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About This Item
Biological source:
human
Recombinant:
expressed in CHO cells
Assay:
≥95% (SDS-PAGE)
Form:
powder
Mol wt:
dimer (12.8/25.6 kDa (112/224 aa))
Impurities:
≤0.1 EU/μg (LAL test)
biological source
human
recombinant
expressed in CHO cells
form
powder
Quality Level
Gene Information
human ... TGFB1(7040)
assay
≥95% (SDS-PAGE)
potency
≤0.5 ng/mL ED50
mol wt
dimer (12.8/25.6 kDa (112/224 aa))
packaging
pkg of 2 μg, pkg of 50 μg
storage condition
avoid repeated freeze/thaw cycles
technique(s)
cell culture | mammalian: suitable
impurities
≤0.1 EU/μg (LAL test)
UniProt accession no.
storage temp.
−20°C
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General description
Tgfb1 (transforming growth factor-β1 human) is a 25kDa peptide encoded by the gene mapped to human chromosome 19q13.2. TGF-β1 polypeptide is produced as a precursor with hydrophobic signal sequence, pro-region and mature peptide. Cleavage of the precursor at tetrabasic cleavage site results in monomers of carboxy-terminal 112 amino acids. The biologically active form of Tgfb1 exists as a disulphide-linked homodimer. In mammals, three isoforms of TGF-β has been identified : TGF-β1, TGF-β2 and TGF-β3.
Application
Transforming Growth Factor-β1 human has been used in
- reporter gene assay.
- in vitro transfection.
- to study the effect of transforming growth factor-β1 (TGF-β1) on gene array analysis of renal cells.
- to study the association of TGF-β1 with shear stress-dependent upregulation of tissue inhibitor of metalloproteinase-1 in microvascular endothelial cells.
- to study the interaction between TGF-β1 activation and myofibroblast formation.
Biochem/physiol Actions
TGF-β1 is a multifunctional peptide capable of influencing cell proliferation, tissue growth, differentiation, and other functions in a wide range of cell types. TGF-β1 plays a fundamental role in differentiation by involvement in adipogenesis, myogenesis, chondrogenesis, osteogenesis, epithelial cell differentiation and immune cell function. All cells possess a specific TGF-β1 receptor. Both transformed and non-neoplastic tissues release transforming growth factors.The multi-modal nature of TGF-β1 is seen in its ability to stimulate or inhibit cellular proliferation. TGF-β1 is associated with the developmental and metastasis of colorectal cancer.
Transforming growth factor-β1 (TGF-β1) is produced by many cell types, but is reported to be most concentrated in mammalian platelets, where it is present at approximately four times the level of TGF-β2.
Physical form
Lyophilized from a 0.2 µm filtered solution containing 0.1 % trifluoroacetic acid (TFA) and Trehalose in a 20:1 Trehalose to protein ratio
Preparation Note
Reconstitution: Sterile 10 mM HCl at 0.1 mg/mL
Analysis Note
The biological activity of TGF-β1 is measured in culture by inhibition of mouse IL-4-dependent proliferation of mouse HT-2 cells.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Interplay between TGF-β signaling and receptor tyrosine kinases in tumor development.
Shi Q and Chen YG
Science China: Life Sciences, 60(10), 1133-1141 (2017)
Matrix metalloproteinase inhibition delays wound healing and blocks latent transforming growth factor-β1 promoted myofibroblast formation and function
Mirastschijski U, et al.
Wound Repair and Regeneration, 18(2), 223-234 (2010)
Tibor Kempf et al.
Clinical chemistry, 53(2), 284-291 (2006-12-23)
Growth-differentiation factor 15 (GDF15) is a member of the transforming growth factor beta (TGF-beta) cytokine superfamily. There has been increasing interest in using circulating GDF15 as a biomarker in patients, for example those with cardiovascular disease. We developed an IRMA
Transforming growth factor β and platelet-derived growth factor modulation of myofibroblast development from corneal fibroblasts in vitro
Singh V, et al.
Experimental Eye Research, 120, 152-160 (2014)
Endothelial cell TIMP-1 is upregulated by shear stress via Sp-1
and the TGF1 signaling pathways
and the TGF1 signaling pathways
Uchida C and Haas TL
Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire, 92.1, 77-83 (2013)
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