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Transforming growth factor beta-1 (TGF-beta-1) [Cleaved into: Latency-associated peptide (LAP)]

 TGFB1_MOUSE             Reviewed;         390 AA.
P04202;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
20-MAR-1987, sequence version 1.
07-NOV-2018, entry version 205.
RecName: Full=Transforming growth factor beta-1 proprotein;
Contains:
RecName: Full=Latency-associated peptide {ECO:0000250|UniProtKB:P01137};
Short=LAP;
Contains:
RecName: Full=Transforming growth factor beta-1 {ECO:0000250|UniProtKB:P01137};
Short=TGF-beta-1;
Flags: Precursor;
Name=Tgfb1 {ECO:0000312|MGI:MGI:98725};
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].
PubMed=3007454;
Derynck R., Jarrett J.A., Chen E.Y., Goeddel D.V.;
"The murine transforming growth factor-beta precursor.";
J. Biol. Chem. 261:4377-4379(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BALB/cJ;
PubMed=8522200; DOI=10.1016/0378-1119(95)00460-N;
Guron C., Sudarshan C., Raghow R.;
"Molecular organization of the gene encoding murine transforming
growth factor beta 1.";
Gene 165:325-326(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J, and NOD/LT; TISSUE=Spleen;
Poirot L., Benoist C., Mathis D.;
"Transforming growth factor-beta 1 sequence and expression: no
difference between NOD/Lt and C57Bl/6 mouse strains.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=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).
[5]
FUNCTION, AND INTERACTION WITH ITGAV AND ITGB6.
PubMed=10025398;
Munger J.S., Huang X., Kawakatsu H., Griffiths M.J., Dalton S.L.,
Wu J., Pittet J.F., Kaminski N., Garat C., Matthay M.A., Rifkin D.B.,
Sheppard D.;
"The integrin alpha v beta 6 binds and activates latent TGF beta 1: a
mechanism for regulating pulmonary inflammation and fibrosis.";
Cell 96:319-328(1999).
[6]
INTERACTION WITH NREP.
PubMed=14985127; DOI=10.1016/j.bbrc.2004.01.171;
Paliwal S., Shi J., Dhru U., Zhou Y., Schuger L.;
"P311 binds to the latency associated protein and downregulates the
expression of TGF-beta1 and TGF-beta2.";
Biochem. Biophys. Res. Commun. 315:1104-1109(2004).
[7]
INTERACTION WITH HTRA3.
PubMed=15206957; DOI=10.1111/j.1440-169X.2004.00743.x;
Tocharus J., Tsuchiya A., Kajikawa M., Ueta Y., Oka C., Kawaichi M.;
"Developmentally regulated expression of mouse HtrA3 and its role as
an inhibitor of TGF-beta signaling.";
Dev. Growth Differ. 46:257-274(2004).
[8]
INTERACTION WITH HTRA1.
PubMed=14973287; DOI=10.1242/dev.00999;
Oka C., Tsujimoto R., Kajikawa M., Koshiba-Takeuchi K., Ina J.,
Yano M., Tsuchiya A., Ueta Y., Soma A., Kanda H., Matsumoto M.,
Kawaichi M.;
"HtrA1 serine protease inhibits signaling mediated by Tgfbeta family
proteins.";
Development 131:1041-1053(2004).
[9]
FUNCTION.
PubMed=18368049; DOI=10.1038/nature06878;
Zhou L., Lopes J.E., Chong M.M., Ivanov I.I., Min R., Victora G.D.,
Shen Y., Du J., Rubtsov Y.P., Rudensky A.Y., Ziegler S.F.,
Littman D.R.;
"TGF-beta-induced Foxp3 inhibits T(H)17 cell differentiation by
antagonizing RORgammat function.";
Nature 453:236-240(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[11]
INTERACTION WITH THSD4.
PubMed=21880733; DOI=10.1074/jbc.M111.243451;
Saito M., Kurokawa M., Oda M., Oshima M., Tsutsui K., Kosaka K.,
Nakao K., Ogawa M., Manabe R., Suda N., Ganjargal G., Hada Y.,
Noguchi T., Teranaka T., Sekiguchi K., Yoneda T., Tsuji T.;
"ADAMTSL6beta protein rescues fibrillin-1 microfibril disorder in a
Marfan syndrome mouse model through the promotion of fibrillin-1
assembly.";
J. Biol. Chem. 286:38602-38613(2011).
[12]
FUNCTION.
