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Interferon gamma receptor 2 (IFN-gamma receptor 2) (IFN-gamma-R2) (Interferon gamma receptor accessory factor 1) (AF-1) (Interferon gamma receptor beta-chain) (IFN-gamma-R-beta) (Interferon gamma transducer 1)

 INGR2_HUMAN             Reviewed;         337 AA.
P38484; Q9BTL5;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
06-MAR-2007, sequence version 2.
25-OCT-2017, entry version 168.
RecName: Full=Interferon gamma receptor 2 {ECO:0000312|HGNC:HGNC:5440};
Short=IFN-gamma receptor 2;
Short=IFN-gamma-R2;
AltName: Full=Interferon gamma receptor accessory factor 1 {ECO:0000303|PubMed:8124716};
Short=AF-1 {ECO:0000303|PubMed:8124716};
AltName: Full=Interferon gamma receptor beta-chain {ECO:0000303|PubMed:7615558};
Short=IFN-gamma-R-beta {ECO:0000303|PubMed:7615558};
AltName: Full=Interferon gamma transducer 1 {ECO:0000312|HGNC:HGNC:5440};
Flags: Precursor;
Name=IFNGR2 {ECO:0000312|HGNC:HGNC:5440};
Synonyms=IFNGT1 {ECO:0000312|HGNC:HGNC:5440};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND VARIANT ARG-64.
TISSUE=Lung fibroblast;
PubMed=8124716; DOI=10.1016/0092-8674(94)90354-9;
Soh J., Donnelly R.J., Kotenko S., Mariano T.M., Cook J.R., Wang N.,
Emanuel S.L., Schwartz B., Miki T., Pestka S.;
"Identification and sequence of an accessory factor required for
activation of the human interferon gamma receptor.";
Cell 76:793-802(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-58; LYS-147 AND
GLU-182.
SeattleSNPs variation discovery resource;
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-64.
TISSUE=Skin;
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
PubMed=8910544; DOI=10.1074/jbc.271.46.28947;
Rhee S., Ebensperger C., Dembic Z., Pestka S.;
"The structure of the gene for the second chain of the human
interferon gamma receptor.";
J. Biol. Chem. 271:28947-28952(1996).
[5]
FUNCTION, AND INTERACTION WITH INGR1 AND JAK2.
PubMed=7615558; DOI=10.1074/jbc.270.29.17528;
Sakatsume M., Igarashi K., Winestock K.D., Garotta G., Larner A.C.,
Finbloom D.S.;
"The Jak kinases differentially associate with the alpha and beta
(accessory factor) chains of the interferon gamma receptor to form a
functional receptor unit capable of activating STAT transcription
factors.";
J. Biol. Chem. 270:17528-17534(1995).
[6]
FUNCTION, AND INTERACTION WITH JAK2.
PubMed=7673114; DOI=10.1074/jbc.270.36.20915;
Kotenko S.V., Izotova L.S., Pollack B.P., Mariano T.M., Donnelly R.J.,
Muthukumaran G., Cook J.R., Garotta G., Silvennoinen O., Ihle J.N.;
"Interaction between the components of the interferon gamma receptor
complex.";
J. Biol. Chem. 270:20915-20921(1995).
[7]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10605012; DOI=10.4049/jimmunol.164.1.201;
Rigamonti L., Ariotti S., Losana G., Gradini R., Russo M.A.,
Jouanguy E., Casanova J.L., Forni G., Novelli F.;
"Surface expression of the IFN-gamma R2 chain is regulated by
intracellular trafficking in human T lymphocytes.";
J. Immunol. 164:201-207(2000).
[8]
FUNCTION, SUBCELLULAR LOCATION, MOTIF, AND MUTAGENESIS OF
274-ARG-GLY-275; LEU-276; ILE-277; 276-LEU-ILE-277 AND
278-LYS-TYR-279.
