GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

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

 TGFB1_BOVIN             Reviewed;         390 AA.
P18341; A5A3B8;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
18-MAR-2008, sequence version 2.
16-OCT-2019, entry version 153.
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;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-118.
Jiang C., Davis J.S.;
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 76-390.
PubMed=3153459; DOI=10.1210/mend-1-10-693;
van Obberghen-Schilling E., Kondaiah P., Ludwig R.L., Sporn M.B.,
Baker C.C.;
"Complementary deoxyribonucleic acid cloning of bovine transforming
growth factor-beta 1.";
Mol. Endocrinol. 1:693-698(1987).
[3]
SUBUNIT.
TISSUE=Bone;
PubMed=1733936;
Ogawa Y., Schmidt D.K., Dasch J.R., Chang R.J., Glaser C.B.;
"Purification and characterization of transforming growth factor-beta
2.3 and -beta 1.2 heterodimers from bovine bone.";
J. Biol. Chem. 267:2325-2328(1992).
-!- 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}.
-!- INTERACTION:
P48616:VIM; NbExp=2; IntAct=EBI-8537762, EBI-1221453;
-!- 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}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; EF523342; ABP57733.1; -; Genomic_DNA.
EMBL; M36271; AAA30778.1; -; mRNA.
PIR; A40057; A40057.
RefSeq; NP_001159540.1; NM_001166068.1.
SMR; P18341; -.
IntAct; P18341; 1.
MINT; P18341; -.
STRING; 9913.ENSBTAP00000027261; -.
PaxDb; P18341; -.
PRIDE; P18341; -.
GeneID; 282089; -.
KEGG; bta:282089; -.
CTD; 7040; -.
eggNOG; KOG3900; Eukaryota.
eggNOG; ENOG410XT8Z; LUCA.
InParanoid; P18341; -.
KO; K13375; -.
OrthoDB; 643840at2759; -.
Proteomes; UP000009136; 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:0031012; C:extracellular matrix; 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:0005125; F:cytokine activity; IBA:GO_Central.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0005160; F:transforming growth factor beta receptor binding; IBA:GO_Central.
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:0030509; P:BMP signaling pathway; IBA:GO_Central.
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: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:0019049; P:evasion or tolerance of host defenses by virus; 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:UniProtKB.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0048535; P:lymph node development; 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:0048146; P:positive regulation of fibroblast proliferation; IMP:AgBase.
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:0033601; P:positive regulation of mammary gland epithelial cell proliferation; IMP: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: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:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0050714; P:positive regulation of protein secretion; 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:1903620; P:positive regulation of transdifferentiation; IMP:AgBase.
GO; GO:0006611; P:protein export from nucleus; ISS:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0032801; P:receptor catabolic process; ISS:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0051098; P:regulation of binding; ISS:UniProtKB.
GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
GO; GO:0051101; P:regulation of DNA binding; ISS:UniProtKB.
GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
GO; GO:0042306; P:regulation of protein import into nucleus; ISS:UniProtKB.
GO; GO:0060390; P:regulation of SMAD protein signal transduction; ISS:UniProtKB.
GO; GO:0016202; P:regulation of striated muscle tissue development; 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:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
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.
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_0000033754.
CHAIN 279 390 Transforming growth factor beta-1.
{ECO:0000250|UniProtKB:P01137}.
/FTId=PRO_0000033755.
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; 44409 MW; 6FB04B2D73D724CA CRC64;
MPPSGLRLLP LLLPLLWLLM LTPGRPVAGL STCKTIDMEL VKRKRIEAIR GQILSKLRLA
SPPSQGDVPP GPLPEAILAL YNSTRDRVAG ESAETEPEPE ADYYAKEVTR VLMVEYGNKI
YDKMKSSSHS IYMFFNTSEL REAVPEPVLL SRADVRLLRL KLKVEQHVEL YQKYSNNSWR
YLSNRLLAPS DSPEWLSFDV TGVVRQWLTR REEIEGFRLS AHCSCDSKDN TLQVDINGFS
SGRRGDLATI HGMNRPFLLL MATPLERAQH LHSSRHRRAL DTNYCFSSTE KNCCVRQLYI
DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA SAAPCCVPQA
LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS


Related products :

