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Recombinant Canine Amphiregulin Protein

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DataSheet   

The recombinant canine AREG protein is derived from in vitro expression of canine AREG 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: GR122143 Categories: , Tag:

Description

Genorise Recombinant Canine Amphiregulin Protein Summary

Alternative names for amphiregulin: AREG

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 AREG.
Accession # A0A8C0QJI3
N-Terminal Sequence Analysis Ser
Amino Acid Sequence Ser101-Ala253
Predicted Molecular Mass 17 kDa
SDS-PAGE 32 kDa, reducing conditions

 

Background: 

Amphiregulin (AREG) is a transmembrane glycoprotein with 252 amino acids that is encoded by the AREG gene.[1][2] AREG is a member of the epidermal growth factor (EGF) family and a critical autocrine growth factor as well as a mitogen for astrocytes, Schwann cells, and fibroblasts. It is a ligand for EGF and related to transforming growth factor alpha (TGF-alpha). AREG interacts with the EGF receptor (EGFR) to promote the growth of normal epithelial cells. AREG is a critical factor in estrogen action and ductal development of the mammary glands.[3][4] Amphiregulin is essential for mammary ductal development, as evidenced by absence of ductal growth in amphiregulin knockout mice,[4] a similar phenotypes of EGFR and ERα knockout mice.[4] Amphiregulin is expressed in many tissues and can be induced by TGF-α, TNF-α, interleukin 1, and prostaglandins.[5] Overexpression of amphiregulin is connected with various cancer.[5] Expression of AREG is connected with proliferation of fibroblasts and production of proinflammatory cytokines interleukin 8 and vascular endothelial growth factor (VEGF).[6] Gene mutations are associated with a psoriasis-like skin phenotype.[16] Higher circulating levels of amphiregulin are associated with AGVHD progression.[7] Amphiregulin is part of cellular response type 2.[8] It was found that the cell source of amphiregulin is innate lymphoid cells 2 (ILC2) which are dependent on interleukin 33. ILC2 expressed amphiregulin after tissue damage of the intestines and activation by IL-33. Moreover, endogenous AREG with IL-33 decreased the intestinal inflammation in mice with normal count of T-lymphocytes and in deficient mice.[9]

References

  1. Shoyab M, et al. (1989). Science. 243 (4894 Pt 1): 1074–6.
  2. Plowman GD, et al. (1990). Molecular and Cellular Biology. 10 (5): 1969–81.
  3. Aupperlee MD, et al. (2013). Breast Cancer Research. 15 (3): R44. doi:1186/bcr3431.
  4. McBryan J, et al. (2008). Journal of Mammary Gland Biology and Neoplasia. 13 (2): 159–69.
  5. Busser B, et al. (2011). Biochimica et Biophysica Acta- Reviews on Cancer. 1816 (2): 119–31.
  6. Yamane S, et al. (2008). Journal of Inflammation. 5: 5.
  7. Bhagavathula N, et al. (2005). The American Journal of Pathology. 166 (4): 1009–16.
  8. Zaiss DM, et al. (2006). Science. 314 (5806): 1746.
  9. Monticelli LA, et al. (2015). Proc Natl Acad Sci USA. 112 (34): 10762–7.

 

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