PubMed=15356148; DOI=10.4049/jimmunol.173.6.3991;
Rosenzweig S.D., Schwartz O.M., Brown M.R., Leto T.L., Holland S.M.;
"Characterization of a dipeptide motif regulating IFN-gamma receptor 2
plasma membrane accumulation and IFN-gamma responsiveness.";
J. Immunol. 173:3991-3999(2004).
[9]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 28-247, SUBCELLULAR
LOCATION, GLYCOSYLATION AT ASN-56; ASN-110; ASN-137; ASN-231; ASN-85
AND ASN-219, MUTAGENESIS OF ASN-110; ASN-137 AND ASN-231, AND
DISULFIDE BOND.
PubMed=27599734; DOI=10.1107/S2059798316012237;
Mikulecky P., Zahradnik J., Kolenko P., Cerny J., Charnavets T.,
Kolarova L., Necasova I., Pham P.N., Schneider B.;
"Crystal structure of human interferon-gamma receptor 2 reveals the
structural basis for receptor specificity.";
Acta Crystallogr. D 75:1017-1024(2016).
[10]
VARIANT IMD28 CYS-114.
PubMed=10608793; DOI=10.1086/315197;
Doeffinger R., Jouanguy E., Dupuis S., Fondaneche M.C., Stephan J.L.,
Emile J.F., Lamhamedi-Cherradi S., Altare F., Pallier A.,
Barcenas-Morales G., Meinl E., Krause C., Pestka S., Schreiber R.D.,
Novelli F., Casanova J.L.;
"Partial interferon-gamma receptor signaling chain deficiency in a
patient with bacille Calmette-Guerin and Mycobacterium abscessus
infection.";
J. Infect. Dis. 181:379-384(2000).
[11]
VARIANTS IMD28 ASN-168 AND 222-ASN--SER-230 DEL, MUTAGENESIS OF
THR-168, CHARACTERIZATION OF VARIANTS IMD28 ASN-168 AND
222-ASN--SER-230 DEL, AND SUBCELLULAR LOCATION.
PubMed=15924140; DOI=10.1038/ng1581;
Vogt G., Chapgier A., Yang K., Chuzhanova N., Feinberg J., Fieschi C.,
Boisson-Dupuis S., Alcais A., Filipe-Santos O., Bustamante J.,
de Beaucoudrey L., Al-Mohsen I., Al-Hajjar S., Al-Ghonaium A.,
Adimi P., Mirsaeidi M., Khalilzadeh S., Rosenzweig S.,
de la Calle-Martin O., Bauer T.R., Puck J.M., Ochs H.D., Furthner D.,
Engelhorn C., Belohradsky B., Mansouri D., Holland S.M.,
Schreiber R.D., Abel L., Cooper D.N., Soudais C., Casanova J.-L.;
"Gains of glycosylation comprise an unexpectedly large group of
pathogenic mutations.";
Nat. Genet. 37:692-700(2005).
[12]
VARIANT IMD28 ARG-227, AND CHARACTERIZATION OF VARIANT IMD28 ARG-227.
PubMed=22902943; DOI=10.1016/j.jinf.2012.08.008;
Kilic S.S., van Wengen A., de Paus R.A., Celebi S., Meziane B.,
Hafizoglu D., van Dissel J.T., van de Vosse E.;
"Severe disseminated mycobacterial infection in a boy with a novel
mutation leading to IFN-gammaR2 deficiency.";
J. Infect. 65:568-572(2012).
[13]
VARIANTS IMD28 PHE-124 AND ARG-141, CHARACTERIZATION OF VARIANTS IMD28
CYS-114; PHE-124; ARG-141; ASN-168 AND ARG-227, AND SUBCELLULAR
LOCATION.
