Recombinant Human Latent TGF-beta beta 1 (Catalog # 299-LT) after acid activation inhibits Recombinant Mouse IL‑4 (Catalog # 404-ML) induced cell proliferation in the HT-2 mouse T cell line. The ED50 for this effect ...read more
1 μg/lane of Recombinant Human Latent TGF‑ beta 1 was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by silverstaining,showing bands at 11, 36-42 kDa (R) and 24, 80-95 kDa ...read more
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Recombinant Human Latent TGF-beta 1 Protein Summary
Additional Information
Soon to be discontinued. New Cat# will be 299-LTB
Details of Functionality
Measured by its ability to inhibit the IL-4-dependent proliferation of HT‑2 mouse T cells. Tsang, M. et al. (1995) Cytokine 7:389. The ED50 for this effect is 10-70 ng/mL before acid activation and 0.15‑0.9 ng/mL after acid activation.
Source
Chinese Hamster Ovary cell line, CHO-derived human TGF-beta 1 protein Leu30-Ser390
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
28.5 kDa (LAP) & 12.8 kDa (Mature), Monomer. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after opening.
3 months, ≤ -20 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in PBS and Glycerol with BSA as a carrier protein.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Latent TGF-beta 1 Protein
CEDLAP
DPD1
latency-associated peptide
TGF beta
TGF beta1
TGFB
TGFB1
TGF-beta 1 protein
TGFbeta 1
TGF-beta 1
TGFbeta
TGF-beta-1
transforming growth factor beta-1
transforming growth factor, beta 1
Background
TGF- beta 1 (transforming growth factor beta 1) and the closely related TGF-beta 2 and -3 are members of the large TGF-beta superfamily. TGF- beta proteins are highly pleiotropic cytokines that regulate processes such as immune function, proliferation and epithelial-mesenchymal transition (1-3). Human TGF-beta 1 cDNA encodes a 390 amino acid (aa) precursor that contains a 29 aa signal peptide and a 361 aa proprotein (4). A furin-like convertase processes the proprotein within the trans-Golgi to generate an N‑terminal 249 aa latency-associated peptide (LAP) and a C-terminal 112 aa mature TGF-beta 1 (4-6). Disulfide-linked homodimers of LAP and TGF-beta 1 remain non‑covalently associated after secretion, forming the small latent TGF-beta 1 complex (4-8). Purified LAP is also capable of associating with active TGF-beta with high affinity, and can neutralize TGF-beta activity (9). Covalent linkage of LAP to one of three latent TGF-beta binding proteins (LTBPs) creates a large latent complex that may interact with the extracellular matrix (5-7). TGF-beta activation from latency is controlled both spatially and temporally, by multiple pathways that include actions of proteases such as plasmin and MMP9, and/or by thrombospondin 1 or selected integrins (5, 8). The LAP portion of human TGF-beta 1 shares 91%, 92%, 85%, 86% and 88% aa identity with porcine, canine, mouse, rat and equine TGF-beta 1 LAP, respectively, while the mature human TGF-beta 1 portion shares 100% aa identity with procine, canine and bovine TGF-beta 1, and 99% aa identity with mouse, rat and equine TGF-beta 1. Although different isoforms of TGF-beta are naturally associated with their own distinct LAPs, the TGF-beta 1 LAP is capable of complexing with, and inactivating, all other human TGF-beta isoforms and those of most other species (9). Mutations within the LAP are associated with Camurati-Engelmann disease, a rare sclerosing bone dysplasia characterized by inappropriate presence of active TGF-beta 1 (10).
Dunker, N. and K. Krieglstein (2000) Eur. J. Biochem. 267:6982.
Wahl, S.M. (2006) Immunol. Rev. 213:213.
Chang, H. et al. (2002) Endocr. Rev. 23:787.
Derynck, R. et al. (1985) Nature 316:701.
Dabovic, B. and D.B. Rifkin (2008) “TGF-beta Bioavailability” in The TGF-beta Family. Derynck, R. and K. Miyazono (eds): Cold Spring Harbor Laboratory Press, p. 179.
Brunner, A.M. et al. (1989) J. Biol. Chem. 264:13660.
Miyazono, K. et al. (1991) EMBO J. 10:1091.
Oklu, R. and R. Hesketh (2000) Biochem. J. 352:601.
Miller, D.M. et al. (1992) Mol. Endocrinol. 6:694.
Janssens, K. et al. (2003) J. Biol. Chem. 278:7718.
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