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Interleukin-12 subunit alpha (IL-12A) (Cytotoxic lymphocyte maturation factor 35 kDa subunit) (CLMF p35) (IL-12 subunit p35) (NK cell stimulatory factor chain 1) (NKSF1)

 IL12A_HUMAN             Reviewed;         219 AA.
P29459; Q96QZ1;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2002, sequence version 2.
02-JUN-2021, entry version 185.
RecName: Full=Interleukin-12 subunit alpha;
Short=IL-12A;
AltName: Full=Cytotoxic lymphocyte maturation factor 35 kDa subunit;
Short=CLMF p35;
AltName: Full=IL-12 subunit p35;
AltName: Full=NK cell stimulatory factor chain 1;
Short=NKSF1;
Flags: Precursor;
Name=IL12A; Synonyms=NKSF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=1673147;
Wolf S.F., Temple P.A., Kobayashi M., Young D., Dicig M., Lowe L.,
Dzialo R., Fitz L., Ferenz C., Hewick R.M., Kelleher K., Herrmann S.H.,
Clark S.C., Azzoni L., Chan S.H., Trinchieri G., Perussia B.;
"Cloning of cDNA for natural killer cell stimulatory factor, a
heterodimeric cytokine with multiple biologic effects on T and natural
killer cells.";
J. Immunol. 146:3074-3081(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=1674604; DOI=10.1073/pnas.88.10.4143;
Gubler U., Chua A.O., Schoenhaut D.S., Dwyer C.M., McComas W., Motyka R.,
Nabavi N., Wolitzky A.G., Quinn P.M., Familletti P.C., Gately M.K.;
"Coexpression of two distinct genes is required to generate secreted
bioactive cytotoxic lymphocyte maturation factor.";
Proc. Natl. Acad. Sci. U.S.A. 88:4143-4147(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[5]
PROTEIN SEQUENCE OF 23-48, AND FUNCTION.
PubMed=2204066; DOI=10.1073/pnas.87.17.6808;
Stern A.S., Podlaski F.J., Hulmes J.D., Pan Y.C.E., Quinn P.M.,
Wolitzky A.G., Familletti P.C., Stremlo D.L., Truitt T., Chizzonite R.,
Gately M.K.;
"Purification to homogeneity and partial characterization of cytotoxic
lymphocyte maturation factor from human B-lymphoblastoid cells.";
Proc. Natl. Acad. Sci. U.S.A. 87:6808-6812(1990).
[6]
SIMILARITY TO IL-6.
PubMed=1374259; DOI=10.1016/0167-5699(92)90140-3;
Merberg D.M., Wolf S.F., Clark S.C.;
"Sequence similarity between NKSF and the IL-6/G-CSF family.";
Immunol. Today 13:77-78(1992).
[7]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=9342359; DOI=10.1073/pnas.94.22.12041;
Devergne O., Birkenbach M., Kieff E.;
"Epstein-Barr virus-induced gene 3 and the p35 subunit of interleukin 12
form a novel heterodimeric hematopoietin.";
Proc. Natl. Acad. Sci. U.S.A. 94:12041-12046(1997).
[8]
INDUCTION (MICROBIAL INFECTION), AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
Leong W.F., Chow V.T.;
"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal
differential cellular gene expression in response to enterovirus 71
infection.";
Cell. Microbiol. 8:565-580(2006).
[9]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 23-219, SUBUNIT, AND DISULFIDE
BONDS.
PubMed=10899108; DOI=10.1093/emboj/19.14.3530;
Yoon C., Johnston S.C., Tang J., Stahl M., Tobin J.F., Somers W.S.;
"Charged residues dominate a unique interlocking topography in the
heterodimeric cytokine interleukin-12.";
EMBO J. 19:3530-3541(2000).
-!- FUNCTION: Cytokine that can act as a growth factor for activated T and
NK cells, enhance the lytic activity of NK/lymphokine-activated killer
cells, and stimulate the production of IFN-gamma by resting PBMC.
{ECO:0000269|PubMed:1673147, ECO:0000269|PubMed:1674604,
ECO:0000269|PubMed:2204066}.
