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T-cell-specific guanine nucleotide triphosphate-binding protein 1 (EC 3.6.5.-) (Interferon-gamma-inducible GTPase Ifggb5)

 TGTP1_MOUSE             Reviewed;         415 AA.
Q62293; Q60711; Q8BN19;
02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
10-APR-2019, entry version 151.
RecName: Full=T-cell-specific guanine nucleotide triphosphate-binding protein 1;
EC=3.6.5.- {ECO:0000269|PubMed:9725230};
AltName: Full=Interferon-gamma-inducible GTPase Ifggb5 {ECO:0000303|PubMed:22892676};
Name=Tgtp1;
Synonyms=Ifggb5 {ECO:0000303|PubMed:22892676},
Irgb6 {ECO:0000303|PubMed:22892676},
Mg21 {ECO:0000303|PubMed:7884320};
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], INDUCTION BY IFNG, AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Peritoneal macrophage;
PubMed=7884320;
Lafuse W.P., Brown D., Castle L., Zwilling B.S.;
"Cloning and characterization of a novel cDNA that is IFN-gamma-
induced in mouse peritoneal macrophages and encodes a putative GTP-
binding protein.";
J. Leukoc. Biol. 57:477-483(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Embryonic stem cell, and Spleen;
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 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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NMRI; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
TISSUE SPECIFICITY.
PubMed=7836757;
Carlow D.A., Marth J., Clark-Lewis I., Teh H.S.;
"Isolation of a gene encoding a developmentally regulated T cell-
specific protein with a guanine nucleotide triphosphate-binding
motif.";
J. Immunol. 154:1724-1734(1995).
[7]
FUNCTION, INDUCTION BY IFNG, AND CATALYTIC ACTIVITY.
PubMed=9725230;
Carlow D.A., Teh S.J., Teh H.S.;
"Specific antiviral activity demonstrated by TGTP, a member of a new
family of interferon-induced GTPases.";
J. Immunol. 161:2348-2355(1998).
[8]
GENOMIC ORGANIZATION OF P47 GTPASE CLUSTER.
PubMed=16277747; DOI=10.1186/gb-2005-6-11-r92;
Bekpen C., Hunn J.P., Rohde C., Parvanova I., Guethlein L., Dunn D.M.,
Glowalla E., Leptin M., Howard J.C.;
"The interferon-inducible p47 (IRG) GTPases in vertebrates: loss of
the cell autonomous resistance mechanism in the human lineage.";
Genome Biol. 6:R92.1-R92.18(2005).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INDUCTION
BY TNF, AND TISSUE SPECIFICITY.
PubMed=19285957; DOI=10.1016/j.bbrc.2009.03.043;
Yamada K., Akimoto H., Ogawa Y., Kinumi T., Kamagata Y., Ohmiya Y.;
"Upregulation of immunity-related GTPase (IRG) proteins by TNF-alpha
in murine astrocytes.";
Biochem. Biophys. Res. Commun. 382:434-439(2009).
[10]
FUNCTION.
PubMed=19265156; DOI=10.4049/jimmunol.0804190;
Zhao Y., Ferguson D.J., Wilson D.C., Howard J.C., Sibley L.D.,
Yap G.S.;
"Virulent Toxoplasma gondii evade immunity-related GTPase-mediated
parasite vacuole disruption within primed macrophages.";
J. Immunol. 182:3775-3781(2009).
[11]
IDENTIFICATION, AND GENOMIC ANALYSIS.
PubMed=22892676; DOI=10.1007/s10142-012-0291-2;
Premzl M.;
"Comparative genomic analysis of eutherian interferon-gamma-inducible
GTPases.";
Funct. Integr. Genomics 12:599-607(2012).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver, Lung, and Spleen;
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).
[13]
FUNCTION, AND INDUCTION BY IFNG.