PubMed=22781750; DOI=10.1016/j.cellsig.2012.07.003;
Bruce D.L., Macartney T., Yong W., Shou W., Sapkota G.P.;
"Protein phosphatase 5 modulates SMAD3 function in the transforming
growth factor-beta pathway.";
Cell. Signal. 24:1999-2006(2012).
[13]
FUNCTION, AND INTERACTION WITH NRROS.
PubMed=29909984; DOI=10.1016/j.cell.2018.05.027;
Qin Y., Garrison B.S., Ma W., Wang R., Jiang A., Li J., Mistry M.,
Bronson R.T., Santoro D., Franco C., Robinton D.A., Stevens B.,
Rossi D.J., Lu C., Springer T.A.;
"A milieu molecule for TGF-beta required for microglia function in the
nervous system.";
Cell 174:156-171(2018).
-!- FUNCTION: Transforming growth factor beta-1 proprotein: Precursor
of the Latency-associated peptide (LAP) and Transforming growth
factor beta-1 (TGF-beta-1) chains, which constitute the regulatory
and active subunit of TGF-beta-1, respectively.
{ECO:0000250|UniProtKB:P01137}.
-!- FUNCTION: Latency-associated peptide: Required to maintain the
Transforming growth factor beta-1 (TGF-beta-1) chain in a latent
state during storage in extracellular matrix (PubMed:29909984).
Associates non-covalently with TGF-beta-1 and regulates its
activation via interaction with 'milieu molecules', such as LTBP1,
LRRC32/GARP and LRRC33/NRROS, that control activation of TGF-beta-
1 (PubMed:29909984). Interaction with LRRC33/NRROS regulates
activation of TGF-beta-1 in macrophages and microglia
(PubMed:29909984). Interaction with LRRC32/GARP controls
activation of TGF-beta-1 on the surface of activated regulatory T-
cells (Tregs) (By similarity). Interaction with integrins
(ITGAV:ITGB6 or ITGAV:ITGB8) results in distortion of the Latency-
associated peptide chain and subsequent release of the active TGF-
beta-1 (PubMed:10025398). {ECO:0000250|UniProtKB:P01137,
ECO:0000269|PubMed:10025398, ECO:0000269|PubMed:29909984}.
-!- FUNCTION: Transforming growth factor beta-1: Multifunctional
protein that regulates the growth and differentiation of various
cell types and is involved in various processes, such as normal
development, immune function, microglia function and responses to
neurodegeneration (PubMed:22781750, PubMed:29909984). Activation
into mature form follows different steps: following cleavage of
the proprotein in the Golgi apparatus, Latency-associated peptide
(LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains
remain non-covalently linked rendering TGF-beta-1 inactive during
storage in extracellular matrix (By similarity). At the same time,
LAP chain interacts with 'milieu molecules', such as LTBP1,
LRRC32/GARP and LRRC33/NRROS that control activation of TGF-beta-1
and maintain it in a latent state during storage in extracellular
milieus (PubMed:29909984). TGF-beta-1 is released from LAP by
integrins (ITGAV:ITGB6 or ITGAV:ITGB8): integrin-binding to LAP
stabilizes an alternative conformation of the LAP bowtie tail and
results in distortion of the LAP chain and subsequent release of
the active TGF-beta-1 (PubMed:10025398) (By similarity). Once
activated following release of LAP, TGF-beta-1 acts by binding to
TGF-beta receptors (TGFBR1 and TGFBR2), which transduce signal (By
similarity). While expressed by many cells types, TGF-beta-1 only
has a very localized range of action within cell environment
thanks to fine regulation of its activation by Latency-associated
peptide chain (LAP) and 'milieu molecules' (PubMed:29909984).
Plays an important role in bone remodeling: acts as a potent
stimulator of osteoblastic bone formation, causing chemotaxis,
proliferation and differentiation in committed osteoblasts
(PubMed:22781750). Can promote either T-helper 17 cells (Th17) or
regulatory T-cells (Treg) lineage differentiation in a
concentration-dependent manner (PubMed:18368049). At high
concentrations, leads to FOXP3-mediated suppression of RORC and
down-regulation of IL-17 expression, favoring Treg cell
development (PubMed:18368049). At low concentrations in concert
with IL-6 and IL-21, leads to expression of the IL-17 and IL-23
receptors, favoring differentiation to Th17 cells
(PubMed:18368049). Stimulates sustained production of collagen
through the activation of CREB3L1 by regulated intramembrane
proteolysis (RIP) (By similarity). Mediates SMAD2/3 activation by
inducing its phosphorylation and subsequent translocation to the
nucleus. Can induce epithelial-to-mesenchymal transition (EMT) and
cell migration in various cell types (By similarity).