-!- SUBUNIT: Heterodimer with IL12B; disulfide-linked (PubMed:1674604,
PubMed:10899108). This heterodimer is known as interleukin IL-12
(PubMed:1674604). Heterodimer with EBI3/IL27B; not disulfide-linked
(PubMed:9342359). This heterodimer is known as interleukin IL-35
(PubMed:9342359). {ECO:0000269|PubMed:10899108,
ECO:0000269|PubMed:1674604, ECO:0000269|PubMed:9342359}.
-!- INTERACTION:
P29459; P29460: IL12B; NbExp=2; IntAct=EBI-1029636, EBI-1029614;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1674604,
ECO:0000269|PubMed:9342359}.
-!- INDUCTION: (Microbial infection) Down-regulated in response to
enterovirus 71 (EV71) infection. {ECO:0000269|PubMed:16548883}.
-!- SIMILARITY: Belongs to the IL-6 superfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA59937.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-12 entry;
URL="https://en.wikipedia.org/wiki/Interleukin_12";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il12a/";
---------------------------------------------------------------------------
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EMBL; M65291; AAA59937.1; ALT_INIT; mRNA.
EMBL; M65271; AAA35694.1; -; mRNA.
EMBL; AF404773; AAK84425.1; -; Genomic_DNA.
EMBL; AC010370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_000873.2; NM_000882.3.
PDB; 1F45; X-ray; 2.80 A; B=23-219.
PDB; 3HMX; X-ray; 3.00 A; B=23-219.
PDBsum; 1F45; -.
PDBsum; 3HMX; -.
SMR; P29459; -.
BioGRID; 109806; 9.
ComplexPortal; CPX-381; Interleukin-12 complex.
ComplexPortal; CPX-382; Interleukin-12-receptor complex.
CORUM; P29459; -.
DIP; DIP-3772N; -.
IntAct; P29459; 8.
STRING; 9606.ENSP00000303231; -.
ChEMBL; CHEMBL2364153; -.
DrugCentral; P29459; -.
GlyGen; P29459; 2 sites.
iPTMnet; P29459; -.
PhosphoSitePlus; P29459; -.
BioMuta; IL12A; -.
DMDM; 20141534; -.
PaxDb; P29459; -.
PeptideAtlas; P29459; -.
PRIDE; P29459; -.
ProteomicsDB; 54569; -.
ABCD; P29459; 1 sequenced antibody.
Antibodypedia; 853; 942 antibodies.
DNASU; 3592; -.
Ensembl; ENST00000305579; ENSP00000303231; ENSG00000168811.
GeneID; 3592; -.
KEGG; hsa:3592; -.
UCSC; uc003fcx.4; human.
CTD; 3592; -.
DisGeNET; 3592; -.
GeneCards; IL12A; -.
HGNC; HGNC:5969; IL12A.
HPA; ENSG00000168811; Tissue enhanced (esophagus).
MalaCards; IL12A; -.
MIM; 161560; gene.
neXtProt; NX_P29459; -.
Orphanet; 117; Behcet disease.
Orphanet; 186; Primary biliary cholangitis.
PharmGKB; PA29784; -.
VEuPathDB; HostDB:ENSG00000168811.6; -.
eggNOG; ENOG502S8JN; Eukaryota.
InParanoid; P29459; -.
OrthoDB; 1409826at2759; -.
PhylomeDB; P29459; -.
TreeFam; TF330814; -.
PathwayCommons; P29459; -.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
Reactome; R-HSA-8984722; Interleukin-35 Signalling.
Reactome; R-HSA-9020591; Interleukin-12 signaling.
SignaLink; P29459; -.
SIGNOR; P29459; -.
BioGRID-ORCS; 3592; 9 hits in 991 CRISPR screens.
EvolutionaryTrace; P29459; -.
GeneWiki; IL12A; -.
GenomeRNAi; 3592; -.
Pharos; P29459; Tclin.
PRO; PR:P29459; -.
Proteomes; UP000005640; Chromosome 3.
RNAct; P29459; protein.
Bgee; ENSG00000168811; Expressed in lower esophagus mucosa and 104 other tissues.
ExpressionAtlas; P29459; baseline and differential.
Genevisible; P29459; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0043514; C:interleukin-12 complex; IDA:UniProtKB.