PubMed=24563254; DOI=10.4049/jimmunol.1302822;
Ohshima J., Lee Y., Sasai M., Saitoh T., Su Ma J., Kamiyama N.,
Matsuura Y., Pann-Ghill S., Hayashi M., Ebisu S., Takeda K., Akira S.,
Yamamoto M.;
"Role of mouse and human autophagy proteins in IFN-gamma-induced cell-
autonomous responses against Toxoplasma gondii.";
J. Immunol. 192:3328-3335(2014).
-!- FUNCTION: Involved in innate cell-autonomous resistance to
intracellular pathogens, such as Toxoplasma gondii. During
avirulent type II T. gondii infection, recruited to the
parasitophorous vacuole (PV) membrane, leading to PV vesiculation
and rupture, and subsequent digestion of the parasite within the
cytosol (PubMed:19265156, PubMed:24563254). Not recruited to
virulent type I T. gondii PV membrane (PubMed:19265156). May
confer an antiviral state for vesicular stomatitis virus
(PubMed:9725230). {ECO:0000269|PubMed:19265156,
ECO:0000269|PubMed:24563254, ECO:0000269|PubMed:9725230}.
-!- CATALYTIC ACTIVITY:
Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
Evidence={ECO:0000269|PubMed:9725230};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19285957}.
Endoplasmic reticulum {ECO:0000269|PubMed:19285957}. Golgi
apparatus {ECO:0000269|PubMed:19285957}. Note=In astrocytes
stimulated with IFNG or TNF, diffuse cytoplasmic localization
decreases and the protein partially relocalizes to the endoplasmic
reticulum and Golgi apparatus (PubMed:19285957). Due to sequence
similarity with Tgtp2, it is impossible to assign unambiguously
experimental data published in the literature to Tgtp1 or Tgtp2
gene (Probable). {ECO:0000269|PubMed:19285957,
ECO:0000305|PubMed:22892676}.
-!- TISSUE SPECIFICITY: Expressed in thymus and lymph nodes,
predominantly T-cells. Not expressed by immature CD4(+) CD8(+)
thymocytes (at protein level) (PubMed:7836757). Expressed in IFNG-
stimulated macrophages (PubMed:7884320). Expressed at low levels
in unstimulated astrocytes (PubMed:19285957). Due to sequence
similarity with Tgtp2, it is impossible to assign unambiguously
experimental data published in the literature to Tgtp1 or Tgtp2
gene. {ECO:0000269|PubMed:19285957, ECO:0000269|PubMed:7836757,
ECO:0000269|PubMed:7884320}.
-!- INDUCTION: In macrophages, up-regulated by IFNG, but not by IL2,
IL4, IL10, nor TNF (PubMed:7884320). Up-regulated by IFNG in lymph
node cells and thymocytes and other cell types (PubMed:7836757,
PubMed:9725230, PubMed:24563254). In astrocytes, up-regulated by
TNF and IFNG; when both cytokines are combined, the effect is
synergistic (PubMed:19285957). Due to sequence similarity with
Tgtp2, it is impossible to assign unambiguously experimental data
published in the literature to Tgtp1 or Tgtp2 gene (Probable).
{ECO:0000269|PubMed:19285957, ECO:0000269|PubMed:24563254,
ECO:0000269|PubMed:7836757, ECO:0000269|PubMed:7884320,
ECO:0000269|PubMed:9725230, ECO:0000305|PubMed:22892676}.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. IRG family. {ECO:0000305}.
-!- CAUTION: The gene Tgtp1 belongs to a large family of eutherian
IFNG-inducible GTPases, called immunity-related p47 GTPases, which
comprises a variable amount of paralogs depending upon the species
studied. In C57BL/6J mice, there is over 20 genes, whereas humans
have only one ortholog. Tgtp1 closest paralog is Tgtp2. Both genes
encode identical proteins. At the nucleotide sequence level, their
CDSs differ at only 4 positions. Consequently it is almost
impossible to assign unambiguously to one gene or the other
experimental data published in the literature.
{ECO:0000305|PubMed:16277747, ECO:0000305|PubMed:22892676}.
-----------------------------------------------------------------------
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EMBL; U15636; AAA66220.1; -; mRNA.
EMBL; AK089836; BAC40974.1; -; mRNA.
EMBL; AK163978; BAE37565.1; -; mRNA.
EMBL; AK172473; BAE43026.1; -; mRNA.