{ECO:0000250|UniProtKB:P01137, ECO:0000269|PubMed:10025398,
ECO:0000269|PubMed:18368049, ECO:0000269|PubMed:22781750,
ECO:0000269|PubMed:29909984}.
-!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts
with the serine proteases, HTRA1 and HTRA3: the interaction with
either inhibits TGFB1-mediated signaling. The HTRA protease
activity is required for this inhibition (PubMed:14973287,
PubMed:15206957). May interact with THSD4; this interaction may
lead to sequestration by FBN1 microfibril assembly and attenuation
of TGFB signaling (PubMed:21880733). Interacts with CD109, DPT and
ASPN. Latency-associated peptide: Homodimer; disulfide-linked (By
similarity). Latency-associated peptide: Interacts with
Transforming growth factor beta-1 (TGF-beta-1) chain; interaction
is non-covalent and maintains (TGF-beta-1) in a latent state; each
Latency-associated peptide (LAP) monomer interacts with TGF-beta-1
in the other monomer (By similarity). Latency-associated peptide:
Interacts with LTBP1; leading to regulate activation of TGF-beta-1
(By similarity). Latency-associated peptide: Interacts with
LRRC32/GARP; leading to regulate activation of TGF-beta-1 on the
surface of activated regulatory T-cells (Tregs) (By similarity).
Latency-associated peptide: Interacts with LRRC33/NRROS; leading
to regulate activation of TGF-beta-1 in macrophages and microglia
(PubMed:29909984). Latency-associated peptide: Interacts (via cell
attachment site) with integrins ITGAV and ITGB6 (ITGAV:ITGB6),
leading to release of the active TGF-beta-1 (PubMed:10025398).
Latency-associated peptide: Interacts with NREP; the interaction
results in a decrease in TGFB1 autoinduction (PubMed:14985127).
Latency-associated peptide: Interacts with HSP90AB1; inhibits
latent TGFB1 activation. Transforming growth factor beta-1:
Homodimer; disulfide-linked. Transforming growth factor beta-1:
Interacts with TGF-beta receptors (TGFBR1 and TGFBR2), leading to
signal transduction (By similarity).
{ECO:0000250|UniProtKB:P01137, ECO:0000269|PubMed:10025398,
ECO:0000269|PubMed:14973287, ECO:0000269|PubMed:14985127,
ECO:0000269|PubMed:15206957, ECO:0000269|PubMed:21880733,
ECO:0000269|PubMed:29909984}.
-!- SUBCELLULAR LOCATION: Latency-associated peptide: Secreted,
extracellular space, extracellular matrix
{ECO:0000250|UniProtKB:P01137}.
-!- SUBCELLULAR LOCATION: Transforming growth factor beta-1: Secreted
{ECO:0000250|UniProtKB:P01137}.
-!- DOMAIN: Latency-associated peptide: The 'straitjacket' and 'arm'
domains encircle the Transforming growth factor beta-1 (TGF-beta-
1) monomers and are fastened together by strong bonding between
Lys-56 and Tyr-103/Tyr-104. {ECO:0000250|UniProtKB:P07200}.
-!- DOMAIN: Latency-associated peptide: The cell attachment site motif
mediates binding to integrins (ITGAV:ITGB6 or ITGAV:ITGB8). The
motif locates to a long loop in the arm domain called the bowtie
tail. Integrin-binding stabilizes an alternative conformation of
the bowtie tail. Activation by integrin requires force application
by the actin cytoskeleton, which is resisted by the 'milieu
molecules' (such as LTBP1, LRRC32/GARP and/or LRRC33/NRROS),
resulting in distortion of the prodomain and release of the active
TGF-beta-1. {ECO:0000250|UniProtKB:P01137}.
-!- PTM: Transforming growth factor beta-1 proprotein: The precursor
proprotein is cleaved in the Golgi apparatus by FURIN to form
Transforming growth factor beta-1 (TGF-beta-1) and Latency-
associated peptide (LAP) chains, which remain non-covalently
linked, rendering TGF-beta-1 inactive.