GO; GO:0031906; C:late endosome lumen; TAS:Reactome.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0042163; F:interleukin-12 beta subunit binding; IPI:AgBase.
GO; GO:0005143; F:interleukin-12 receptor binding; NAS:UniProtKB.
GO; GO:0045513; F:interleukin-27 binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; IDA:BHF-UCL.
GO; GO:0016477; P:cell migration; IDA:UniProtKB.
GO; GO:0098586; P:cellular response to virus; IMP:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IEP:UniProtKB.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
GO; GO:0006955; P:immune response; TAS:UniProtKB.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0070757; P:interleukin-35-mediated signaling pathway; TAS:Reactome.
GO; GO:1903588; P:negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IGI:ARUK-UCL.
GO; GO:0032700; P:negative regulation of interleukin-17 production; IDA:BHF-UCL.
GO; GO:0050709; P:negative regulation of protein secretion; IGI:ARUK-UCL.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; IGI:ARUK-UCL.
GO; GO:0045785; P:positive regulation of cell adhesion; IDA:UniProtKB.
GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; IMP:UniProtKB.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:0050671; P:positive regulation of lymphocyte proliferation; IDA:UniProtKB.
GO; GO:0032946; P:positive regulation of mononuclear cell proliferation; IMP:AgBase.
GO; GO:0032816; P:positive regulation of natural killer cell activation; IDA:UniProtKB.
GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IDA:UniProtKB.
GO; GO:0002860; P:positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; IDA:UniProtKB.
GO; GO:0051135; P:positive regulation of NK T cell activation; IDA:BHF-UCL.
GO; GO:0034393; P:positive regulation of smooth muscle cell apoptotic process; IDA:BHF-UCL.
GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IDA:UniProtKB.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0010224; P:response to UV-B; IDA:UniProtKB.
GO; GO:0009615; P:response to virus; IEP:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR004281; IL-12_alpha.
Pfam; PF03039; IL12; 1.
SUPFAM; SSF47266; SSF47266; 1.
1: Evidence at protein level;
3D-structure; Cytokine; Direct protein sequencing; Disulfide bond;
Glycoprotein; Growth factor; Host-virus interaction; Reference proteome;
Secreted; Signal.
SIGNAL 1..22
/evidence="ECO:0000269|PubMed:2204066"
CHAIN 23..219
/note="Interleukin-12 subunit alpha"
/id="PRO_0000015604"
CARBOHYD 93
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 107
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 64..196
/evidence="ECO:0000269|PubMed:10899108"
DISULFID 85..123
/evidence="ECO:0000269|PubMed:10899108"
DISULFID 96
/note="Interchain (with C-199 in IL12B)"
/evidence="ECO:0000269|PubMed:10899108"
CONFLICT 213
/note="M -> T (in Ref. 2; AAA35694)"
/evidence="ECO:0000305"
HELIX 43..58
/evidence="ECO:0007829|PDB:1F45"
HELIX 59..61
/evidence="ECO:0007829|PDB:1F45"
TURN 74..78
/evidence="ECO:0007829|PDB:3HMX"
HELIX 81..84
/evidence="ECO:0007829|PDB:1F45"
HELIX 88..92
/evidence="ECO:0007829|PDB:1F45"
STRAND 107..109
/evidence="ECO:0007829|PDB:3HMX"
TURN 114..116
/evidence="ECO:0007829|PDB:3HMX"
HELIX 118..145
/evidence="ECO:0007829|PDB:1F45"
HELIX 155..169
/evidence="ECO:0007829|PDB:1F45"
HELIX 190..217
/evidence="ECO:0007829|PDB:1F45"
SEQUENCE 219 AA; 24874 MW; 7C658AB7716112B2 CRC64;
MCPARSLLLV ATLVLLDHLS LARNLPVATP DPGMFPCLHH SQNLLRAVSN MLQKARQTLE
FYPCTSEEID HEDITKDKTS TVEACLPLEL TKNESCLNSR ETSFITNGSC LASRKTSFMM
ALCLSSIYED LKMYQVEFKT MNAKLLMDPK RQIFLDQNML AVIDELMQAL NFNSETVPQK
SSLEEPDFYK TKIKLCILLH AFRIRAVTID RVMSYLNAS


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WP1566: Citrate cycle (TCA cycle)
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WP1672: Mismatch repair
WP1693: Purine metabolism