EMBL; AL627237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466575; EDL33781.1; -; Genomic_DNA.
EMBL; BC085259; AAH85259.1; -; mRNA.
EMBL; FR734025; CBY65988.1; -; Genomic_DNA.
CCDS; CCDS24593.1; -.
PIR; I56251; I56251.
RefSeq; NP_001138636.1; NM_001145164.1.
RefSeq; NP_035709.3; NM_011579.3.
UniGene; Mm.15793; -.
UniGene; Mm.482363; -.
ProteinModelPortal; Q62293; -.
SMR; Q62293; -.
IntAct; Q62293; 2.
MINT; Q62293; -.
STRING; 10090.ENSMUSP00000069914; -.
iPTMnet; Q62293; -.
PhosphoSitePlus; Q62293; -.
MaxQB; Q62293; -.
PaxDb; Q62293; -.
PRIDE; Q62293; -.
DNASU; 21822; -.
Ensembl; ENSMUST00000046745; ENSMUSP00000045025; ENSMUSG00000078921.
Ensembl; ENSMUST00000068063; ENSMUSP00000069914; ENSMUSG00000078922.
Ensembl; ENSMUST00000229241; ENSMUSP00000155831; ENSMUSG00000115886.
Ensembl; ENSMUST00000229815; ENSMUSP00000155662; ENSMUSG00000115886.
GeneID; 100039796; -.
GeneID; 21822; -.
KEGG; mmu:100039796; -.
KEGG; mmu:21822; -.
UCSC; uc007ipm.3; mouse.
CTD; 100039796; -.
CTD; 21822; -.
MGI; MGI:98734; Tgtp1.
eggNOG; ENOG410IJSM; Eukaryota.
eggNOG; ENOG41125KF; LUCA.
GeneTree; ENSGT00950000183007; -.
HOVERGEN; HBG054304; -.
InParanoid; Q62293; -.
OMA; QCKILEL; -.
OrthoDB; 688334at2759; -.
PhylomeDB; Q62293; -.
TreeFam; TF331897; -.
PRO; PR:Q62293; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000078921; Expressed in 26 organ(s), highest expression level in spleen.
ExpressionAtlas; Q62293; baseline and differential.
GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0005622; C:intracellular; NAS:UniProtKB.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0035458; P:cellular response to interferon-beta; IDA:MGI.
GO; GO:0006952; P:defense response; IBA:GO_Central.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0009617; P:response to bacterium; IEP:MGI.
GO; GO:0035455; P:response to interferon-alpha; IDA:MGI.
GO; GO:0034341; P:response to interferon-gamma; IDA:MGI.
GO; GO:0009615; P:response to virus; IDA:UniProtKB.
InterPro; IPR030385; G_IRG_dom.
InterPro; IPR007743; Immunity-related_GTPase-like.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF05049; IIGP; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51716; G_IRG; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Endoplasmic reticulum; Golgi apparatus;
GTP-binding; Hydrolase; Immunity; Innate immunity; Nucleotide-binding;
Reference proteome.
CHAIN 1 415 T-cell-specific guanine nucleotide
triphosphate-binding protein 1.
/FTId=PRO_0000437942.
DOMAIN 55 237 IRG-type G.
NP_BIND 64 71 GTP. {ECO:0000250}.
NP_BIND 89 93 GTP. {ECO:0000250}.
NP_BIND 218 220 GTP. {ECO:0000250}.
CONFLICT 91 91 A -> G (in Ref. 1; AAA66220).
{ECO:0000305}.
CONFLICT 272 272 E -> G (in Ref. 2; BAC40974).
{ECO:0000305}.
