{ECO:0000269|PubMed:1693331,
ECO:0000269|PubMed:1714377}.
VARIANT 664 664 T -> M (in Wv spotting).
{ECO:0000269|PubMed:1693331}.
VARIANT 794 794 D -> N (in W42 spotting; loss of kinase
activity and impaired internalization
after exposure to KITLG/SCF).
{ECO:0000269|PubMed:1688471,
ECO:0000269|PubMed:7527401}.
VARIANT 835 835 V -> M (in W41 spotting; decreased kinase
activity). {ECO:0000269|PubMed:1693331,
ECO:0000269|PubMed:1714377}.
MUTAGEN 571 571 Y->F: Abolishes interaction with
PTPN11/SHP-2.
{ECO:0000269|PubMed:9528781}.
MUTAGEN 573 573 Y->F: Abolishes interaction with
PTPN6/SHP-1.
{ECO:0000269|PubMed:9528781}.
MUTAGEN 573 573 Missing: Abolishes interaction with
PTPN6/SHP-1.
{ECO:0000269|PubMed:9528781}.
MUTAGEN 723 723 Y->F: Abolishes interaction with PIK3R1.
{ECO:0000269|PubMed:7527401}.
MUTAGEN 860 860 F->S: Mice display white fur, hearing
loss, anemia and mast cell deficiency,
plus sterility in both males and females.
{ECO:0000269|PubMed:15731517}.
CONFLICT 551 551 L -> F (in Ref. 6; AAH52457).
{ECO:0000305}.
CONFLICT 781 781 G -> A (in Ref. 1; CAA68772 and 2;
CAA46799). {ECO:0000305}.
CONFLICT 860 860 F -> S (in Ref. 4; AAS45607).
{ECO:0000305}.
STRAND 38 41 {ECO:0000244|PDB:2O26}.
STRAND 43 49 {ECO:0000244|PDB:2O26}.
STRAND 54 59 {ECO:0000244|PDB:2O26}.
STRAND 63 69 {ECO:0000244|PDB:2O26}.
STRAND 71 73 {ECO:0000244|PDB:2O26}.
STRAND 75 78 {ECO:0000244|PDB:2O26}.
STRAND 80 85 {ECO:0000244|PDB:2O26}.
HELIX 90 92 {ECO:0000244|PDB:2O26}.
STRAND 94 103 {ECO:0000244|PDB:2O26}.
STRAND 105 113 {ECO:0000244|PDB:2O26}.
STRAND 125 128 {ECO:0000244|PDB:2O26}.
STRAND 133 135 {ECO:0000244|PDB:2O26}.
STRAND 145 151 {ECO:0000244|PDB:2O26}.
STRAND 162 166 {ECO:0000244|PDB:2O26}.
TURN 167 169 {ECO:0000244|PDB:2O26}.
STRAND 170 175 {ECO:0000244|PDB:2O26}.
HELIX 178 180 {ECO:0000244|PDB:2O26}.
STRAND 184 191 {ECO:0000244|PDB:2O26}.
STRAND 194 197 {ECO:0000244|PDB:2O26}.
STRAND 201 206 {ECO:0000244|PDB:2O26}.
STRAND 214 216 {ECO:0000244|PDB:2O26}.
STRAND 230 240 {ECO:0000244|PDB:2O26}.
STRAND 244 256 {ECO:0000244|PDB:2O26}.
STRAND 264 268 {ECO:0000244|PDB:2O26}.
STRAND 271 282 {ECO:0000244|PDB:2O26}.
STRAND 285 287 {ECO:0000244|PDB:2O26}.
STRAND 289 296 {ECO:0000244|PDB:2O26}.
STRAND 301 308 {ECO:0000244|PDB:2O26}.
SEQUENCE 979 AA; 109343 MW; 03FB4D672248585E CRC64;
MRGARGAWDL LCVLLVLLRG QTATSQPSAS PGEPSPPSIH PAQSELIVEA GDTLSLTCID
PDFVRWTFKT YFNEMVENKK NEWIQEKAEA TRTGTYTCSN SNGLTSSIYV FVRDPAKLFL
VGLPLFGKED SDALVRCPLT DPQVSNYSLI ECDGKSLPTD LTFVPNPKAG ITIKNVKRAY
HRLCVRCAAQ RDGTWLHSDK FTLKVRAAIK AIPVVSVPET SHLLKKGDTF TVVCTIKDVS
TSVNSMWLKM NPQPQHIAQV KHNSWHRGDF NYERQETLTI SSARVDDSGV FMCYANNTFG
SANVTTTLKV VEKGFINISP VKNTTVFVTD GENVDLVVEY EAYPKPEHQQ WIYMNRTSAN
KGKDYVKSDN KSNIRYVNQL RLTRLKGTEG GTYTFLVSNS DASASVTFNV YVNTKPEILT
YDRLINGMLQ CVAEGFPEPT IDWYFCTGAE QRCTTPVSPV DVQVQNVSVS PFGKLVVQSS
IDSSVFRHNG TVECKASNDV GKSSAFFNFA FKGNNKEQIQ AHTLFTPLLI GFVVAAGAMG
IIVMVLTYKY LQKPMYEVQW KVVEEINGNN YVYIDPTQLP YDHKWEFPRN RLSFGKTLGA
GAFGKVVEAT AYGLIKSDAA MTVAVKMLKP SAHLTEREAL MSELKVLSYL GNHMNIVNLL
GACTVGGPTL VITEYCCYGD LLNFLRRKRD SFIFSKQEEQ AEAALYKNLL HSTEPSCDSS
NEYMDMKPGV SYVVPTKTDK RRSARIDSYI ERDVTPAIME DDELALDLDD LLSFSYQVAK
GMAFLASKNC IHRDLAARNI LLTHGRITKI CDFGLARDIR NDSNYVVKGN ARLPVKWMAP
ESIFSCVYTF ESDVWSYGIF LWELFSLGSS PYPGMPVDSK FYKMIKEGFR MVSPEHAPAE
MYDVMKTCWD ADPLKRPTFK QVVQLIEKQI SDSTKHIYSN LANCNPNPEN PVVVDHSVRV
NSVGSSASST QPLLVHEDA


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