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Rat E-Cadherin / CDH1 / E-cad / CD324 Protein (His Tag)

CDH1

Catalog Number P80274-R08H
Organism Species Rat
Host Human Cells
Synonyms CDH1
Molecular Weight The recombinant rat CDH1 comprises 702 amino acids and predicts a molecular mass of 78.4 kDa. The apparent molecular mass of the recombinant protein is approximately 79 kDa in SDS-PAGE under reducing conditions due to glycosylation.
predicted N Gln 24
SDS-PAGE
Purity > 85 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the rat CDH1 (Q9R0T4) (Met1-Ala713) was expressed with a polyhistidine tag at the C-terminus.
Bio-activity
Research Area Cancer |Invasion microenvironment |Adhesion molecule |Cell adhesion |Cadherins
Formulation Lyophilized from sterile PBS, pH 7.4.
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Cadherins are calcium-dependent cell adhesion proteins which preferentially interact with themselves in a homophilic manner in connecting cells, and thus may contribute to the sorting of heterogeneous cell type. E-cadherin (E-Cad), also known as CDH1 and CD324, is a calcium-dependent cell adhesion molecule the intact function of which is crucial for the establishment and maintenance of epithelial tissue polarity and structural integrity. Mutations in CDH1 occur in diffuse type gastric cancer, lobular breast cancer, and endometrial cancer. In human cancers, partial or complete loss of E-cadherin expression correlates with malignancy. During apoptosis or with calcium influx, E-Cad is cleaved by the metalloproteinase to produce fragments of about 38 kDa (E-CAD/CTF1), 33 kDa (E-CAD/CTF2) and 29 kDa (E-CAD/CTF3), respectively. E-Cad has been identified as a potent invasive suppressor, as downregulation of E-cadherin expression is involved in dysfunction of the cell-cell adhesion system, and often correlates with strong invasive potential and poor prognosis of human carcinomas.
Reference
  • Wang HD, et al. (2004) CDH1 germline mutation in hereditary gastric carcinoma. World J Gastroenterol. 10(21): 3088-93.
  • Masterson J, et al. (2007) Posttranslational truncation of E-cadherin and significance for tumour progression. Cells Tissues Organs. 185(1-3): 175-9.
  • Mrgineanu E, et al. (2008) Correlation between E-cadherin abnormal expressions in different types of cancer and the process of metastasis. Rev Med Chir Soc Med Nat Iasi. 112(2): 432-6.