Recombinant Human TGF-beta 3 (CHO-expressed) Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human TGF-beta 3 (CHO-expressed) Protein, CF 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 0.01-0.04 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human TGF-beta 3 protein
Ala301-Ser412
Accession #
N-terminal Sequence
Ala301
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
TGFB3
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.

Applications/Dilutions

Theoretical MW
13 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.
SDS-PAGE
9-11 kDa, reducing conditions
Publications
Read Publications using
8420-B3/CF 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.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 50 μg/mL in 4 mM HCl.

Notes

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

Alternate Names for Recombinant Human TGF-beta 3 (CHO-expressed) Protein, CF

  • ARVD
  • ARVD1
  • FLJ16571
  • LDS5
  • RNHF
  • TGFB3
  • TGFbeta 3
  • TGF-beta 3
  • TGF-beta3
  • TGF-beta-3
  • transforming growth factor beta-3
  • transforming growth factor, beta 3

Background

TGF­-beta 3 (transforming growth factor-beta 3) is a member of a TGF­-beta superfamily subgroup that is defined by their structural and functional similarities (1-5). TGF-beta 3 and its closely related proteins, TGF-beta 1 and ­ beta 2, act as cellular switches to regulate immune function, cell proliferation, and epithelial-­mesenchymal transition (4, 6, 7). The non-redundant biological effects of TGF-­ beta 3 include involvement in palatogenesis, chondrogenesis, and pulmonary development (1, 2, 7-9). Human TGF­-beta 3 cDNA encodes a 412 amino acid (aa) precursor that contains a 20 aa signal peptide and a 392 aa proprotein. The proprotein is processed by a furin-­like convertase to generate a 220 aa latency-­associated peptide (LAP) and a 112 aa mature TGF­-beta 3 (10, 11). Mature human TGF-­ beta 3 shows 100%, 99%, and 98% aa identity with mouse/dog/horse, rat, and pig TGF-­ beta 3, respectively. TGF-beta 3 is secreted as a latent complex. This latent form of TGF-beta 3 is activated by integrins, thrombospondin-1, plasmin, and matrix metalloproteases (12, 13). It can also be activated by extreme pH and reactive oxygen species (1-5, 12). TGF-beta 3 binds with high affinity to TGF-beta RII, a type II serine/threonine kinase receptor. This receptor then phosphorylates and activates type I serine/threonine kinase receptors, TGF-­ beta RI or ALK-­1, to modulate transcription through Smad phosphorylation (14-16). The divergent biological effects exerted by individual TGF-beta isoforms is dependent upon the recruitment of co-receptors (TGF-­ beta RIII and endoglin) and the subsequent initiation of Smad­-dependent or -independent signaling pathways (15, 17, 18).

  1. Barrio, M.C. et al. (2014) Cells Tissues Organs. [Epub ahead of print; PMID 24861080].
  2. Doetschman, T. et al. (2012) Genesis 50:59.
  3. Mittl, P.R. et al. (1996) Protein Sci. 5:1261.
  4. Sporn, M.B. (2006) Cytokine Growth Factor Rev. 17:3.
  5. Wahl, S.M. et al. (2006) Immunol. Rev. 213:213.
  6. Chang, H. et al. (2002) Endocr. Rev. 23:787.
  7. Dunker, N. and K. Krieglstein (2000) Eur. J. Biochem. 267:6982.
  8. Jin, J.Z. et al. (2014) Dev. Dyn. [Epub ahead of print; PMID 25104574].
  9. Tang, Q.O. et al. (2009) Expert Opin. Biol Ther. 9:689.
  10. Derynck, R. et al. (1988) EMBO J. 7:3737.
  11. Miyazono, K. et al. (1988) J. Biol. Chem. 263:6407.
  12. Munger, J.S. et al. (1997) Kidney Int 51:1376.
  13. Wipff, P.J. and B. Hinz (2008) Eur J Cell Biol 87:601.
  14. Cui, X.M. and C.F. Shuler (2000) Int. J. Dev. Biol. 44:397.
  15. de Caestecker, M. (2004) Cytokine Growth Factor Rev. 15:1.
  16. Nakajima, A. et al. (2007) Dev. Dyn. 236:791.
  17. Iwata, J. et al. (2012) J. Clin. Invest. 122:873.
  18. Gatza, C.E. et al. (2010) Cell. Signal. 22:1163.

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Bioinformatics

Gene Symbol TGFB3
Uniprot