SEQUENCE 415 AA; 47121 MW; 3AFB5F940242952A CRC64;
MAWASSFDAF FKNFKRESKI ISEYDITLIM TYIEENKLQK AVSVIEKVLR DIESAPLHIA
VTGETGAGKS TFINTLRGVG HEEKGAAPTG AIETTMKRTP YPHPKLPNVT IWDLPGIGTT
NFTPQNYLTE MKFGEYDFFI IISATRFKEN DAQLAKAIAQ MGMNFYFVRT KIDSDLDNEQ
KFKPKSFNKE EVLKNIKDYC SNHLQESLDS EPPVFLVSNV DISKYDFPKL ETKLLQDLPA
HKRHVFSLSL QSLTEATINY KRDSLKQKVF LEAMKAGALA TIPLGGMISD ILENLDETFN
LYRSYFGLDD ASLENIAQDL NMSVDDFKVH LRFPHLFAEH NDESLEDKLF KYIKHISSVT
GGPVAAVTYY RMAYYLQNLF LDTAANDAIA LLNSKALFEK KVGPYISEPP EYWEA


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Pathways :
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WP731: Sterol regulatory element binding protein related
WP1011: T Cell Receptor Signaling Pathway
WP1017: Type II interferon signaling (IFNG)
WP1025: B Cell Receptor Signaling Pathway
WP1042: Nucleotide GPCRs
WP1043: Calcium Regulation in the Cardiac Cell
WP1049: G Protein Signaling Pathways
WP1069: Integrin-mediated cell adhesion
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Related Genes :
[Tgtp1 Ifggb5 Irgb6 Mg21] T-cell-specific guanine nucleotide triphosphate-binding protein 1 (EC 3.6.5.-) (Interferon-gamma-inducible GTPase Ifggb5)
[Tgtp2 Ifggb6 Irgb6 Mg21 Tgtp] T-cell-specific guanine nucleotide triphosphate-binding protein 2 (EC 3.6.5.-) (Interferon-gamma-inducible GTPase Ifggb6 protein) (T-cell-specific guanine nucleotide triphosphate-binding protein)
[Irgm1 Ifi1 Iigp3 Irgm] Immunity-related GTPase family M protein 1 (EC 3.6.5.-) (Interferon-inducible GTPase 3) (Interferon-inducible protein 1) (LPS-stimulated RAW 264.7 macrophage protein 47) (LRG-47)
[Samhd1 Mg11] Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-) (Interferon-gamma-inducible protein Mg11) (SAM domain and HD domain-containing protein 1) (mSAMHD1)
[IRGM IFI1 IRGM1 LRG47] Immunity-related GTPase family M protein (EC 3.6.5.-) (Immunity-related GTPase family M protein 1) (Interferon-inducible protein 1) (LPS-stimulated RAW 264.7 macrophage protein 47 homolog) (LRG-47)
[ADAR ADAR1 DSRAD G1P1 IFI4] Double-stranded RNA-specific adenosine deaminase (DRADA) (EC 3.5.4.37) (136 kDa double-stranded RNA-binding protein) (p136) (Interferon-inducible protein 4) (IFI-4) (K88DSRBP)
[IFI16 IFNGIP1] Gamma-interferon-inducible protein 16 (Ifi-16) (Interferon-inducible myeloid differentiation transcriptional activator)
[Ifih1] Interferon-induced helicase C domain-containing protein 1 (EC 3.6.4.13) (Helicase with 2 CARD domains) (Helicard) (Interferon induced with helicase C domain protein 1) (Melanoma differentiation-associated protein 5) (MDA-5) (RIG-I-like receptor 2) (RLR-2)
[CXCL11 ITAC SCYB11 SCYB9B] C-X-C motif chemokine 11 (Beta-R1) (H174) (Interferon gamma-inducible protein 9) (IP-9) (Interferon-inducible T-cell alpha chemoattractant) (I-TAC) (Small-inducible cytokine B11)
[Cxcl10 Crg2 Ifi10 Inp10 Scyb10] C-X-C motif chemokine 10 (10 kDa interferon gamma-induced protein) (Gamma-IP10) (IP-10) (C7) (Interferon-gamma induced protein CRG-2) (Small-inducible cytokine B10)
[ITK EMT LYK] Tyrosine-protein kinase ITK/TSK (EC 2.7.10.2) (Interleukin-2-inducible T-cell kinase) (IL-2-inducible T-cell kinase) (Kinase EMT) (T-cell-specific kinase) (Tyrosine-protein kinase Lyk)
[Ifi30 Gilt Ip30] Gamma-interferon-inducible lysosomal thiol reductase (EC 1.8.-.-) (Gamma-interferon-inducible protein IP-30) (Lysosomal thiol reductase IP30)