{ECO:0000250|UniProtKB:P01137}.
-!- PTM: Latency-associated peptide: N-glycosylated. Deglycosylation
leads to activation of Transforming growth factor beta-1 (TGF-
beta-1); mechanisms triggering deglycosylation-driven activation
of TGF-beta-1 are however unclear. {ECO:0000250|UniProtKB:P01137}.
-!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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EMBL; M13177; AAA40423.1; -; mRNA.
EMBL; L42462; AAB00138.1; -; Genomic_DNA.
EMBL; L42456; AAB00138.1; JOINED; Genomic_DNA.
EMBL; L42457; AAB00138.1; JOINED; Genomic_DNA.
EMBL; L42458; AAB00138.1; JOINED; Genomic_DNA.
EMBL; L42459; AAB00138.1; JOINED; Genomic_DNA.
EMBL; L42460; AAB00138.1; JOINED; Genomic_DNA.
EMBL; L42461; AAB00138.1; JOINED; Genomic_DNA.
EMBL; AJ009862; CAA08900.1; -; mRNA.
EMBL; BC013738; AAH13738.1; -; mRNA.
CCDS; CCDS20993.1; -.
PIR; A01396; WFMS2.
RefSeq; NP_035707.1; NM_011577.2.
UniGene; Mm.248380; -.
ProteinModelPortal; P04202; -.
SMR; P04202; -.
BioGrid; 204157; 4.
ComplexPortal; CPX-821; TGF-beta-1 complex.
ComplexPortal; CPX-823; TGF-beta-1-TGFR complex.
DIP; DIP-48640N; -.
IntAct; P04202; 1.
STRING; 10090.ENSMUSP00000002678; -.
iPTMnet; P04202; -.
PhosphoSitePlus; P04202; -.
EPD; P04202; -.
PaxDb; P04202; -.
PeptideAtlas; P04202; -.
PRIDE; P04202; -.
Ensembl; ENSMUST00000002678; ENSMUSP00000002678; ENSMUSG00000002603.
GeneID; 21803; -.
KEGG; mmu:21803; -.
UCSC; uc009ftq.1; mouse.
CTD; 7040; -.
MGI; MGI:98725; Tgfb1.
eggNOG; KOG3900; Eukaryota.
eggNOG; ENOG410XT8Z; LUCA.
GeneTree; ENSGT00910000143982; -.
HOGENOM; HOG000290198; -.
HOVERGEN; HBG074115; -.
InParanoid; P04202; -.
KO; K13375; -.
OMA; FSAHCSC; -.
OrthoDB; EOG091G0BMM; -.
PhylomeDB; P04202; -.
TreeFam; TF318514; -.
Reactome; R-MMU-114608; Platelet degranulation.
Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
Reactome; R-MMU-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-MMU-2173789; TGF-beta receptor signaling activates SMADs.
Reactome; R-MMU-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
Reactome; R-MMU-3000170; Syndecan interactions.
Reactome; R-MMU-8941855; RUNX3 regulates CDKN1A transcription.
Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-MMU-8951936; RUNX3 regulates p14-ARF.
PMAP-CutDB; P04202; -.
PRO; PR:P04202; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000002603; Expressed in 223 organ(s), highest expression level in bone marrow.
CleanEx; MM_TGFB1; -.
ExpressionAtlas; P04202; baseline and differential.
Genevisible; P04202; MM.
GO; GO:0030424; C:axon; ISO:MGI.
GO; GO:0072562; C:blood microparticle; ISS:AgBase.
GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:MGI.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005902; C:microvillus; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0030141; C:secretory granule; ISO:MGI.
GO; GO:0003823; F:antigen binding; ISS:AgBase.
GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:UniProtKB.
GO; GO:0005160; F:transforming growth factor beta receptor binding; IPI:MGI.
GO; GO:0034713; F:type I transforming growth factor beta receptor binding; ISS:AgBase.
GO; GO:0005114; F:type II transforming growth factor beta receptor binding; ISS:UniProtKB.
GO; GO:0034714; F:type III transforming growth factor beta receptor binding; ISS:AgBase.
GO; GO:0002460; P:adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains; IDA:BHF-UCL.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0009887; P:animal organ morphogenesis; TAS:MGI.
GO; GO:0031100; P:animal organ regeneration; ISO:MGI.
GO; GO:0003180; P:aortic valve morphogenesis; IMP:BHF-UCL.
