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|Purity Confirmation||> 98% by SDS-PAGE & HPLC analyses|
|Molecular Weight||25 kDa|
|Endotoxin Levels||< 0.1 ng/µg of protein (<1EU/µg)|
|Biological Activity||The ED50 was determined by TGF-β1’s ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells is ≤ 0.05 ng/ml (≥ 2 x 107 units/mg).|
|Species Reactivity||Chicken, Cow, Dog, Frog, Monkey, Mouse, Pig, Rat, Human, Donkey, Rabbit|
|Reconstitution||Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at ‑20°C to -80°C.|
|Stability and Storage||The lyophilized protein is stable at room temperature for 1 month and at 4°C for 6 months. Reconstituted working aliquots are stable for 1 week at 2°C to 8°C and for 12 months at -20°C to -80°C.|
|Description||The three mammalian isoforms of TGF-ß, TGF-ß1, ß2, ß3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes including embryogenesis, tissue remodeling and would healing. They are secreted predominantly as latent complexes which are stored at the cell surface and in the extracellular matrix. The release of biologically active TGF-ß isoform from a latent complex involves proteolytic processing of the complex and /or induction of conformational changes by proteins such as thrombospondin-1. TGF-ß1 is the most abundant isoform secreted by almost every cell type. It was originally identified for its ability to induce phenotypic transformation of fibroblasts and recently it has been implicated in the formation of skin tumors. Recombinant human TGF-ß1 is a 25.0 kDa protein composed of two identical 112 amino acid polypeptide chains linked by a single disulfide bond.|
|Protein Sequence||ALDTNYCFSS TEKNCCVRQL YIDFRKDLGW KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASAAPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS|
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- Negative Control of Cell Migration by Rac1b in Highly Metastatic Pancreatic Cancer Cells Is Mediated by Sequential Induction of Nonactivated Smad3 and Biglycan. H. Otterbein et al., Cancers (Basel). 2019 Dec; 11(12): 1959.
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- RAC1B Suppresses TGF-β-Dependent Chemokinesis and Growth Inhibition through an Autoregulatory Feed-Forward Loop Involving PAR2 and ALK5. H. Otterbein et al., Cancers (Basel). 2019 Aug 20;11(8). pii: E1211.
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- Downregulation of TRAIL-Receptor 1 Increases TGFβ Type II Receptor Expression and TGFβ Signalling Via MicroRNA-370-3p in Pancreatic Cancer Cells. Radke DI et al., Cancers (Basel). 2018 Oct 25;10(11). pii: E399.
- The Role of PAR2 in TGF-β1-Induced ERK Activation and Cell Motility. H. Ungefroren et al., Int J Mol Sci. 2017 Dec; 18(12): 2776.
- TGF-β-Dependent Growth Arrest and Cell Migration in Benign and Malignant Breast Epithelial Cells Are Antagonistically Controlled by Rac1 and Rac1b. C. Melzer et al., Int J Mol Sci. 2017 Jul; 18(7): 1574.
- Negative regulation of TGF-β1-induced MKK6-p38 and MEK-ERK signalling and epithelial-mesenchymal transition by Rac1b. D. Witte et al., Sci Rep. 2017; 7: 17313.
- Epithelial-Mesenchymal Transition in Chronic Rhinosinusitis: Differences Revealed Between Epithelial Cells from Nasal Polyps and Inferior Turbinates. Könnecke M. et al., Arch Immunol Ther Exp (Warsz). 2017 Apr;65(2):157-173.
- Proteinase-activated receptor 2 (PAR2) in hepatic stellate cells – evidence for a role in hepatocellular carcinoma growth in vivo. F. Mußbach et al., Mol Cancer. 2016; 15: 54.
- Proteinase-activated receptor 2 promotes TGF-β-dependent cell motility in pancreatic cancer cells by sustaining expression of the TGF-β type I receptor ALK5. F. Zeeh et al., Oncotarget. 2016 Jul 5; 7(27): 41095–41109.
- TGF-β1 Is Present at High Levels in Wound Fluid from Breast Cancer Patients Immediately Post-Surgery, and Is Not Increased by Intraoperative Radiation Therapy (IORT). S. D. Scherer et al., PLoS One. 2016; 11(9): e0162221.
- Endothelial Cells Derived from Non-malignant Tissues Are of Limited Value as Models for Brain Tumor Vasculature. Lohr J. et al., Anticancer Res. 2015 May;35(5):2681-90.
- Dasatinib blocks transcriptional and promigratory responses to transforming growth factor-beta in pancreatic adenocarcinoma cells through inhibition of Smad signalling: implications for in vivo mode of action. T. Bartscht et al., Mol Cancer. 2015; 14: 199.
- Rac1b negatively regulates TGF-β1-induced cell motility in pancreatic ductal epithelial cells by suppressing Smad signalling. H. Ungefroren et al., Oncotarget. 2014 Jan; 5(1): 277–290.
- Characterization of Spontaneous and TGF-β-Induced Cell Motility of Primary Human Normal and Neoplastic Mammary Cells In Vitro Using Novel Real-Time Technology. K. Mandel et al., PLoS One. 2013; 8(2): e56591.
- TGF-β1-dependent L1CAM expression has an essential role in macrophage-induced apoptosis resistance and cell migration of human intestinal epithelial cells. Schäfer H et al., Oncogene. 2013 Jan 10;32(2):180-9.
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