PubMed=23963039; DOI=10.1182/blood-2013-01-480814;
Moncada-Velez M., Martinez-Barricarte R., Bogunovic D., Kong X.F.,
Blancas-Galicia L., Tirpan C., Aksu G., Vincent Q.B., Boisson B.,
Itan Y., Ramirez-Alejo N., Okada S., Kreins A.Y., Bryant V.L.,
Franco J.L., Migaud M., Espinosa-Padilla S., Yamazaki-Nakashimada M.,
Espinosa-Rosales F., Kutukculer N., Abel L., Bustamante J., Vogt G.,
Casanova J.L., Boisson-Dupuis S.;
"Partial IFN-gammaR2 deficiency is due to protein misfolding and can
be rescued by inhibitors of glycosylation.";
Blood 122:2390-2401(2013).
-!- FUNCTION: Associates with IFNGR1 to form a receptor for the
cytokine interferon gamma (IFNG) (PubMed:8124716,
PubMed:7673114,PubMed:7615558). Ligand binding stimulates
activation of the JAK/STAT signaling pathway (PubMed:8124716,
PubMed:7673114, PubMed:15356148). Required for signal transduction
in contrast to other receptor subunit responsible for ligand
binding (PubMed:7673114). {ECO:0000269|PubMed:15356148,
ECO:0000269|PubMed:7615558, ECO:0000269|PubMed:7673114,
ECO:0000269|PubMed:8124716}.
-!- SUBUNIT: Heterodimer with IFNGR1, to form the IFNG receptor
complex (PubMed:7615558). Interacts (via intracellular domain)
with JAK2 (PubMed:7615558, PubMed:7673114).
{ECO:0000269|PubMed:7615558, ECO:0000269|PubMed:7673114}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15356148,
ECO:0000269|PubMed:15924140, ECO:0000269|PubMed:27599734}; Single-
pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle
membrane {ECO:0000269|PubMed:10605012}; Single-pass type I
membrane protein {ECO:0000255}. Golgi apparatus membrane
{ECO:0000269|PubMed:23963039}; Single-pass type I membrane protein
{ECO:0000255}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:23963039}; Single-pass type I membrane protein
{ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:10605012}. Note=Has
low cell surface expression and high cytoplasmic expression in T
cells. The bias towards cytoplasmic expression may be due to
ligand-independent receptor internalization and recycling.
{ECO:0000269|PubMed:10605012, ECO:0000269|PubMed:15356148}.
-!- TISSUE SPECIFICITY: Expressed in T-cells (at protein level).
{ECO:0000269|PubMed:10605012}.
-!- DISEASE: Immunodeficiency 28 (IMD28) [MIM:614889]: A form of
Mendelian susceptibility to mycobacterial disease, a rare
condition caused by impairment of interferon-gamma mediated
immunity. It is characterized by predisposition to illness caused
by moderately virulent mycobacterial species, such as Bacillus
Calmette-Guerin (BCG) vaccine, environmental non-tuberculous
mycobacteria, and by the more virulent Mycobacterium tuberculosis.
Other microorganisms rarely cause severe clinical disease in
individuals with susceptibility to mycobacterial infections, with
the exception of Salmonella which infects less than 50% of these
individuals. Clinical outcome severity depends on the degree of
impairment of interferon-gamma mediated immunity. Some patients
die of overwhelming mycobacterial disease with lepromatous-like
lesions in early childhood, whereas others develop, later in life,
disseminated but curable infections with tuberculoid granulomas.
IMD28 manifests early in life, with severe, often fatal,
infection. {ECO:0000269|PubMed:10608793,
ECO:0000269|PubMed:15924140, ECO:0000269|PubMed:22902943,
ECO:0000269|PubMed:23963039}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the type II cytokine receptor family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=IFNGR2base; Note=IFNGR2 mutation db;
URL="http://structure.bmc.lu.se/idbase/IFNGR2base/";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/ifngr2/";
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EMBL; U05875; AAA16955.1; -; mRNA.
EMBL; U05877; AAA16956.1; -; mRNA.
EMBL; AY644470; AAT45458.1; -; Genomic_DNA.
EMBL; BC003624; AAH03624.1; -; mRNA.
EMBL; U68755; AAC52066.1; -; Genomic_DNA.