GO; GO:0006754; P:ATP biosynthetic process; ISS:UniProtKB.
GO; GO:0060751; P:branch elongation involved in mammary gland duct branching; IMP:MGI.
GO; GO:0002362; P:CD4-positive, CD25-positive, alpha-beta regulatory T cell lineage commitment; TAS:UniProtKB.
GO; GO:0001775; P:cell activation; IDA:MGI.
GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
GO; GO:0048468; P:cell development; IBA:GO_Central.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0008283; P:cell proliferation; IDA:MGI.
GO; GO:0045216; P:cell-cell junction organization; ISS:UniProtKB.
GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; ISO:MGI.
GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:MGI.
GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEA:Ensembl.
GO; GO:0071479; P:cellular response to ionizing radiation; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; ISS:UniProtKB.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:MGI.
GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
GO; GO:0007182; P:common-partner SMAD protein phosphorylation; ISS:UniProtKB.
GO; GO:0006952; P:defense response; TAS:MGI.
GO; GO:0009817; P:defense response to fungus, incompatible interaction; ISO:MGI.
GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
GO; GO:1990402; P:embryonic liver development; IMP:BHF-UCL.
GO; GO:0007492; P:endoderm development; IDA:MGI.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
GO; GO:0019049; P:evasion or tolerance of host defenses by virus; ISS:UniProtKB.
GO; GO:0085029; P:extracellular matrix assembly; IDA:BHF-UCL.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISS:BHF-UCL.
GO; GO:0060325; P:face morphogenesis; IEP:UniProtKB.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0060364; P:frontal suture morphogenesis; IEA:Ensembl.
GO; GO:0008354; P:germ cell migration; IDA:MGI.
GO; GO:0007507; P:heart development; IMP:BHF-UCL.
GO; GO:0003179; P:heart valve morphogenesis; IMP:BHF-UCL.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISS:UniProtKB.
GO; GO:0030214; P:hyaluronan catabolic process; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; IMP:MGI.
GO; GO:0048839; P:inner ear development; IEA:Ensembl.
GO; GO:0070306; P:lens fiber cell differentiation; IMP:MGI.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0048535; P:lymph node development; IMP:MGI.
GO; GO:0060744; P:mammary gland branching involved in thelarche; IMP:MGI.
GO; GO:0030879; P:mammary gland development; IDA:MGI.
GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
GO; GO:0031293; P:membrane protein intracellular domain proteolysis; ISS:UniProtKB.
GO; GO:0007093; P:mitotic cell cycle checkpoint; ISS:UniProtKB.
GO; GO:0032943; P:mononuclear cell proliferation; IMP:MGI.
GO; GO:0001763; P:morphogenesis of a branching structure; ISO:MGI.
GO; GO:0042552; P:myelination; ISO:MGI.
GO; GO:0043011; P:myeloid dendritic cell differentiation; IMP:MGI.
GO; GO:0070168; P:negative regulation of biomineral tissue development; IMP:BHF-UCL.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISS:UniProtKB.
GO; GO:0045786; P:negative regulation of cell cycle; ISS:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; IDA:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISS:UniProtKB.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
GO; GO:0060965; P:negative regulation of gene silencing by miRNA; ISO:MGI.
GO; GO:1900126; P:negative regulation of hyaluronan biosynthetic process; ISS:UniProtKB.
GO; GO:0050777; P:negative regulation of immune response; ISO:MGI.
GO; GO:0032700; P:negative regulation of interleukin-17 production; IDA:UniProtKB.
GO; GO:0010936; P:negative regulation of macrophage cytokine production; ISS:AgBase.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0045662; P:negative regulation of myoblast differentiation; ISS:UniProtKB.
GO; GO:0007406; P:negative regulation of neuroblast proliferation; ISO:MGI.
GO; GO:0030279; P:negative regulation of ossification; IDA:MGI.
GO; GO:0050765; P:negative regulation of phagocytosis; ISO:MGI.
GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; ISO:MGI.
GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:MGI.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0051280; P:negative regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
GO; GO:0048642; P:negative regulation of skeletal muscle tissue development; ISS:UniProtKB.
GO; GO:0050868; P:negative regulation of T cell activation; IMP:MGI.
GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0001843; P:neural tube closure; IMP:BHF-UCL.
GO; GO:0021915; P:neural tube development; IMP:BHF-UCL.
GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
GO; GO:0014003; P:oligodendrocyte development; IMP:CACAO.
GO; GO:0043932; P:ossification involved in bone remodeling; ISS:AgBase.
GO; GO:0030316; P:osteoclast differentiation; IDA:MGI.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0006796; P:phosphate-containing compound metabolic process; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISS:UniProtKB.
GO; GO:0030501; P:positive regulation of bone mineralization; ISS:AgBase.
GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; ISO:MGI.
GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; ISO:MGI.
GO; GO:0071158; P:positive regulation of cell cycle arrest; IDA:MGI.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0030335; P:positive regulation of cell migration; ISS:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; ISS:UniProtKB.
GO; GO:0050921; P:positive regulation of chemotaxis; ISS:UniProtKB.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:BHF-UCL.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:MGI.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0031536; P:positive regulation of exit from mitosis; ISO:MGI.
GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:MGI.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0035066; P:positive regulation of histone acetylation; IDA:MGI.
GO; GO:0031065; P:positive regulation of histone deacetylation; IDA:MGI.
GO; GO:0032740; P:positive regulation of interleukin-17 production; IDA:BHF-UCL.
GO; GO:0048298; P:positive regulation of isotype switching to IgA isotypes; ISS:AgBase.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
GO; GO:0014008; P:positive regulation of microglia differentiation; IMP:UniProtKB.
GO; GO:0071677; P:positive regulation of mononuclear cell migration; ISO:MGI.
GO; GO:1901666; P:positive regulation of NAD+ ADP-ribosyltransferase activity; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
GO; GO:0042482; P:positive regulation of odontogenesis; IDA:MGI.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISS:UniProtKB.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; ISO:MGI.
GO; GO:1903800; P:positive regulation of production of miRNAs involved in gene silencing by miRNA; ISO:MGI.
GO; GO:0031334; P:positive regulation of protein complex assembly; ISS:UniProtKB.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISS:UniProtKB.
GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:AgBase.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IGI:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0050714; P:positive regulation of protein secretion; ISS:UniProtKB.
GO; GO:1903911; P:positive regulation of receptor clustering; IDA:UniProtKB.
GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IMP:UniProtKB.
GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISS:AgBase.
GO; GO:0051152; P:positive regulation of smooth muscle cell differentiation; ISO:MGI.
GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0043117; P:positive regulation of vascular permeability; ISO:MGI.
GO; GO:0006611; P:protein export from nucleus; ISS:UniProtKB.
GO; GO:0000060; P:protein import into nucleus, translocation; ISS:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0032801; P:receptor catabolic process; ISS:UniProtKB.
GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IGI:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0051098; P:regulation of binding; IDA:MGI.
GO; GO:0060762; P:regulation of branching involved in mammary gland duct morphogenesis; IGI:MGI.
GO; GO:0061035; P:regulation of cartilage development; IDA:MGI.
GO; GO:0032829; P:regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; TAS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IDA:MGI.
GO; GO:0051101; P:regulation of DNA binding; IDA:MGI.
GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
GO; GO:0032667; P:regulation of interleukin-23 production; IDA:UniProtKB.
GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
GO; GO:0042306; P:regulation of protein import into nucleus; IDA:MGI.
GO; GO:0045589; P:regulation of regulatory T cell differentiation; IGI:MGI.
GO; GO:0060390; P:regulation of SMAD protein signal transduction; ISS:UniProtKB.
GO; GO:0002028; P:regulation of sodium ion transport; IDA:MGI.
GO; GO:0016202; P:regulation of striated muscle tissue development; IDA:MGI.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
GO; GO:0045066; P:regulatory T cell differentiation; IDA:MGI.
GO; GO:0070723; P:response to cholesterol; ISS:UniProtKB.
GO; GO:0032355; P:response to estradiol; ISS:UniProtKB.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
GO; GO:0034616; P:response to laminar fluid shear stress; IEA:Ensembl.
GO; GO:0010033; P:response to organic substance; ISO:MGI.
GO; GO:0032570; P:response to progesterone; ISS:UniProtKB.
GO; GO:1902074; P:response to salt; IEA:Ensembl.
GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
GO; GO:0009611; P:response to wounding; ISS:AgBase.
GO; GO:0007435; P:salivary gland morphogenesis; ISS:AgBase.
GO; GO:0007519; P:skeletal muscle tissue development; TAS:MGI.
