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Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain]

 IGF1R_RAT               Reviewed;        1370 AA.
P24062;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
25-OCT-2017, entry version 172.
RecName: Full=Insulin-like growth factor 1 receptor;
EC=2.7.10.1;
AltName: Full=Insulin-like growth factor I receptor;
Short=IGF-I receptor;
AltName: CD_antigen=CD221;
Contains:
RecName: Full=Insulin-like growth factor 1 receptor alpha chain;
Contains:
RecName: Full=Insulin-like growth factor 1 receptor beta chain;
Flags: Precursor;
Name=Igf1r;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=7758167; DOI=10.1161/01.RES.76.6.963;
Du J., Delafontaine P.;
"Inhibition of vascular smooth muscle cell growth through antisense
transcription of a rat insulin-like growth factor I receptor cDNA.";
Circ. Res. 76:963-972(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-364.
STRAIN=Sprague-Dawley;
PubMed=2477843; DOI=10.1073/pnas.86.19.7451;
Werner H., Woloschak M., Adamo M., Shen-Orr Z., Roberts C.T. Jr.,
Leroith D.;
"Developmental regulation of the rat insulin-like growth factor I
receptor gene.";
Proc. Natl. Acad. Sci. U.S.A. 86:7451-7455(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 913-1017.
PubMed=1530648; DOI=10.1016/0006-291X(92)91287-Z;
Kurachi H., Jobo K., Ohta M., Kawasaki T., Itoh N.;
"A new member of the insulin receptor family, insulin receptor-related
receptor, is expressed preferentially in the kidney.";
Biochem. Biophys. Res. Commun. 187:934-939(1992).
[4]
FUNCTION, AND FORMATION OF A HYBRID RECEPTOR WITH INSR.
PubMed=16803852; DOI=10.1152/ajpendo.00565.2005;
Johansson G.S., Arnqvist H.J.;
"Insulin and IGF-I action on insulin receptors, IGF-I receptors, and
hybrid insulin/IGF-I receptors in vascular smooth muscle cells.";
Am. J. Physiol. 291:E1124-E1130(2006).
-!- FUNCTION: Receptor tyrosine kinase which mediates actions of
insulin-like growth factor 1 (IGF1). Binds IGF1 with high affinity
and IGF2 and insulin (INS) with a lower affinity. The activated
IGF1R is involved in cell growth and survival control. IGF1R is
crucial for tumor transformation and survival of malignant cell.
Ligand binding activates the receptor kinase, leading to receptor
autophosphorylation, and tyrosines phosphorylation of multiple
substrates, that function as signaling adapter proteins including,
the insulin-receptor substrates (IRS1/2), Shc and 14-3-3 proteins.
Phosphorylation of IRSs proteins lead to the activation of two
main signaling pathways: the PI3K-AKT/PKB pathway and the Ras-MAPK
pathway. The result of activating the MAPK pathway is increased
cellular proliferation, whereas activating the PI3K pathway
inhibits apoptosis and stimulates protein synthesis.
Phosphorylated IRS1 can activate the 85 kDa regulatory subunit of
PI3K (PIK3R1), leading to activation of several downstream
substrates, including protein AKT/PKB. AKT phosphorylation, in
turn, enhances protein synthesis through mTOR activation and
triggers the antiapoptotic effects of IGFIR through
phosphorylation and inactivation of BAD. In parallel to PI3K-
driven signaling, recruitment of Grb2/SOS by phosphorylated IRS1
or Shc leads to recruitment of Ras and activation of the ras-MAPK
pathway. In addition to these two main signaling pathways IGF1R
signals also through the Janus kinase/signal transducer and
activator of transcription pathway (JAK/STAT). Phosphorylation of
JAK proteins can lead to phosphorylation/activation of signal
transducers and activators of transcription (STAT) proteins. In
particular activation of STAT3, may be essential for the
transforming activity of IGF1R. The JAK/STAT pathway activates
gene transcription and may be responsible for the transforming
activity. JNK kinases can also be activated by the IGF1R. IGF1
exerts inhibiting activities on JNK activation via phosphorylation
and inhibition of MAP3K5/ASK1, which is able to directly associate
with the IGF1R (By similarity). When present in a hybrid receptor
with INSR, binds IGF1 (By similarity). {ECO:0000250,
ECO:0000269|PubMed:16803852}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: Activated by autophosphorylation at Tyr-1162,
Tyr-1166 and Tyr-1167 on the kinase activation loop;
phosphorylation at all three tyrosine residues is required for
optimal kinase activity. Inhibited by MSC1609119A-1, BMS-754807,
PQIP, benzimidazole pyridinone, isoquinolinedione, bis-azaindole,
3-cyanoquinoline, 2,4-bis-arylamino-1,3-pyrimidine,
pyrrolopyrimidine, pyrrole-5-carboxaldehyde, picropodophyllin
(PPP), tyrphostin derivatives. While most inhibitors bind to the
ATP binding pocket, MSC1609119A-1 functions as allosteric
inhibitor and binds close to the DFG motif and the activation loop
(By similarity). Dephosphorylated by PTPN1 (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Tetramer of 2 alpha and 2 beta chains linked by disulfide
bonds. The alpha chains contribute to the formation of the ligand-
binding domain, while the beta chain carries the kinase domain.