[IFI30 GILT IP30] Gamma-interferon-inducible lysosomal thiol reductase (EC 1.8.-.-) (Gamma-interferon-inducible protein IP-30) (Legumaturain)
[Gngt1 Gng1] Guanine nucleotide-binding protein G(T) subunit gamma-T1 (Transducin gamma chain)
[Ifitm3] Interferon-induced transmembrane protein 3 (Dispanin subfamily A member 2b) (DSPA2b) (Fragilis protein) (Interferon-inducible protein 15) (Mouse ifitm-like protein 1) (Mil-1)
[MX1] Interferon-induced GTP-binding protein Mx1 (Interferon-induced protein p78) (IFI-78K) (Interferon-regulated resistance GTP-binding protein MxA) (Myxoma resistance protein 1) (Myxovirus resistance protein 1) [Cleaved into: Interferon-induced GTP-binding protein Mx1, N-terminally processed]
[Hspa5 Grp78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[IFIH1 MDA5 RH116] Interferon-induced helicase C domain-containing protein 1 (EC 3.6.4.13) (Clinically amyopathic dermatomyositis autoantigen 140 kDa) (CADM-140 autoantigen) (Helicase with 2 CARD domains) (Helicard) (Interferon-induced with helicase C domain protein 1) (Melanoma differentiation-associated protein 5) (MDA-5) (Murabutide down-regulated protein) (RIG-I-like receptor 2) (RLR-2) (RNA helicase-DEAD box protein 116)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[Gnai3] Guanine nucleotide-binding protein G(k) subunit alpha (G(i) alpha-3)
[Eif2ak2 Pkr Prkr Tik] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Serine/threonine-protein kinase TIK) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)
[Rack1 Gnb2-rs1 Gnb2l1] Receptor of activated protein C kinase 1 (12-3) (Guanine nucleotide-binding protein subunit beta-2-like 1) (Receptor for activated C kinase) (Receptor of activated protein kinase C 1) (p205) [Cleaved into: Receptor of activated protein C kinase 1, N-terminally processed (Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed)]
[DDX58] Probable ATP-dependent RNA helicase DDX58 (EC 3.6.4.13) (DEAD box protein 58) (RIG-I-like receptor 1) (RLR-1) (Retinoic acid-inducible gene 1 protein) (RIG-1) (Retinoic acid-inducible gene I protein) (RIG-I)
[RACK1 GNB2L1 HLC7 PIG21] Receptor of activated protein C kinase 1 (Cell proliferation-inducing gene 21 protein) (Guanine nucleotide-binding protein subunit beta-2-like 1) (Guanine nucleotide-binding protein subunit beta-like protein 12.3) (Human lung cancer oncogene 7 protein) (HLC-7) (Receptor for activated C kinase) (Small ribosomal subunit protein RACK1) [Cleaved into: Receptor of activated protein C kinase 1, N-terminally processed (Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[EIF2AK2 PKR PRKR] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CG691_19145 CG705_13560 CG706_14580 CIJ94_05515 COD46_23180 CQP61_17160 CRD98_26150 D3I61_11545 D5653_07335 D9D20_21030 D9D23_19420 D9D43_06110 D9D77_14400 D9H68_20750 D9H70_25730 D9H84_23295 DL800_09215 DLU27_07380 DNQ41_14245 DQE83_22775 DTL43_21780 DTM25_06080 DU290_13085 DU321_04440 E2855_02503 EAI36_14435 EC95NR1_00961 ED648_25045 ED653_23400 ED658_13700 ERS085379_01273 ERS085386_05041 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[Rapgef2 Kiaa0313 Pdzgef1] Rap guanine nucleotide exchange factor 2 (Cyclic nucleotide ras GEF) (CNrasGEF) (Neural RAP guanine nucleotide exchange protein) (nRap GEP) (PDZ domain-containing guanine nucleotide exchange factor 1) (PDZ-GEF1) (RA-GEF-1) (Ras/Rap1-associating GEF-1)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]

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