Reactivity | MuSpecies Glossary |
Applications | Bioactivity |
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 0.05‑0.3 ng/mL. |
Source | Chinese Hamster Ovary cell line, CHO-derived mouse TGF-beta 2 protein Met1-Ser414 |
Accession # | |
N-terminal Sequence | Ala303 |
Structure / Form | Disulfide-linked homodimer |
Protein/Peptide Type | Recombinant Proteins |
Gene | Tgfb2 |
Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 12.7 kDa. 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. |
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SDS-PAGE | 10 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in HCl with BSA as a carrier protein. |
Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in 4 mM HCl containing at least 0.1% human or bovine serum albumin. |
TGF-beta 2 (transforming growth factor beta 2) is one of three closely related mammalian members of the large TGF-beta superfamily that share a characteristic cysteine knot structure (1‑7). TGF-beta 1, -2 and -3 are highly pleiotropic cytokines proposed to act as cellular switches that regulate processes such as immune function, proliferation and epithelial-mesenchymal transition (1-4). Each TGF-beta isoform has some non-redundant functions; for TGF-beta 2, mice with targeted deletion show defects in development of cardiac, lung, craniofacial, limb, eye, ear and urogenital systems (2). Mouse TGF-beta 2 cDNA encodes a 414 amino acid (aa) precursor that contains a 19 aa signal peptide and a 395 aa proprotein (8). A furin-like convertase processes the proprotein to generate an N-terminal 283 aa latency-associated peptide (LAP) and a C-terminal 112 aa mature TGF- beta 2 (8, 9). Disulfide-linked homodimers of LAP and TGF-beta 2 remain non-covalently associated after secretion, forming the small latent TGF-beta 2 complex (8-10). 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 (9, 10). TGF-beta is activated from latency by pathways that include actions of the protease plasmin, matrix metalloproteases, thrombospondin 1 and a subset of integrins (10). Mature mouse TGF-beta 2 shares 100% aa identity with rat TGF-beta 2, and 97% aa identity with human, porcine, canine, equine and bovine
TGF‑ beta 2. It demonstrates cross-species activity (1). In most cells, TGF-beta 2 signaling begins with binding to a complex of the accessory receptor betaglycan (also known as TGF-beta RIII) and a type II ser/thr kinase receptor termed TGF-beta RII, which then phosphorylates and activates another ser/thr kinase receptor, TGF-beta RI (also called activin receptor-like kinase (ALK) -5), or alternatively, ALK-1. The whole complex phosphorylates and activates Smad proteins that regulate transcription (3, 11, 12). In bone -related cells, however, TGF-beta 2 also signals through TGF-beta RIIB (a splice variant of TGF-beta RII), independently of TGF-beta RIII (13). Use of other signaling pathways that are Smad-independent allows for disparate actions observed in response to TGF-beta in different contexts (11).
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