Interacts with PIK3R1 and with the PTB/PID domains of IRS1 and
SHC1 in vitro when autophosphorylated on tyrosine residues. Forms
a hybrid receptor with INSR, the hybrid is a tetramer consisting
of 1 alpha chain and 1 beta chain of INSR and 1 alpha chain and 1
beta chain of IGF1R. Interacts with ARRB1 and ARRB2. Interacts
with GRB10. Interacts with RACK1 (By similarity). Interacts with
SOCS1, SOCS2 and SOCS3 (By similarity). Interacts with 14-3-3
proteins (By similarity). Interacts with NMD2 (By similarity).
Interacts with MAP3K5 (By similarity). Interacts with STAT3. Found
in a ternary complex with IGF1 and ITGAV:ITGB3 or ITGA6:ITGB4 (By
similarity). {ECO:0000250|UniProtKB:P08069}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}.
-!- PTM: Autophosphorylated on tyrosine residues in response to ligand
binding. Autophosphorylation occurs in trans, i.e. one subunit of
the dimeric receptor phosphorylates tyrosine residues on the other
subunit. Autophosphorylation occurs in a sequential manner; Tyr-
1166 is predominantly phosphorylated first, followed by
phosphorylation of Tyr-1162 and Tyr-1167. While every single
phosphorylation increases kinase activity, all three tyrosine
residues in the kinase activation loop (Tyr-1162, Tyr-1166 and
Tyr-1167) have to be phosphorylated for optimal activity. Can be
autophosphorylated at additional tyrosine residues (in vitro).
Autophosphorylated is followed by phosphorylation of juxtamembrane
tyrosines and C-terminal serines. Phosphorylation of Tyr-981 is
required for IRS1- and SHC1-binding. Phosphorylation of Ser-1279
by GSK-3beta restrains kinase activity and promotes cell surface
expression, it requires a priming phosphorylation at Ser-1283 (By
similarity). Dephosphorylated by PTPN1. {ECO:0000250}.
-!- PTM: Polyubiquitinated at Lys-1169 and Lys-1172 through both 'Lys-
48' and 'Lys-29' linkages, promoting receptor endocytosis and
subsequent degradation by the proteasome. Ubiquitination is
facilitated by pre-existing phosphorylation (By similarity).
{ECO:0000250}.
-!- PTM: Sumoylated with SUMO1. {ECO:0000250}.
-!- PTM: Controlled by regulated intramembrane proteolysis (RIP).
Undergoes metalloprotease-dependent constitutive ectodomain
shedding to produce a membrane-anchored 52 kDa C-Terminal fragment
which is further processed by presenilin gamma-secretase to yield
an intracellular 50 kDa fragment (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; L29232; AAA41392.1; -; mRNA.
EMBL; M27293; AAA41384.1; -; mRNA.
RefSeq; NP_434694.1; NM_052807.2.
UniGene; Rn.10957; -.
UniGene; Rn.165078; -.
ProteinModelPortal; P24062; -.
SMR; P24062; -.
BioGrid; 247747; 2.
STRING; 10116.ENSRNOP00000019267; -.
BindingDB; P24062; -.
ChEMBL; CHEMBL1075098; -.
iPTMnet; P24062; -.
PhosphoSitePlus; P24062; -.
PaxDb; P24062; -.
PRIDE; P24062; -.
GeneID; 25718; -.
KEGG; rno:25718; -.
UCSC; RGD:2869; rat.
CTD; 3480; -.
