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Recombinant Canine TGF alpha Protein

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DataSheet   

The recombinant canine TGFa protein is derived from in vitro expression of canine TGFA gene in E. coli and purified using his-tag affinity column and can be used in multiple applications such as antigen, cell culture, ELISA and western blot.

Alternative names for TGFa: Transforming growth factor alpha

This product is for Laboratory Research Use Only, not for diagnostic and therapeutic purposes or any other purposes.

CAT: GR122126 Categories: , Tag:

Description

Genorise Recombinant Canine TGF alpha Protein Summary

Alternative names for TGF alpha: Transforming growth factor alpha, TGFa

Alternative names for monkey: Dog

Product Specifications

Purity > 96%, by SDSPAGE under reducing conditions and visualized by silver stain.
Endotoxin Level < 0.01 EU per 1 μg of the protein by the LAL method.
Activity Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. Marquard H (1984) Science 223:1079. The ED50 for this effect is typically 0.1-0.5 ng/mL.
Source E. coli derived canine TGFa.
Accession # A0A8I3Q273
N-Terminal Sequence Analysis Ser
Amino Acid Sequence Ser31-Val160
Predicted Molecular Mass 14 kDa
SDS-PAGE 29 kDa, reducing conditions

 

Background: 

Transforming growth factor alpha (TGF-α) is a protein that is encoded by the TGFA gene.[1] As a member of the epidermal growth factor (EGF) family, TGF-α is a mitogenic polypeptide.[2] The protein becomes activated when binding to receptors capable of protein kinase activity for cellular signaling. The protein, however, is not directly related to TGF-β. TGF-α is a ligand for the epidermal growth factor receptor, which activates a signaling pathway for cell proliferation, differentiation and development. This protein may act as either a transmembrane-bound ligand or a soluble ligand. This gene has been associated with many types of cancers, and it may also be involved in some cases of cleft lip/palate. TGF-α can be produced in macrophages, brain cells, and keratinocytes. TGF-α induces epithelial development. In the stomach, TGF-α is produced within the normal gastric mucosa.[3] TGF-α has been shown to inhibit gastric acid secretion. The biological actions of TGF-α and EGF are similar. When TGF-α binds to EGFR it can initiate multiple cell proliferation events.[4] Cell proliferation events that involve TGF-α bound to EGFR include wound healing and embryogenesis. TGF-α is also involved in tumerogenesis and believed to promote angiogenesis.[5] TGF-α has also been shown to stimulate neural cell proliferation in the adult injured brain.[6] TGF-α is heavily involved in cancer progression (e.g., lung, breast, pancreatic), acts as a biomarker for various tumors, and is associated with Menetrier’s disease, a rare stomach condition. It acts synergistically with TGF-beta to encourage anchorage-independent cell proliferation. Overexpression is associated with gastric cancer, pancreatic cancer, and melanoma. It is also implicated in fibroproliferative diseases and cartilage degradation.

References

  1. Lee DC, et al. (1985). Nature. 313 (6002): 489–491.
  2. Ojeda SR, et al. (1997). Molecular Psychiatry. 2 (5): 355–358.
  3. Coffey RJ, et al. (1995). European Journal of Gastroenterology & Hepatology. 7 (10): 923–7.
  4. McInnes C, et al. (1998). The Journal of Biological Chemistry. 273 (42): 27357–27363.
  5. Ferrer I, et al. (1996). Progress in Neurobiology. 49 (2): 99–123.
  6. Fallon J, et al. (2000). Proc Acad Sci USA. 97 (26): 14686–14691.

 

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