Recombinant Human Latent TGF-beta 1 Protein, CF Summary
Product Specifications
Leu30-Ser390
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
299-LTB
Formulation | Supplied as a 0.2 μm filtered solution in PBS with Trehalose. |
Shipping | The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
Recombinant Human Latent TGF-beta 1 (Catalog # 299-LTB) binds to Recombinant Human LRRC32/GARP (6055-LR) with an ED50 of 3.00‑30.0 ng/mL.
2 μg/lane of Recombinant Human Latent TGF‑ beta 1 Protein (Catalog # 299-LTB) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 36-42 kDa & 9-13 kDa, and 70-80 kDa and 18-26 kDa, respectively.
Reconstitution Calculator
Background: TGF-beta 1
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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