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Biotinylated Human Mature TGF beta 1 Protein 4639

$600.00$2,000.00

Summary

  • Expression: HEK293
  • Functional: Yes (ELISA)
  • Amino Acid Range: Ala279-Ser390
Weight1 lbs
Dimensions9 × 5 × 2 in
product tag

C-Avi, also biotinylated

Biotinylated Human Mature TGF beta 1 Protein 4639

protein
Size and concentration
100, 500µg and lyophilized
Form
Lyophilized
Storage Instructions
Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer
Shipped at ambient temperature.
Purity
> 95% as determined by Tris-Bis PAGE
target relevance
TGF-beta 1 (transforming growth factor beta 1) is one of three closely related mammalian members of the large TGF-beta superfamily that share a characteristic cystine knot structure. TGF-beta 1, -2 and -3 are highly pleiotropic cytokines that are proposed to act as cellular switches that regulate processes such as immune function, proliferation and epithelial-mesenchymal transition.Transforming growth factor beta-1 is 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.
Protein names
Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
Gene names
TGFB1,TGFB1 TGFB
Protein family
TGF-beta family
Mass
9606Da
Function
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:0000269|PubMed:29109152, ECO:0000303|PubMed:27252363}.; 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:28117447). 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:19651619, PubMed:19750484, PubMed:2022183, PubMed:22278742, PubMed:8617200, PubMed:8939931). Interaction with LRRC33/NRROS regulates activation of TGF-beta-1 in macrophages and microglia (Probable). Interaction with LRRC32/GARP controls activation of TGF-beta-1 on the surface of activated regulatory T-cells (Tregs) (PubMed:19651619, PubMed:19750484, PubMed:22278742). 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:22278742, PubMed:28117447). {ECO:0000269|PubMed:19651619, ECO:0000269|PubMed:19750484, ECO:0000269|PubMed:2022183, ECO:0000269|PubMed:22278742, ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:8617200, ECO:0000269|PubMed:8939931, ECO:0000305|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 (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 (PubMed:29109152). 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:19651619, PubMed:19750484, PubMed:2022183, PubMed:22278742, PubMed:8617200, PubMed:8939931). 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:22278742, PubMed:28117447). Once activated following release of LAP, TGF-beta-1 acts by binding to TGF-beta receptors (TGFBR1 and TGFBR2), which transduce signal (PubMed:20207738). 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' (By similarity). Plays an important role in bone remodeling: acts as a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts (By similarity). Can promote either T-helper 17 cells (Th17) or regulatory T-cells (Treg) lineage differentiation in a concentration-dependent manner (By similarity). At high concentrations, leads to FOXP3-mediated suppression of RORC and down-regulation of IL-17 expression, favoring Treg cell development (By similarity). 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) (PubMed:25310401). Mediates SMAD2/3 activation by inducing its phosphorylation and subsequent translocation to the nucleus (PubMed:25893292, PubMed:29483653, PubMed:30696809). Positively regulates odontoblastic differentiation in dental papilla cells, via promotion of IPO7-mediated translocation of phosphorylated SMAD2 to the nucleus and subsequent transcription of target genes (By similarity). Can induce epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types (PubMed:25893292, PubMed:30696809). {ECO:0000250|UniProtKB:P04202, ECO:0000269|PubMed:19651619, ECO:0000269|PubMed:19750484, ECO:0000269|PubMed:20207738, ECO:0000269|PubMed:2022183, ECO:0000269|PubMed:22278742, ECO:0000269|PubMed:25310401, ECO:0000269|PubMed:25893292, ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:29109152, ECO:0000269|PubMed:29483653, ECO:0000269|PubMed:30696809, ECO:0000269|PubMed:8617200, ECO:0000269|PubMed:8939931}.
Subellular location
SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:17827158}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-1]: Secreted {ECO:0000269|PubMed:17827158, ECO:0000269|PubMed:29483653}.
Tissues
TISSUE SPECIFICITY: Highly expressed in bone (PubMed:11746498, PubMed:17827158). Abundantly expressed in articular cartilage and chondrocytes and is increased in osteoarthritis (OA) (PubMed:11746498, PubMed:17827158). Colocalizes with ASPN in chondrocytes within OA lesions of articular cartilage (PubMed:17827158). {ECO:0000269|PubMed:11746498, ECO:0000269|PubMed:17827158}.
Structure
SUBUNIT: Homodimer; disulfide-linked (PubMed:20207738, PubMed:25209176, PubMed:28117447, PubMed:29109152). Interacts with the serine proteases, HTRA1 and HTRA3: the interaction with either inhibits TGFB1-mediated signaling and the HTRA protease activity is required for this inhibition (By similarity). 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 (PubMed:16754747, PubMed:17827158, PubMed:9895299). Interacts with EFEMP2 (PubMed:27339457). Interacts with TSKU; the interaction contributes to regulation of the hair cycle (By similarity). {ECO:0000250|UniProtKB:P04202, ECO:0000269|PubMed:16754747, ECO:0000269|PubMed:17827158, ECO:0000269|PubMed:20207738, ECO:0000269|PubMed:25209176, ECO:0000269|PubMed:27339457, ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:29109152, ECO:0000269|PubMed:9895299}.; SUBUNIT: [Latency-associated peptide]: Homodimer; disulfide-linked (PubMed:28117447, PubMed:29109152). 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 (PubMed:29109152). Interacts with LTBP1; leading to regulation of TGF-beta-1 activation (PubMed:2022183, PubMed:8617200, PubMed:8939931). Interacts with LRRC32/GARP; leading to regulation of TGF-beta-1 activation on the surface of activated regulatory T-cells (Tregs) (PubMed:19651619, PubMed:19750484, PubMed:22278742). Interacts with LRRC33/NRROS; leading to regulation of TGF-beta-1 in macrophages and microglia (Probable). Interacts (via cell attachment site) with integrins ITGAV and ITGB6 (ITGAV:ITGB6), leading to release of the active TGF-beta-1 (PubMed:22278742, PubMed:28117447). Interacts with NREP; the interaction results in a decrease in TGFB1 autoinduction (By similarity). Interacts with HSP90AB1; inhibits latent TGFB1 activation (PubMed:20599762). Interact with PSG9; leading to TGFB1 activation (PubMed:27389696). {ECO:0000250|UniProtKB:P04202, ECO:0000269|PubMed:19651619, ECO:0000269|PubMed:19750484, ECO:0000269|PubMed:2022183, ECO:0000269|PubMed:20599762, ECO:0000269|PubMed:22278742, ECO:0000269|PubMed:25209176, ECO:0000269|PubMed:27389696, ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:29109152, ECO:0000269|PubMed:8617200, ECO:0000269|PubMed:8939931, ECO:0000305|PubMed:29909984}.; SUBUNIT: [Transforming growth factor beta-1]: Homodimer; disulfide-linked (PubMed:20207738, PubMed:25209176, PubMed:28117447, PubMed:29109152). Interacts with TGF-beta receptors (TGFBR1 and TGFBR2), leading to signal transduction (PubMed:20207738). {ECO:0000269|PubMed:20207738, ECO:0000269|PubMed:25209176, ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:29109152}.
Post-translational modification
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:0000269|PubMed:7737999}.; PTM: [Latency-associated peptide]: N-glycosylated (PubMed:2493139, PubMed:28117447, PubMed:3162913). 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 (PubMed:2493139). {ECO:0000269|PubMed:2493139, ECO:0000269|PubMed:28117447, ECO:0000269|PubMed:3162913}.
Domain
DOMAIN: [L
Target Relevance information above includes information from UniProt accession : P01137
The UniProt Consortium

Data

ELISA with Biotinylated Human Mature TGF beta 1 Protein
Immobilized Human TGF-beta RII, hFc Tag at 1µg/ml (100µl/Well) on the plate. Dose response curve for Biotinylated Human Mature TGF beta 1, Avi Tag with the EC50 of 9.9ng/ml determined by ELISA.
SDS-PAGE gel of Biotinylated Human Mature TGF beta 1 Protein
Biotinylated Human Mature TGF beta 1 on Tris-Bis PAGE under reduced (R) condition and Non reducing (N) condition. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.




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