RGD; 2869; Igf1r.
eggNOG; KOG4258; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000038045; -.
HOVERGEN; HBG006134; -.
InParanoid; P24062; -.
KO; K05087; -.
OrthoDB; EOG091G00GE; -.
PhylomeDB; P24062; -.
BRENDA; 2.7.10.1; 5301.
PRO; PR:P24062; -.
Proteomes; UP000002494; Unplaced.
Genevisible; P24062; RN.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0005901; C:caveola; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0030315; C:T-tubule; IDA:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:RGD.
GO; GO:0043560; F:insulin receptor substrate binding; IPI:RGD.
GO; GO:0005520; F:insulin-like growth factor binding; ISS:UniProtKB.
GO; GO:0005010; F:insulin-like growth factor-activated receptor activity; IDA:RGD.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISS:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0007409; P:axonogenesis; IMP:RGD.
GO; GO:0003230; P:cardiac atrium development; IEP:RGD.
GO; GO:1904045; P:cellular response to aldosterone; IEP:RGD.
GO; GO:1904385; P:cellular response to angiotensin; IDA:RGD.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
GO; GO:0071392; P:cellular response to estradiol stimulus; IEP:RGD.
GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IPI:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
GO; GO:0071393; P:cellular response to progesterone stimulus; IEP:RGD.
GO; GO:0071394; P:cellular response to testosterone stimulus; IEP:RGD.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IPI:RGD.
GO; GO:0090398; P:cellular senescence; IEP:RGD.
GO; GO:0021549; P:cerebellum development; IMP:RGD.
GO; GO:0097062; P:dendritic spine maintenance; IGI:ARUK-UCL.
GO; GO:0030010; P:establishment of cell polarity; IMP:RGD.
GO; GO:0044849; P:estrous cycle; IMP:RGD.
GO; GO:0021766; P:hippocampus development; IEP:RGD.
GO; GO:0051389; P:inactivation of MAPKK activity; ISS:UniProtKB.
GO; GO:0008286; P:insulin receptor signaling pathway; IMP:ARUK-UCL.
GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:1904193; P:negative regulation of cholangiocyte apoptotic process; IMP:RGD.
GO; GO:1903944; P:negative regulation of hepatocyte apoptotic process; IMP:RGD.
GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; IMP:RGD.
GO; GO:0031175; P:neuron projection development; IDA:RGD.
GO; GO:0048680; P:positive regulation of axon regeneration; IMP:RGD.
GO; GO:0032467; P:positive regulation of cytokinesis; IMP:RGD.
GO; GO:0051054; P:positive regulation of DNA metabolic process; IMP:RGD.
GO; GO:0033690; P:positive regulation of osteoblast proliferation; IMP:RGD.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:RGD.
GO; GO:0043243; P:positive regulation of protein complex disassembly; IGI:ARUK-UCL.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
GO; GO:0090031; P:positive regulation of steroid hormone biosynthetic process; IMP:BHF-UCL.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0051291; P:protein heterooligomerization; IDA:RGD.
GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB.
GO; GO:0046328; P:regulation of JNK cascade; ISS:UniProtKB.
GO; GO:0045471; P:response to ethanol; IDA:RGD.
GO; GO:0032868; P:response to insulin; IEP:RGD.
GO; GO:1902065; P:response to L-glutamate; IDA:RGD.
GO; GO:0035094; P:response to nicotine; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0033197; P:response to vitamin E; IEP:RGD.
CDD; cd00063; FN3; 3.
Gene3D; 2.60.40.10; -; 3.
Gene3D; 3.80.20.20; -; 3.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR006211; Furin-like_Cys-rich_dom.
InterPro; IPR006212; Furin_repeat.
InterPro; IPR009030; Growth_fac_rcpt_.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR032675; L_dom-like.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR000494; Rcpt_L-dom.
InterPro; IPR036941; Rcpt_L-dom_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016246; Tyr_kinase_insulin-like_rcpt.
InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
Pfam; PF00757; Furin-like; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF01030; Recep_L_domain; 2.
PIRSF; PIRSF000620; Insulin_receptor; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00060; FN3; 3.
SMART; SM00261; FU; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF49265; SSF49265; 4.
SUPFAM; SSF52058; SSF52058; 2.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS50853; FN3; 3.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
2: Evidence at transcript level;
ATP-binding; Cell membrane; Cleavage on pair of basic residues;
Complete proteome; Disulfide bond; Glycoprotein; Isopeptide bond;
Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 737 Insulin-like growth factor 1 receptor
alpha chain.