WP1711: Trinitrotoluene degradation
WP2292: Chemokine signaling pathway
WP1644: DNA replication
WP1671: Methane metabolism
WP1680: Oxidative phosphorylation
WP1634: Butanoate metabolism
WP2272: Pathogenic Escherichia coli infection
WP1694: Pyrimidine metabolism
WP1718: Vitamin B6 metabolism
WP1162: Signaling of Hepatocyte Growth Factor Receptor
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Related Genes :
[CDK5R1 CDK5R NCK5A] Cyclin-dependent kinase 5 activator 1 (CDK5 activator 1) (Cyclin-dependent kinase 5 regulatory subunit 1) (TPKII regulatory subunit) [Cleaved into: Cyclin-dependent kinase 5 activator 1, p35 (p35); Cyclin-dependent kinase 5 activator 1, p25 (p25) (Tau protein kinase II 23 kDa subunit) (p23)]
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.22.-) (Papain-like proteinase) (PL-PRO) (p195); Non-structural protein 4 (nsp4) (Peptide HD2) (p41); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p33); Non-structural protein 6 (nsp6) (p34); Non-structural protein 7 (nsp7) (p9); Non-structural protein 8 (nsp8) (p24); Non-structural protein 9 (nsp9) (p10); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p16); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12) (p100); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13) (p68); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14) (p58); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15) (p39); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16) (p35)]
[Cdk5r1 Cdk5r] Cyclin-dependent kinase 5 activator 1 (CDK5 activator 1) (Cyclin-dependent kinase 5 regulatory subunit 1) (TPKII regulatory subunit) [Cleaved into: Cyclin-dependent kinase 5 activator 1, p35 (p35); Cyclin-dependent kinase 5 activator 1, p25 (p25) (Tau protein kinase II 23 kDa subunit) (p23)]
[CDK5R1 CDK5R NCK5A] Cyclin-dependent kinase 5 activator 1 (CDK5 activator 1) (Cyclin-dependent kinase 5 regulatory subunit 1) (TPKII regulatory subunit) [Cleaved into: Cyclin-dependent kinase 5 activator 1, p35 (p35); Cyclin-dependent kinase 5 activator 1, p25 (p25) (Tau protein kinase II 23 kDa subunit) (p23)]
[Cdk5r1 Cdk5r Nck5a] Cyclin-dependent kinase 5 activator 1 (CDK5 activator 1) (Cyclin-dependent kinase 5 regulatory subunit 1) (TPKII regulatory subunit) [Cleaved into: Cyclin-dependent kinase 5 activator 1, p35 (p35); Cyclin-dependent kinase 5 activator 1, p25 (p25) (Tau protein kinase II 23 kDa subunit) (p23)]
[EIF3J EIF3S1 PRO0391] Eukaryotic translation initiation factor 3 subunit J (eIF3j) (Eukaryotic translation initiation factor 3 subunit 1) (eIF-3-alpha) (eIF3 p35)
[] Genome polyprotein [Cleaved into: Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VP1-pX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.22.-) (Papain-like proteinase) (PL-PRO) (p195); Non-structural protein 4 (nsp4) (Peptide HD2) (p41); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p33); Non-structural protein 6 (nsp6) (p34); Non-structural protein 7 (nsp7) (p9); Non-structural protein 8 (nsp8) (p24); Non-structural protein 9 (nsp9) (p10); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p16); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12) (p100); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13) (p68); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14) (p58); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15) (p39); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16) (p35)]
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.22.-) (Papain-like proteinase) (PL-PRO) (p195); Non-structural protein 4 (nsp4) (Peptide HD2) (p41); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p33); Non-structural protein 6 (nsp6) (p34); Non-structural protein 7 (nsp7) (p9); Non-structural protein 8 (nsp8) (p24); Non-structural protein 9 (nsp9) (p10); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p16); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12) (p100); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13) (p68); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14) (p58); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15) (p39); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16) (p35)]