CCDS; CCDS33544.1; -.
PIR; I38500; I38500.
RefSeq; NP_005525.2; NM_005534.3.
UniGene; Hs.634632; -.
PDB; 5EH1; X-ray; 1.80 A; A=28-247.
PDBsum; 5EH1; -.
ProteinModelPortal; P38484; -.
SMR; P38484; -.
BioGrid; 109682; 6.
IntAct; P38484; 2.
MINT; MINT-1508054; -.
STRING; 9606.ENSP00000290219; -.
ChEMBL; CHEMBL2364171; -.
DrugBank; DB00033; Interferon gamma-1b.
iPTMnet; P38484; -.
PhosphoSitePlus; P38484; -.
BioMuta; IFNGR2; -.
DMDM; 145559548; -.
PaxDb; P38484; -.
PeptideAtlas; P38484; -.
PRIDE; P38484; -.
DNASU; 3460; -.
Ensembl; ENST00000290219; ENSP00000290219; ENSG00000159128.
Ensembl; ENST00000576463; ENSP00000458487; ENSG00000262795.
GeneID; 3460; -.
KEGG; hsa:3460; -.
UCSC; uc002yrp.4; human.
CTD; 3460; -.
DisGeNET; 3460; -.
EuPathDB; HostDB:ENSG00000159128.14; -.
GeneCards; IFNGR2; -.
HGNC; HGNC:5440; IFNGR2.
HPA; HPA001535; -.
MalaCards; IFNGR2; -.
MIM; 147569; gene.
MIM; 614889; phenotype.
neXtProt; NX_P38484; -.
OpenTargets; ENSG00000159128; -.
Orphanet; 319589; Autosomal dominant mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR2 deficiency.
Orphanet; 319574; Autosomal recessive mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR2 deficiency.
Orphanet; 319547; Mendelian susceptibility to mycobacterial diseases due to complete IFNgammaR2 deficiency.
PharmGKB; PA29676; -.
eggNOG; ENOG410IVC9; Eukaryota.
eggNOG; ENOG410YR1U; LUCA.
GeneTree; ENSGT00530000063449; -.
HOGENOM; HOG000013157; -.
HOVERGEN; HBG052129; -.
InParanoid; P38484; -.
KO; K05133; -.
PhylomeDB; P38484; -.
TreeFam; TF337223; -.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-877312; Regulation of IFNG signaling.
SignaLink; P38484; -.
SIGNOR; P38484; -.
ChiTaRS; IFNGR2; human.
GenomeRNAi; 3460; -.
PRO; PR:P38484; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000159128; -.
CleanEx; HS_IFNGR2; -.
ExpressionAtlas; P38484; baseline and differential.
Genevisible; P38484; HS.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0004906; F:interferon-gamma receptor activity; TAS:ProtInc.
GO; GO:0004920; F:interleukin-10 receptor activity; IBA:GO_Central.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0009615; P:response to virus; TAS:ProtInc.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR015373; Interferon/interleukin_rcp_dom.
Pfam; PF09294; Interfer-bind; 1.
Pfam; PF01108; Tissue_fac; 1.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Disease mutation; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane;
Polymorphism; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 337 Interferon gamma receptor 2.
/FTId=PRO_0000011011.
TOPO_DOM 28 247 Extracellular. {ECO:0000255}.
TRANSMEM 248 268 Helical. {ECO:0000255}.
TOPO_DOM 269 337 Cytoplasmic. {ECO:0000255}.
DOMAIN 31 129 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 142 240 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOTIF 276 277 Dileucine internalization motif.
{ECO:0000269|PubMed:15356148}.
CARBOHYD 56 56 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:27599734}.
CARBOHYD 85 85 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:27599734}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:27599734}.
CARBOHYD 137 137 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:27599734}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:27599734}.
CARBOHYD 231 231 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:27599734}.
DISULFID 86 94 {ECO:0000269|PubMed:27599734}.
DISULFID 209 234 {ECO:0000269|PubMed:27599734}.