GO; GO:0001501; P:skeletal system development; TAS:MGI.
GO; GO:0007183; P:SMAD protein complex assembly; ISS:UniProtKB.
GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
GO; GO:0042110; P:T cell activation; IDA:MGI.
GO; GO:0030217; P:T cell differentiation; IMP:MGI.
GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
GO; GO:0072540; P:T-helper 17 cell lineage commitment; TAS:UniProtKB.
GO; GO:0002513; P:tolerance induction to self antigen; IMP:MGI.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:MGI.
GO; GO:1905313; P:transforming growth factor beta receptor signaling pathway involved in heart development; IMP:BHF-UCL.
GO; GO:0001657; P:ureteric bud development; IEP:UniProtKB.
GO; GO:0001570; P:vasculogenesis; IMP:BHF-UCL.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
GO; GO:0042060; P:wound healing; ISO:MGI.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR001839; TGF-b_C.
InterPro; IPR001111; TGF-b_propeptide.
InterPro; IPR016319; TGF-beta.
InterPro; IPR015615; TGF-beta-rel.
InterPro; IPR003939; TGFb1.
InterPro; IPR017948; TGFb_CS.
PANTHER; PTHR11848; PTHR11848; 1.
Pfam; PF00019; TGF_beta; 1.
Pfam; PF00688; TGFb_propeptide; 1.
PIRSF; PIRSF001787; TGF-beta; 1.
PRINTS; PR01423; TGFBETA.
PRINTS; PR01424; TGFBETA1.
SMART; SM00204; TGFB; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS00250; TGF_BETA_1; 1.
PROSITE; PS51362; TGF_BETA_2; 1.
1: Evidence at protein level;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Extracellular matrix; Glycoprotein; Growth factor; Mitogen;
Reference proteome; Secreted; Signal.
SIGNAL 1 29 {ECO:0000250|UniProtKB:P01137}.
CHAIN 30 278 Latency-associated peptide.
{ECO:0000250|UniProtKB:P01137}.
/FTId=PRO_0000033766.
CHAIN 279 390 Transforming growth factor beta-1.
{ECO:0000250|UniProtKB:P01137}.
/FTId=PRO_0000033767.
REGION 30 74 Straightjacket domain.
{ECO:0000250|UniProtKB:P07200}.
REGION 75 271 Arm domain.
{ECO:0000250|UniProtKB:P07200}.
REGION 226 252 Bowtie tail.
{ECO:0000250|UniProtKB:P01137}.
MOTIF 244 246 Cell attachment site. {ECO:0000255}.
SITE 278 279 Cleavage; by FURIN.
{ECO:0000250|UniProtKB:P01137}.
CARBOHYD 82 82 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 136 136 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 176 176 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 33 33 Interchain (with C-1359 or C-1384 in
LTBP1); in inactive form.
{ECO:0000250|UniProtKB:P07200}.
DISULFID 223 223 Interchain (with C-225).
{ECO:0000250|UniProtKB:P01137}.
DISULFID 225 225 Interchain (with C-223).
{ECO:0000250|UniProtKB:P01137}.
DISULFID 285 294 {ECO:0000250|UniProtKB:P01137}.
DISULFID 293 356 {ECO:0000250|UniProtKB:P01137}.
DISULFID 322 387 {ECO:0000250|UniProtKB:P01137}.
DISULFID 326 389 {ECO:0000250|UniProtKB:P01137}.
DISULFID 355 355 Interchain.
{ECO:0000250|UniProtKB:P01137}.
SEQUENCE 390 AA; 44310 MW; 4381A51B711D689E CRC64;
MPPSGLRLLP LLLPLPWLLV LTPGRPAAGL STCKTIDMEL VKRKRIEAIR GQILSKLRLA
SPPSQGEVPP GPLPEAVLAL YNSTRDRVAG ESADPEPEPE ADYYAKEVTR VLMVDRNNAI
YEKTKDISHS IYMFFNTSDI REAVPEPPLL SRAELRLQRL KSSVEQHVEL YQKYSNNSWR
YLGNRLLTPT DTPEWLSFDV TGVVRQWLNQ GDGIQGFRFS AHCSCDSKDN KLHVEINGIS
PKRRGDLGTI HDMNRPFLLL MATPLERAQH LHSSRHRRAL DTNYCFSSTE KNCCVRQLYI
DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA SASPCCVPQA
LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS


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