[pol] Gag-Pro-Pol polyprotein [Cleaved into: Matrix protein p19; Core protein p16; Capsid protein p35 (Capsid protein p34); Probable nucleocapsid protein-dUTPase (NC-dUTPase) (EC 3.6.1.23); Protease 17 kDa (EC 3.4.23.-); Protease 13 kDa (EC 3.4.23.-); G-patch peptide; Reverse transcriptase/ribonuclease H (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[pro prt] Gag-Pro polyprotein [Cleaved into: Matrix protein p19; Core protein p16; Capsid protein p35 (Capsid protein p34); Probable nucleocapsid protein-dUTPase (NC-dUTPase) (EC 3.6.1.23); Protease 17 kDa (EC 3.4.23.-); Protease 13 kDa (EC 3.4.23.-); G-patch peptide]
[IL6 IFNB2] Interleukin-6 (IL-6) (B-cell stimulatory factor 2) (BSF-2) (CTL differentiation factor) (CDF) (Hybridoma growth factor) (Interferon beta-2) (IFN-beta-2)
[IL4] Interleukin-4 (IL-4) (B-cell stimulatory factor 1) (BSF-1) (Binetrakin) (Lymphocyte stimulatory factor 1) (Pitrakinra)
[] 3C-like proteinase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.6.4.12) (EC 3.6.4.13) (Exoribonuclease) (Growth factor-like peptide) (Helicase) (M-PRO) (NendoU) (Non-structural protein 1) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (Peptide HD2) (Putative 2'-O-methyl transferase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (nsp12) (nsp13) (nsp14) (nsp15) (nsp16) (nsp5) (p12) (p195) (p23) (p34) (p5) (p87) (p9)
[IL16] Pro-interleukin-16 [Cleaved into: Interleukin-16 (IL-16) (Lymphocyte chemoattractant factor) (LCF)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[FCN3 FCNH HAKA1] Ficolin-3 (Collagen/fibrinogen domain-containing lectin 3 p35) (Collagen/fibrinogen domain-containing protein 3) (Hakata antigen)
[POLY] Core protein precursor (EC 2.7.7.48) (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Envelope glycoprotein E1) (Envelope glycoprotein E2) (Genome polyprotein) (Gp32) (Hepacivirin) (Mature core protein) (NS1) (NS3 helicase) (NS3 protease) (NS3P) (NS5B) (Non-structural protein 4A) (Non-structural protein 4B) (Non-structural protein 5A) (Protease NS2) (RNA-directed RNA polymerase) (Serine protease/helicase NS3) (Viroporin p7) (Viroporin p70) (gp35) (gp68) (gp70) (p21) (p23) (p27) (p56/58) (p68) (p8) (Fragment)
[CITED2 MRG1] Cbp/p300-interacting transactivator 2 (MSG-related protein 1) (MRG-1) (P35srj)
[IFNLR1 IL28RA LICR2] Interferon lambda receptor 1 (IFN-lambda receptor 1) (IFN-lambda-R1) (Cytokine receptor class-II member 12) (Cytokine receptor family 2 member 12) (CRF2-12) (Interleukin-28 receptor subunit alpha) (IL-28 receptor subunit alpha) (IL-28R-alpha) (IL-28RA) (Likely interleukin or cytokine receptor 2) (LICR2)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)] (Fragment)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)] (Fragment)
[IL27RA CRL1 TCCR WSX1 UNQ296/PRO336] Interleukin-27 receptor subunit alpha (IL-27 receptor subunit alpha) (IL-27R subunit alpha) (IL-27R-alpha) (IL-27RA) (Cytokine receptor WSX-1) (Cytokine receptor-like 1) (Type I T-cell cytokine receptor) (TCCR) (ZcytoR1)
[IL12RB2] Interleukin-12 receptor subunit beta-2 (IL-12 receptor subunit beta-2) (IL-12R subunit beta-2) (IL-12R-beta-2) (IL-12RB2)
[IL23A SGRF UNQ2498/PRO5798] Interleukin-23 subunit alpha (IL-23 subunit alpha) (IL-23-A) (Interleukin-23 subunit p19) (IL-23p19)
[Il12rb2] Interleukin-12 receptor subunit beta-2 (IL-12 receptor subunit beta-2) (IL-12R subunit beta-2) (IL-12R-beta-2) (IL-12RB2)

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