/FTId=PRO_0000016685.
CHAIN 742 1370 Insulin-like growth factor 1 receptor
beta chain.
/FTId=PRO_0000016686.
TOPO_DOM 742 936 Extracellular. {ECO:0000255}.
TRANSMEM 937 960 Helical. {ECO:0000255}.
TOPO_DOM 961 1370 Cytoplasmic. {ECO:0000255}.
DOMAIN 490 610 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 611 709 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 835 928 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1000 1275 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 1006 1014 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 978 981 IRS1- and SHC1-binding. {ECO:0000250}.
ACT_SITE 1136 1136 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 1034 1034 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 1162 1162 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P08069}.
MOD_RES 1166 1166 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P08069}.
MOD_RES 1167 1167 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P08069}.
MOD_RES 1279 1279 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q60751}.
MOD_RES 1283 1283 Phosphoserine.
{ECO:0000250|UniProtKB:Q60751}.
CARBOHYD 51 51 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 102 102 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 135 135 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 245 245 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 314 314 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 418 418 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 439 439 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 535 535 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 608 608 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 623 623 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 641 641 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 748 748 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 757 757 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 765 765 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 901 901 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 914 914 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 33 52 {ECO:0000250}.
DISULFID 150 178 {ECO:0000250}.
DISULFID 182 205 {ECO:0000250}.
DISULFID 192 211 {ECO:0000250}.
DISULFID 215 224 {ECO:0000250}.
DISULFID 219 230 {ECO:0000250}.
DISULFID 231 239 {ECO:0000250}.
DISULFID 235 248 {ECO:0000250}.
DISULFID 251 260 {ECO:0000250}.
DISULFID 264 276 {ECO:0000250}.
DISULFID 282 303 {ECO:0000250}.
DISULFID 307 321 {ECO:0000250}.
DISULFID 324 328 {ECO:0000250}.
DISULFID 332 354 {ECO:0000250}.
DISULFID 456 489 {ECO:0000250}.
CROSSLNK 1169 1169 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P08069}.
CROSSLNK 1172 1172 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P08069}.
CONFLICT 985 986 AD -> PY (in Ref. 3; no nucleotide
entry). {ECO:0000305}.
SEQUENCE 1370 AA; 155396 MW; A5946897A41CB145 CRC64;
MKSGSGGGSP TSLWGLVFLS AALSLWPTSG EICGPGIDIR NDYQQLKRLE NCTVIEGFLH
ILLISKAEDY RSYRFPKLTV ITEYLLLFRV AGLESLGDLF PNLTVIRGWK LFYNYALVIF
EMTNLKDIGL YNLRNITRGA IRIEKNADLC YLSTIDWSLI LDAVSNNYIV GNKPPKECGD
LCPGTLEEKP MCEKTTINNE YNYRCWTTNR CQKMCPSVCG KRACTENNEC CHPECLGSCH
TPDDNTTCVA CRHYYYKGVC VPACPPGTYR FEGWRCVDRD FCANIPNAES SDSDGFVIHD
GECMQECPSG FIRNSTQSMY CIPCEGPCPK VCGDEEKKTK TIDSVTSAQM LQGCTILKGN
LLINIRRGNN IASELENFMG LIEVVTGYVK IRHSHALVSL SFLKNLRLIL GEEQLEGNYS
FYVLDNQNLQ QLWDWNHRNL TVRSGKMYFA FNPKLCVSEI YRMEEVTGTK GRQSKGDINT
RNNGERASCE SDVLRFTSTT TWKNRIIITW HRYRPPDYRD LISFTVYYKE APFKNVTEYD
