Recombinant Human TGFβ-1 / TGFB1 Protein Recombinant

Collections: Cytokines and growth factors, Growth factors and receptors, Recombinant proteins

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Product Overview

Tag	N/A
Host Species	Human
Synonym	Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.
Background	Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
Description	TGFB1 Human Recombinant expressed in CHO cells is a glycosylated homodimeric polypeptide chain containing 2 x 112a.a. and having a total molecular weight of 25.6kDa. The TGFB1 is purified by unique purification methods.
Source	CHO
AA Sequence	ALDTNYCFSS TEKNCCVRQL YIDFRKDLGW KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASAAPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS.
Purity	>95.0% as determined by SDS-PAGE.
Endotoxin	<1.0 EU per μg by the LAL method.
Bioactivity	The ED50 as determined by the dose-dependent inhibition of IL-4-induced proliferation of HT-2 cells is 0.148ng/ml, corresponding to a specific activity of 6.8x106units/mg.
Formulation	Lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid (TFA) And trehalose (1:20 protein to Trehalose ratio).
Stability	Recombinant protein is stable for 12 months at -70°C
Usage	For Research Use Only
Storage	Lyophilized TGFB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB1 Human should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

Target Details

Target 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.; 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.; 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. 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. 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. 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.
Subcellular Location	[Latency-associated peptide]: Secreted, extracellular space, extracellular matrix.; [Transforming growth factor beta-1]: Secreted.
Protein Families	TGF-beta family
Database References	KEGG: bta:282089 STRING: 9913.ENSBTAP00000027261 UniGene: Bt.469

Gene Functions References

TGF-beta1 stimulated lubricin secretion by superficial zone chondrocytes at all densities with twice-a-week TGF-beta treatment. It is noteworthy that the daily treatment of TGF-beta1 increased lubricin much higher compared with twice-a-week treatment. PMID: 28578597
hypoxia increased the expression of platelet-derived growth factor (PDGF) and transforming growth factor-beta1 (TGF-beta1) and decreased the expression of neprilysin (NEP), which contributed to the hypoxia-induced Endothelial-to-mesenchymal transition of pulmonary artery endothelial cells. PMID: 27373199
TGF-beta1 modulates the expression of syndecan-4 in cultured vascular endothelial cells in a biphasic manner. PMID: 28019669
Taken together, Staphylococcus aureus induces TGF-beta1 and bFGF expression through the activation of AP-1 and NF-kappaB in bovine mammary gland fibroblasts. PMID: 26948281
localized to maternal septum in the interdigitation area of cotyledonary villi and caruncle PMID: 26382756
The results identify TGFB1 and ESRRA as likely transcriptional regulators of rumen epithelial development and energy metabolism, respectively, and provide targets for modulation of rumen development and function in the growing calf. PMID: 24767884
the combined treatment with TGF-beta1 and BMP-7 or treatment first with TGF-beta1 followed by BMP-7 was more effective than other treatment groups in both chondrogenic differentiation and SZP secretion. PMID: 23848497
Tenascin-X promotes activation of latent TGF-beta1 and subsequent epithelial to mesenchymal transition in mammary epithelial cells. PMID: 24821840
a detailed computational model for TGF-beta signalling that incorporates elements of previous models together with crosstalking between Smad1/5/8 and Smad2/3 channels through a negative feedback loop dependent on Smad7. PMID: 23804438
Endogenous TGF-beta1 became more bioactive following activation of the transgene protein product in chondrocytes. PMID: 24105960
A novel peptide, P2K, regulating TGF-beta1 signaling had an anabolic effect on bovine intervertebral disc cells and rabbit degenerated discs. PMID: 23124260
Data show that TGF-beta pathways operate during ovarian fetal development, and fibrillin 3 is highly expressed at a critical stage early in developing human and bovine fetal ovaries. PMID: 21411746
Role of TGF-beta1 and TNF-alpha in IL-1beta mediated activation of proMMP-9 in pulmonary artery smooth muscle cells: involvement of an aprotinin sensitive protease. PMID: 21722622
Immunohistochemistry in rectus abdominis muscle from foetuses at 180 and 260 days post-conception PMID: 12441094
vascular endothelial growth factor indirectly stimulates smooth muscle cell proliferation and migration through the modulation of basic fibroblast growth factor and transforming growth factor beta(1) released by endothelial cells PMID: 12591230
Data show that as antral follicles develop, transforming growth factor (TGF)-beta3 is the most abundant TGF-beta isoform and TGF-beta1 protein levels decline in large follicles. PMID: 14502602
TGF-beta 1 signaling pathway controls pericyte growth state and contractile phenotype PMID: 14609524
Reactive oxygen species mediate TGF-beta1-induced TIMP-3 gene expression PMID: 15203191
MGP plays a role in endothelial cell function, by increasing transforming growth factor-beta1 activity and stimulating VEGF expression PMID: 15456771
Exogenous TGF-beta1, IGF-I, EGF and GH inhibited fetal bovine serum-deficiency-stimulated TGF-beta1 expression in mammary epithelium. PMID: 15747730
ALK5 and Smad4 have roles in TGF-beta1-induced pulmonary endothelial permeability PMID: 16004987
IGF-1 protects against TGF-beta1 mediated apoptosis in mammary gland. PMID: 16077202
TGF-beta1 which is expressed in airways of asthmatics may contribute to irreversible airway remodeling by enhancing airway smooth muscle proliferation PMID: 16390551
The roles of TGF-beta1 and somatotropic pathways proteins in control of the switch between survival and death of bovine mammary epithelial cells are reported. PMID: 17388018
role for TGFbeta signaling in the mechanism of cellular mechanotransduction that is especially significant for joint lubrication PMID: 17968924
Transforming growth factor-beta1 protects against pulmonary artery endothelial cell apoptosis via ALK5. PMID: 18456797
the low friction of articular cartilage can be modified by TGF-beta1 and IL-1beta treatment and that the friction coefficient depends on multiple factors, including superficial zone protein localization and surface roughness PMID: 18683879
Delayed parturition in clone calving may be associated with persistence of elevated TGF-beta-1 expression in late pregnancy. PMID: 19167845
Sustained restoration of circulating latent TGFB1 to levels approaching the normal physiological range does not rescue the infertility phenotype caused by TGFB1 deficiency. PMID: 19383262
TGF-beta1 downregulates caveolin-1 of cultured endothelial cells, involving ALK-5 receptor subtype PMID: 19710365

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.