VARIANT 58 58 T -> R (in dbSNP:rs4986958).
{ECO:0000269|Ref.2}.
/FTId=VAR_020003.
VARIANT 64 64 Q -> R (in dbSNP:rs9808753).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8124716}.
/FTId=VAR_002718.
VARIANT 114 114 R -> C (in IMD28; encodes misfolded
protein with abnormal glycosylation;
affects receptor trafficking to the cell
surface; reduces response to IFNG).
{ECO:0000269|PubMed:10608793,
ECO:0000269|PubMed:23963039}.
/FTId=VAR_075305.
VARIANT 124 124 S -> F (in IMD28; encodes misfolded
protein with abnormal glycosylation;
affects receptor trafficking to the cell
surface; reduces response to IFNG).
{ECO:0000269|PubMed:23963039}.
/FTId=VAR_075306.
VARIANT 141 141 G -> R (in IMD28; encodes misfolded
protein with abnormal glycosylation;
affects receptor trafficking to the cell
surface; reduces response to IFNG).
{ECO:0000269|PubMed:23963039}.
/FTId=VAR_075307.
VARIANT 147 147 E -> K (in dbSNP:rs17878639).
{ECO:0000269|Ref.2}.
/FTId=VAR_021383.
VARIANT 168 168 T -> N (in IMD28; does not affect
receptor trafficking to the cell surface;
loss of function due to gain of N-
glycosylation; dbSNP:rs74315444).
{ECO:0000269|PubMed:15924140,
ECO:0000269|PubMed:23963039}.
/FTId=VAR_023281.
VARIANT 182 182 K -> E (in dbSNP:rs17878711).
{ECO:0000269|Ref.2}.
/FTId=VAR_021384.
VARIANT 222 230 Missing (in IMD28; affects receptor
trafficking to the cell surface).
{ECO:0000269|PubMed:15924140}.
/FTId=VAR_023282.
VARIANT 227 227 G -> R (in IMD28; encodes misfolded
protein with abnormal glycosylation;
affects receptor trafficking to the cell
surface; reduces response to IFNG).
{ECO:0000269|PubMed:22902943,
ECO:0000269|PubMed:23963039}.
/FTId=VAR_075308.
MUTAGEN 110 110 N->Q: Complete inhibition of transport to
the cell membrane.
{ECO:0000269|PubMed:27599734}.
MUTAGEN 137 137 N->Q: Complete inhibition of transport to
the cell membrane.
{ECO:0000269|PubMed:27599734}.
MUTAGEN 168 168 T->A,Q: Does not affect function.
{ECO:0000269|PubMed:15924140}.
MUTAGEN 231 231 N->Q: Complete inhibition of transport to
the cell membrane.
{ECO:0000269|PubMed:27599734}.
MUTAGEN 274 275 Missing: Leads to overaccumulation on the
cell membrane.
{ECO:0000269|PubMed:15356148}.
MUTAGEN 276 277 LI->AA: Leads to overaccumulation on the
cell membrane. Enhances function.
{ECO:0000269|PubMed:15356148}.
MUTAGEN 276 277 Missing: Leads to overaccumulation on the
cell membrane. Enhances function.
{ECO:0000269|PubMed:15356148}.
MUTAGEN 276 276 L->A: Leads to small increase in
accumulation on the cell membrane.
{ECO:0000269|PubMed:15356148}.
MUTAGEN 277 277 I->A: Does not affect accumulation on the
cell membrane.
{ECO:0000269|PubMed:15356148}.
MUTAGEN 278 279 Missing: Does not affect accumulation on
the cell membrane.
{ECO:0000269|PubMed:15356148}.
STRAND 37 41 {ECO:0000244|PDB:5EH1}.
STRAND 44 48 {ECO:0000244|PDB:5EH1}.
STRAND 62 68 {ECO:0000244|PDB:5EH1}.
HELIX 79 82 {ECO:0000244|PDB:5EH1}.