GQDACGSNSW NMVDVDLPPN KEGEPGILLH GLKPWTQYAV YVKAVTLTMV ENDHIRGAKS
EILYIRTNAS VPSIPLDVLS ASNSSSQLIV KWNPPTLPNG NLSYYIVRWQ RQPQDGYLFR
HNYCSKDKIP IRKYADGTID VEEVTENPKT EVCGGDKGPC CACPKTEAEK QAEKEEAEYR
KVFENFLHNS IFVPRPERRR RDVLQVANTT MSSRSRNTTV ADTYNITDPE EFETEYPFFE
SRVDNKERTV ISNLRPFTLY RIDIHSCNHE AEKLGCSASN FVFARTMPAE GADDIPGPVT
WEPRPENSIF LKWPEPENPN GLILMYEIKY GSQVEDQREC VSRQEYRKYG GAKLNRLNPG
NYTARIQATS LSGNGSWTDP VFFYVPAKTT YENFMHLIIA LPVAILLIVG GLVIMLYVFH
RKRNNSRLGN GVLYASVNPE YFSAADVYVP DEWEVAREKI TMNRELGQGS FGMVYEGVAK
GVVKDEPETR VAIKTVNEAA SMRERIEFLN EASVMKEFNC HHVVRLLGVV SQGQPTLVIM
ELMTRGDLKS YLRSLRPEVE NNLVLIPPSL SKMIQMAGEI ADGMAYLNAN KFVHRDLAAR
NCMVAEDFTV KIGDFGMTRD IYETDYYRKG GKGLLPVRWM SPESLKDGVF TTHSDVWSFG
VVLWEIATLA EQPYQGLSNE QVLRFVMEGG LLDKPDNCPD MLFELMRMCW QYNPKMRPSF
LEIIGSIKDE MEPSFQEVSF YYSEENKPPE PEELEMELEL EPENMESVPL DPSASSASLP
LPERHSGHKA ENGPGVLVLR ASFDERQPYA HMNGGRANER ALPLPQSSTC


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18-785-210214 IGF-1R (Phospho-Tyr1161) - EC 2.7.10.1; Insulin-like growth factor I receptor; IGF-I receptor; CD221 antigen Polyclonal 0.05 mg
18-785-210214 IGF-1R (Phospho-Tyr1161) - EC 2.7.10.1; Insulin-like growth factor I receptor; IGF-I receptor; CD221 antigen Polyclonal 0.1 mg
E1629m ELISA kit 300 kDa mannose 6-phosphate receptor,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,Igf2r,IGF-II receptor,Insulin-like growth factor 2 receptor,Insulin-like grow 96T
17-8849-41 Anti-Human CD221 (Insulin-like Growth Factor-1 Receptor) APC 25 tests
17-8849-42 Anti-Human CD221 (Insulin-like Growth Factor-1 Receptor) APC 100 tests
53-8849-41 Anti-Human CD221 (Insulin-like Growth Factor-1 Receptor) Alexa Fluor
53-8849-42 Anti-Human CD221 (Insulin-like Growth Factor-1 Receptor) Alexa Fluor
YSRTMCA2344A488 CD221, Insulin Like Growth Factor I Receptor, Clone 1H7, Mab anti_, ALEXA 488 conj. vial
16-8849-80 Anti-Human CD221 (Insulin-like Growth Factor-1 Receptor) Functional Grade Purified 25 ug
16-8849-82 Anti-Human CD221 (Insulin-like Growth Factor-1 Receptor) Functional Grade Purified 100 ug
orb82618 Human LR3IGF1 protein Insulin-like growth factor-1 (IGF1) is the principal hormonal mediator of statural growth. Under normal circumstances, growth hormone (GH) binds to its receptor in the liver, and 20
U1629h CLIA 300 kDa mannose 6-phosphate receptor,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,Homo sapiens,Human,IGF2R,IGF-II receptor,Insulin-like growth factor 2 receptor,Insu 96T
E1629h ELISA 300 kDa mannose 6-phosphate receptor,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,Homo sapiens,Human,IGF2R,IGF-II receptor,Insulin-like growth factor 2 receptor,Ins 96T
U1629b CLIA 300 kDa mannose 6-phosphate receptor,Bos taurus,Bovine,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,IGF2R,IGF-II receptor,Insulin-like growth factor 2 receptor,Insul 96T
E1629b ELISA 300 kDa mannose 6-phosphate receptor,Bos taurus,Bovine,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,IGF2R,IGF-II receptor,Insulin-like growth factor 2 receptor,Insu 96T
E1629b ELISA kit 300 kDa mannose 6-phosphate receptor,Bos taurus,Bovine,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,IGF2R,IGF-II receptor,Insulin-like growth factor 2 receptor 96T
IQ391 Mouse Anti-Insulin-Like Growth Factor (IGF-1) Target Antigen Insulin-Like Growth Factor (IGF-1) Host Isotype Mouse IgG1 Application RIA or EIA assay development & studies of IGF-1 on frozen & paraf 0.1ml (1mg/ml)


 

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