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

 TGFB1_SHEEP             Reviewed;         390 AA.
P50414;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
26-FEB-2020, entry version 122.
RecName: Full=Transforming growth factor beta-1 proprotein;
Contains:
RecName: Full=Latency-associated peptide;
Short=LAP;
Contains:
RecName: Full=Transforming growth factor beta-1;
Short=TGF-beta-1;
Flags: Precursor;
Name=TGFB1;
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7821809; DOI=10.1016/0378-1119(94)90455-3;
Woodall C.J., McLaren L.J., Watt N.J.;
"Sequence and chromosomal localisation of the gene encoding ovine latent
transforming growth factor-beta 1.";
Gene 150:371-373(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 281-390.
STRAIN=Merino; TISSUE=Skin;
PubMed=7749621; DOI=10.1016/0305-0491(94)00208-c;
Sutton R., Ward W.G., Raphael K.A., Cam G.R.;
"Growth factor expression in skin during wool follicle development.";
Comp. Biochem. Physiol. 110B:697-705(1995).
-!- 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. 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. Interaction with LRRC33/NRROS regulates
activation of TGF-beta-1 in macrophages and microglia. Interaction with
LRRC32/GARP controls activation of TGF-beta-1 on the surface of
activated regulatory T-cells (Tregs). 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. {ECO:0000250|UniProtKB:P01137}.
-!- 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 (By
similarity). 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. 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. 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. 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'. Plays an
important role in bone remodeling: acts as a potent stimulator of
osteoblastic bone formation, causing chemotaxis, proliferation and
differentiation in committed osteoblasts. Can promote either T-helper
17 cells (Th17) or regulatory T-cells (Treg) lineage differentiation in
a concentration-dependent manner. At high concentrations, leads to
FOXP3-mediated suppression of RORC and down-regulation of IL-17
expression, favoring Treg cell development. 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 (By similarity).
Stimulates sustained production of collagen through the activation of
CREB3L1 by regulated intramembrane proteolysis (RIP). 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:0000250|UniProtKB:P04202}.
-!- 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. May interact with THSD4; this interaction
may lead to sequestration by FBN1 microfibril assembly and attenuation
of TGFB signaling (By similarity). Interacts with CD109, DPT and ASPN.
Latency-associated peptide: Homodimer; disulfide-linked. 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. Latency-
associated peptide: Interacts with LTBP1; leading to regulate
activation of TGF-beta-1. Latency-associated peptide: Interacts with
LRRC32/GARP; leading to regulate activation of TGF-beta-1 on the
surface of activated regulatory T-cells (Tregs). Interacts with
LRRC33/NRROS; leading to regulate activation of TGF-beta-1 in
macrophages and microglia. Latency-associated peptide: Interacts (via
cell attachment site) with integrins ITGAV and ITGB6 (ITGAV:ITGB6),
leading to release of the active TGF-beta-1 (By similarity). Latency-
associated peptide: Interacts with NREP; the interaction results in a
decrease in TGFB1 autoinduction (By similarity). 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:0000250|UniProtKB:P04202}.
-!- 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; X76916; CAA54242.1; -; mRNA.
EMBL; L36038; AAA31526.1; -; mRNA.
PIR; I46463; I46463.
RefSeq; NP_001009400.1; NM_001009400.1.
SMR; P50414; -.
STRING; 9940.ENSOARP00000008013; -.
PRIDE; P50414; -.
GeneID; 443417; -.
KEGG; oas:443417; -.
CTD; 7040; -.
KO; K13375; -.
OrthoDB; 643840at2759; -.
Proteomes; UP000002356; Unplaced.
GO; GO:0072562; C:blood microparticle; ISS:AgBase.
GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0003823; F:antigen binding; ISS:AgBase.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
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:0006754; P:ATP biosynthetic process; ISS:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0045216; P:cell-cell junction organization; ISS:UniProtKB.
GO; GO:0071407; P:cellular response to organic cyclic compound; ISS:UniProtKB.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISS:AgBase.
GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
GO; GO:0007182; P:common-partner SMAD protein phosphorylation; ISS:UniProtKB.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
GO; GO:0085029; P:extracellular matrix assembly; ISS:UniProtKB.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISS: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; ISS:AgBase.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
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: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; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell population 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; ISS:BHF-UCL.
GO; GO:1900126; P:negative regulation of hyaluronan biosynthetic process; ISS: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:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0048642; P:negative regulation of skeletal muscle tissue development; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0043932; P:ossification involved in bone remodeling; ISS:AgBase.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
GO; GO:0006796; P:phosphate-containing compound metabolic process; ISS:UniProtKB.
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: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 population proliferation; ISS:UniProtKB.
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; ISS:UniProtKB.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0010763; P:positive regulation of fibroblast migration; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
GO; GO:0032740; P:positive regulation of interleukin-17 production; ISS:UniProtKB.
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; ISS:UniProtKB.
GO; GO:1901666; P:positive regulation of NAD+ ADP-ribosyltransferase activity; ISS:UniProtKB.
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:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; 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:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0050714; P:positive regulation of protein secretion; ISS:UniProtKB.
GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISS:UniProtKB.
GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISS:AgBase.
GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:AgBase.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0006611; P:protein export from nucleus; ISS:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
GO; GO:0032801; P:receptor catabolic process; ISS:UniProtKB.
GO; GO:0060390; P:regulation of SMAD protein signal transduction; ISS:UniProtKB.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
GO; GO:0070723; P:response to cholesterol; ISS:UniProtKB.
GO; GO:0032355; P:response to estradiol; ISS:UniProtKB.
GO; GO:0032570; P:response to progesterone; ISS:UniProtKB.
GO; GO:0009611; P:response to wounding; ISS:AgBase.
GO; GO:0007435; P:salivary gland morphogenesis; ISS:AgBase.
GO; GO:0007183; P:SMAD protein complex assembly; ISS:UniProtKB.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
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.
2: Evidence at transcript level;
Cleavage on pair of basic residues; Disulfide bond; Extracellular matrix;
Glycoprotein; Growth factor; Mitogen; Reference proteome; Secreted; Signal.
SIGNAL 1..29
/evidence="ECO:0000250|UniProtKB:P01137"
CHAIN 30..278
/note="Latency-associated peptide"
/evidence="ECO:0000250|UniProtKB:P01137"
/id="PRO_0000033772"
CHAIN 279..390
/note="Transforming growth factor beta-1"
/evidence="ECO:0000250|UniProtKB:P01137"
/id="PRO_0000033773"
REGION 30..74
/note="Straightjacket domain"
/evidence="ECO:0000250|UniProtKB:P07200"
REGION 75..271
/note="Arm domain"
/evidence="ECO:0000250|UniProtKB:P07200"
REGION 226..252
/note="Bowtie tail"
/evidence="ECO:0000250|UniProtKB:P01137"
MOTIF 244..246
/note="Cell attachment site"
/evidence="ECO:0000255"
SITE 278..279
/note="Cleavage; by FURIN"
/evidence="ECO:0000250|UniProtKB:P01137"
CARBOHYD 82
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 136
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 176
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 33
/note="Interchain (with C-1359 or C-1384 in LTBP1); in
inactive form"
/evidence="ECO:0000250|UniProtKB:P07200"
DISULFID 223
/note="Interchain (with C-225)"
/evidence="ECO:0000250|UniProtKB:P01137"
DISULFID 225
/note="Interchain (with C-223)"
/evidence="ECO:0000250|UniProtKB:P01137"
DISULFID 285..294
/evidence="ECO:0000250|UniProtKB:P01137"
DISULFID 293..356
/evidence="ECO:0000250|UniProtKB:P01137"
DISULFID 322..387
/evidence="ECO:0000250|UniProtKB:P01137"
DISULFID 326..389
/evidence="ECO:0000250|UniProtKB:P01137"
DISULFID 355
/note="Interchain"
/evidence="ECO:0000250|UniProtKB:P01137"
SEQUENCE 390 AA; 44291 MW; 1C247299484D0E57 CRC64;
MPPSGLRLLP LLLPLLWLLM LTPGRPVAGL STCKTIDMEL VKRKGIEAIR GQILSKLRLA
SPPSQGDVPP GPLPEAILAL YNSTRDRVAG ESAETEPEPE ADYYAKEVTR VLMVEYGNKI
YDKMKSSSHS IYMFFNTSEL REAVPEPVLL SRADVRLLRL KLKVEQHVEL YQKYSNNSWR
YLSNRLLAPS DSPEWLSFDV TGVVRQWLTH REEIEGFRLS AHCSCDSKDN TLQVDINGFS
SGRRGDLATI HGMNRPFLLL MATPLERAQH LHSSRHRRAL DTNYCFSSTE KNCCVRQLYI
DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA SAAPCCVPQA
LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS


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Related Genes :
[TGFB1 TGFB] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[Tgfb1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[Tgfb1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB2] Transforming growth factor beta-2 proprotein (Cetermin) (Glioblastoma-derived T-cell suppressor factor) (G-TSF) [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-2 (TGF-beta-2)]
[TGFB3] Transforming growth factor beta-3 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-3 (TGF-beta-3)]
[TGFB2] Transforming growth factor beta-2 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-2 (TGF-beta-2)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFBR1 ALK5 SKR4] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (Activin A receptor type II-like protein kinase of 53kD) (Activin receptor-like kinase 5) (ALK-5) (ALK5) (Serine/threonine-protein kinase receptor R4) (SKR4) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[Tgfbr1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (Serine/threonine-protein kinase receptor R4) (SKR4) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[TGFBR1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[TGFBR1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[Tgfbr3] Transforming growth factor beta receptor type 3 (TGF-beta receptor type 3) (TGFR-3) (Betaglycan) (Transforming growth factor beta receptor III) (TGF-beta receptor type III)
[Tgfbr1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (ESK2) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[MAP3K7 TAK1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[Lefty1 Ebaf Lefty Stra3 Tgfb4] Left-right determination factor 1 (Protein lefty-1) (Lefty protein) (Stimulated by retinoic acid gene 3 protein) (Transforming growth factor beta-4) (TGF-beta-4)
[TGFBR2] TGF-beta receptor type-2 (TGFR-2) (EC 2.7.11.30) (TGF-beta type II receptor) (Transforming growth factor-beta receptor type II) (TGF-beta receptor type II) (TbetaR-II)
[Map3k7 Tak1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[LEFTY2 EBAF LEFTA LEFTYA TGFB4 PSEC0024] Left-right determination factor 2 (Endometrial bleeding-associated factor) (Left-right determination factor A) (Protein lefty-2) (Protein lefty-A) (Transforming growth factor beta-4) (TGF-beta-4)
[Nrros Lrrc33] Transforming growth factor beta activator LRRC33 (Leucine-rich repeat-containing protein 33) (Negative regulator of reactive oxygen species)
[LTBP4] Latent-transforming growth factor beta-binding protein 4 (LTBP-4)
[tgfb1] Transforming growth factor beta-1 proprotein (TGF-beta-5) [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[tgfb1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]

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