Recombinant Human Latent TGF-beta 1 Protein, CF

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.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human Latent TGF-beta 1 Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. Recombinant Human Latent TGF-beta 1 (Catalog # 299-LTB) binds to Recombinant Human LRRC32/GARP (Catalog # 6055-LR) with an ED 50 of 3.00-30.0 ng/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived human TGF-beta 1 protein Leu30-Ser390
• Accession #: P01137
• N-terminal Sequence: Leu30 (LAP) & Ala 279 (Mature)
• Protein/Peptide Type: Recombinant Proteins
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 29 kDa (LAP) & 13 kDa (Mature).
  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.
• SDS-PAGE: 36-42 kDa & 9-13 kDa, under reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  12 months from date of receipt, -70 degreesC as supplied. 2 weeks, 2 to 8 degreesC under sterile conditions after opening. 3 months, -20 to -70 degreesC under sterile conditions after opening.
• Buffer: Supplied as a 0.2 μm filtered solution in PBS with Trehalose.

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, CF

• 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).

1. Dunker, N. and K. Krieglstein (2000) Eur. J. Biochem. 267:6982.
2. Wahl, S.M. (2006) Immunol. Rev. 213:213.
3. Chang, H. et al. (2002) Endocr. Rev. 23:787.
4. Derynck, R. et al. (1985) Nature 316:701.
5. 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.
6. Brunner, A.M. et al. (1989) J. Biol. Chem. 264:13660.
7. Miyazono, K. et al. (1991) EMBO J. 10:1091.
8. Oklu, R. and R. Hesketh (2000) Biochem. J. 352:601.
9. Miller, D.M. et al. (1992) Mol. Endocrinol. 6:694.
10. Janssens, K. et al. (2003) J. Biol. Chem. 278:7718.

Bioinformatics

• Uniprot:
  • P01137(Human)