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Porcine TGF-beta 2 Protein

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Reactivity PoSpecies Glossary
Applications Bioactivity

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Porcine TGF-beta 2 Protein Summary

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 0.03-0.18 ng/mL.
Source
Porcine platelet-derived TGF-beta 2 protein
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Natural Proteins
Gene
TGFB2
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
SDS-PAGE
12 kDa, reducing conditions
Publications
Read Publications using
102-B2 in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 1 μg/mL in sterile 4 mM HCl containing at least 0.1% human or bovine serum albumin.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Porcine TGF-beta 2 Protein

  • BSC-1 cell growth inhibitor
  • cetermin
  • Glioblastoma-derived T-cell suppressor factor
  • G-TSF
  • MGC116892
  • polyergin
  • TGFB2
  • TGFbeta 2
  • TGF-beta 2
  • TGF-beta2
  • TGF-beta-2
  • transforming growth factor beta-2
  • transforming growth factor, beta 2

Background

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 are 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). Porcine TGF-beta 2 cDNA encodes a 435 amino acid (aa) precursor that contains a 19 aa signal peptide and a 416 aa proprotein (8). A furin-like convertase processes the proprotein to generate an N-terminal 232 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 1 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 porcine TGF-beta 2 shows 100% aa identity with human, dog, horse and cow TGF-beta 2, and 97% aa identity with mouse and rat TGF-beta 2. It demonstrates cross-species activity (1). 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. This receptor 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). Use of other signaling pathways that are Smad-independent allows for disparate actions observed in response to TGF-beta in different contexts (11).

  1. Sporn, M.B. (2006) Cytokine Growth Factor Rev. 17:3.
  2. Dunker, N. and K. Krieglstein (2000) Eur. J. Biochem. 267:6982.
  3. Wahl, S.M. (2006) Immunol. Rev. 213:213.
  4. Chang, H. et al. (2002) Endocr. Rev. 23:787.
  5. Lin, J.S. et al. (2006) Reproduction 132:179.
  6. Hinck, A.P. et al. (1996) Biochemistry 35:8517.
  7. Mittl, P.R.E. et al. (1996) Protein Sci. 5:1261.
  8. Cheifetz, S. et al. (1987) Cell 48:409.
  9. Miyazono, K. et al. (1988) J. Biol. Chem. 263:6407.
  10. Oklu, R. and R. Hesketh (2000) Biochem. J. 352:601.
  11. de Caestecker, M. et al. (2004) Cytokine Growth Factor Rev. 15:1.
  12. Zuniga, J.E. et al. (2005) J. Mol. Biol. 354:1052.

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Publications for TGF-beta 2 (102-B2)(8)

We have publications tested in 5 confirmed species: Human, Bovine, Mink, Porcine, Xenopus.

We have publications tested in 3 applications: Bioassay, ELISA Standard, In Vivo.


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Bioassay
(6)
ELISA Standard
(1)
In Vivo
(1)
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Human
(2)
Bovine
(1)
Mink
(1)
Porcine
(3)
Xenopus
(1)
All Species
Showing Publications 1 - 8 of 8.
Publications using 102-B2 Applications Species
N Shiraki, K Maruyama, R Hayashi, A Oguchi, Y Murakawa, T Katayama, T Takigawa, S Sakimoto, AJ Quantock, M Tsujikawa, K Nishida PAX6-positive microglia evolve locally in hiPSC-derived ocular organoids Stem Cell Reports, 2022-01-13;0(0):. 2022-01-13 [PMID: 35030319] (Bioassay, Human) Bioassay Human
T Fujimoto, M Inoue-Moch, S Iraha, H Tanihara, T Inoue Suberoylanilide hydroxamic acid (SAHA) inhibits transforming growth factor-beta 2-induced increases in aqueous humor outflow resistance The Journal of Biological Chemistry, 2021-08-11;0(0):101070. 2021-08-11 [PMID: 34389355] (Bioassay, Porcine) Bioassay Porcine
A Yogi, M Rukhlova, C Charlebois, G Tian, DB Stanimirov, MJ Moreno Differentiation of Adipose-Derived Stem Cells into Vascular Smooth Muscle Cells for Tissue Engineering Applications Biomedicines, 2021-07-09;9(7):. 2021-07-09 [PMID: 34356861] (Bioassay, Porcine) Bioassay Porcine
RJ Playford, MJ Weiser, T Marchbank Methods to improve efficacy of orally administered bioactive peptides using bovine colostrum as an exemplar PLoS ONE, 2021-06-17;16(6):e0253422. 2021-06-17 [PMID: 34138960] (ELISA Standard, Bovine) ELISA Standard Bovine
S Holvoet, M Perrot, N de Groot, G Prioult, T Mikogami, V Verhasselt, S Nutten Oral Tolerance Induction to Newly Introduced Allergen is Favored by a Transforming Growth Factor-beta-Enriched Formula Nutrients, 2019-09-13;11(9):. 2019-09-13 [PMID: 31540231] (Bioassay, Mink) Bioassay Mink
Buijs JT, Henriquez NV, van Overveld PG, van der Horst G, Que I, Schwaninger R, Rentsch C, ten Dijke P, Cleton-Jansen AM, Driouch K, Lidereau R, Bachelier R, Vukicevic S, Clezardin P, Papapoulos SE, Cecchini MG, Lowik CW, Van Der Pluijm G Bone morphogenetic protein 7 in the development and treatment of bone metastases from breast cancer. Cancer Res., 2007-09-15;67(18):8742-51. 2007-09-15 [PMID: 17875715] (Bioassay, Human) Bioassay Human
Saika S, Kono-Saika S, Tanaka T, Yamanaka O, Ohnishi Y, Sato M, Muragaki Y, Ooshima A, Yoo J, Flanders KC, Roberts AB Smad3 is required for dedifferentiation of retinal pigment epithelium following retinal detachment in mice. Lab. Invest., 2004-10-01;84(10):1245-58. 2004-10-01 [PMID: 15273699] (Bioassay, Porcine) Bioassay Porcine
Mogi K, Goto M, Ohno E, Azumi Y, Takeuchi S, Toyoizumi R Xenopus neurula left-right asymmetry is respeficied by microinjecting TGF-beta5 protein. Int. J. Dev. Biol., 2003-02-01;47(1):15-29. 2003-02-01 [PMID: 12653248] (In Vivo, Xenopus) In Vivo Xenopus

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Bioinformatics

Gene Symbol TGFB2