Catalog number Product name Quantity
10-288-23152 Transforming Growth Factor beta 2 (Human). E coli - Glioblastoma-derived T-cell suppressor factor; BSC-1 cell growth inhibitor; Polyergin; Cetermin; TGFB2 protein; Transforming growth factor beta-2; T 0.05 mg
10-288-23152 Transforming Growth Factor beta 2 (Human). E coli - Glioblastoma-derived T-cell suppressor factor; BSC-1 cell growth inhibitor; Polyergin; Cetermin; TGFB2 protein; Transforming growth factor beta-2; T 0.005 mg
20-663-48060 Transforming Growth Factor-beta - Mouse Anti Human Transforming Growth Factor-beta; TGF-beta-1 Monoclonal 0.5 mg
20-663-48060 Transforming Growth Factor-beta - Mouse Anti Human Transforming Growth Factor-beta; TGF-beta-1 Monoclonal 1 mg
EIAAB42139 Betaglycan,Homo sapiens,Human,TGF-beta receptor type 3,TGF-beta receptor type III,TGFBR3,TGFR-3,Transforming growth factor beta receptor III,Transforming growth factor beta receptor type 3
LF-MA42051 Anti-Transforming Growth Factor Beta (TGFB) (TB21), Mouse Monoclonal to Transforming Growth Factor Beta (TGFB), Isotype IgG1, Host Mouse 50
EIAAB42137 Betaglycan,Mouse,Mus musculus,TGF-beta receptor type 3,TGF-beta receptor type III,Tgfbr3,TGFR-3,Transforming growth factor beta receptor III,Transforming growth factor beta receptor type 3
EIAAB42140 Betaglycan,Rat,Rattus norvegicus,TGF-beta receptor type 3,TGF-beta receptor type III,Tgfbr3,TGFR-3,Transforming growth factor beta receptor III,Transforming growth factor beta receptor type 3
EIAAB42138 Betaglycan,Pig,Sus scrofa,TGF-beta receptor type 3,TGF-beta receptor type III,TGFBR3,TGFR-3,Transforming growth factor beta receptor III,Transforming growth factor beta receptor type 3
U0218b CLIA Bos taurus,Bovine,MGF,Milk growth factor,TGFB2,TGF-beta-2,Transforming growth factor beta-2 96T
E0218b ELISA Bos taurus,Bovine,MGF,Milk growth factor,TGFB2,TGF-beta-2,Transforming growth factor beta-2 96T
E0218b ELISA kit Bos taurus,Bovine,MGF,Milk growth factor,TGFB2,TGF-beta-2,Transforming growth factor beta-2 96T
U0218h CLIA BSC-1 cell growth inhibitor,Cetermin,Glioblastoma-derived T-cell suppressor factor,G-TSF,Homo sapiens,Human,Polyergin,TGFB2,TGF-beta-2,Transforming growth factor beta-2 96T
E0218h ELISA kit BSC-1 cell growth inhibitor,Cetermin,Glioblastoma-derived T-cell suppressor factor,G-TSF,Homo sapiens,Human,Polyergin,TGFB2,TGF-beta-2,Transforming growth factor beta-2 96T
E0218h ELISA BSC-1 cell growth inhibitor,Cetermin,Glioblastoma-derived T-cell suppressor factor,G-TSF,Homo sapiens,Human,Polyergin,TGFB2,TGF-beta-2,Transforming growth factor beta-2 96T
RF003-5 rHuman TGF beta-2 Active; Transforming growth factor beta-2; TGF-beta-2 5ug
RF004-5 Transforming growth factor beta-3; TGF-beta-3 , rHuman TGF beta-3 Active 5ug
RF003-2.5 Transforming growth factor beta-2; TGF-beta-2 , rHuman TGF beta-2 Active 2.5ug
RF004-2.5 Transforming growth factor beta-3; TGF-beta-3 , rHuman TGF beta-3 Active 2.5ug
RF003-5 Transforming growth factor beta-2; TGF-beta-2 , rHuman TGF beta-2 Active 5ug
RF004-2.5 rHuman TGF beta-3 Active; Transforming growth factor beta-3; TGF-beta-3 2.5ug
RF004-5 rHuman TGF beta-3 Active; Transforming growth factor beta-3; TGF-beta-3 5ug
RF003-2.5 rHuman TGF beta-2 Active; Transforming growth factor beta-2; TGF-beta-2 2.5ug
AS10 1397 Antibody: TGF-beta | transforming growth factor beta , Host: chicken, polyclonal, Comfirmed reactivity: human, mouse, rat, swine TGF (beta) 100
32-224 TGF beta(transforming growth factor beta), with 390-amino acid protein (about 43 kDa), is a multifunctional peptide that controls proliferation, differentiation, and other functions in many cell types 0.1 mL
Pathways :
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP1370: TGF Beta Signaling Pathway
WP505: TGF Beta Signaling Pathway
WP1897: Regulation of beta-cell development
WP368: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP871: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1224: EBV LMP1 signaling
WP401: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1048: TGF Beta Signaling Pathway
WP1434: Osteopontin Signaling
WP542: Electron Transport Chain
WP1061: Fatty Acid Beta Oxidation
WP1571: EBV LMP1 signaling
WP25: Fatty Acid Beta Oxidation 3

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) (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)
[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)
[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)
[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)]
[TGF beta TGFB1] Transforming growth factor beta

Bibliography :