STRAND 87 89 {ECO:0000244|PDB:5EH1}.
STRAND 91 95 {ECO:0000244|PDB:5EH1}.
STRAND 109 119 {ECO:0000244|PDB:5EH1}.
STRAND 122 124 {ECO:0000244|PDB:5EH1}.
HELIX 134 137 {ECO:0000244|PDB:5EH1}.
STRAND 144 151 {ECO:0000244|PDB:5EH1}.
STRAND 154 160 {ECO:0000244|PDB:5EH1}.
TURN 168 170 {ECO:0000244|PDB:5EH1}.
STRAND 171 181 {ECO:0000244|PDB:5EH1}.
STRAND 187 199 {ECO:0000244|PDB:5EH1}.
STRAND 207 218 {ECO:0000244|PDB:5EH1}.
STRAND 224 226 {ECO:0000244|PDB:5EH1}.
STRAND 233 236 {ECO:0000244|PDB:5EH1}.
SEQUENCE 337 AA; 37806 MW; 18C68BAF7D91B8AA CRC64;
MRPTLLWSLL LLLGVFAAAA AAPPDPLSQL PAPQHPKIRL YNAEQVLSWE PVALSNSTRP
VVYQVQFKYT DSKWFTADIM SIGVNCTQIT ATECDFTAAS PSAGFPMDFN VTLRLRAELG
ALHSAWVTMP WFQHYRNVTV GPPENIEVTP GEGSLIIRFS SPFDIADTST AFFCYYVHYW
EKGGIQQVKG PFRSNSISLD NLKPSRVYCL QVQAQLLWNK SNIFRVGHLS NISCYETMAD
ASTELQQVIL ISVGTFSLLS VLAGACFFLV LKYRGLIKYW FHTPPSIPLQ IEEYLKDPTQ
PILEALDKDS SPKDDVWDSV SIISFPEKEQ EDVLQTL


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E1579m ELISA kit Fc gamma receptor IIB,Fc-gamma RII,Fc-gamma-RIIB,Fcgr2,Fcgr2b,FcRII,IgG Fc receptor II beta,Low affinity immunoglobulin gamma Fc region receptor II,Ly-17,Ly-17,Lymphocyte antigen 17,Mouse,M 96T
CSB-PA011052GA01HU Rabbit anti-human interferon gamma receptor 2 (interferon gamma transducer 1) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
CSB-PA011052GA01HU Rabbit anti-human interferon gamma receptor 2 (interferon gamma transducer 1) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
18-783-78408 RABBIT ANTI HUMAN INTERFERON GAMMA Biotin - INTERFERON GAMMA; IFN-gamma Polyclonal 0.05 mg
20-663-48022 Interferon-gamma (mAHuIFNg) - Mouse Anti Human Interferon-gamma (mAHuIFNg); IFN-gamma; Immune interferon Monoclonal 1 mg
20-663-48022 Interferon-gamma (mAHuIFNg) - Mouse Anti Human Interferon-gamma (mAHuIFNg); IFN-gamma; Immune interferon Monoclonal 0.5 mg
orb82062 Human Interferon-gamma, recombinant protein Interferon gamma (IFN-gamma) Recombinant is a purified cytokine_growth factor. For research use only. 20
101-M513 IFN-gamma Receptor 1 Anti-Human Host: Mouse IFNGR1; CD119; IFNGR; Interferon gamma receptor 1; 100
101-M513 IFN-gamma Receptor 1, Host: Mouse, Species: Anti-Human, Synonyms: IFNGR1; CD119; IFNGR; Interferon gamma receptor 1; 100 ug
103-M234 IFN-gamma Receptor-1 Anti-Mouse Host: Rat Ifngr1; Ifgr; CD119; Ifngr; Nktar; IFN-gammaR; Interferon gamma Receptor 1 100
20-271-80026 Interferon-gamma - Mouse Anti Human Interferon-gamma; IFN-gamma Monoclonal 1 mg


 

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