E8780
Epiregulin from mouse
recombinant, expressed in E. coli, lyophilized powder, suitable for cell culture
Sinónimos:
EREG
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About This Item
Número MDL:
Código UNSPSC:
12352200
Productos recomendados
recombinante
expressed in E. coli
Análisis
≥97% (SDS-PAGE)
formulario
lyophilized powder
mol peso
predicted mol wt ~5.5 kDa
técnicas
cell culture | mammalian: suitable
impurezas
endotoxin, tested
Nº de acceso UniProt
temp. de almacenamiento
−20°C
Información sobre el gen
mouse ... Ereg(13874)
Acciones bioquímicas o fisiológicas
Binds and activates the tyrosine kinase ErbB family receptors (ErbB1-ErbB4). Inhibits the growth of several epithelial tumor cells and stimulates the growth of fibroblasts and other cell types. Its expression is upregulated in a number of carcinoma cell lines.
Forma física
Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline containing 0.5 mg bovine serum albumin.
Nota de preparación
Recombinant Mouse Epiregulin is produced from a DNA sequence encoding the mature mouse epiregulin protein sequence. The protein is expressed in E. coli.
Epiregulin is a member of EGF (epidermal growth factor) family. All members of the EGF family are synthesized as transmembrane precursors and converted to soluble forms by proteolytic cleavage. Epiregulin was originally purified from the mouse fibroblast-derived tumor cell line NIH3T3/T7. Mouse epiregulin cDNA encodes a transmembrane precursorof 162 amino acids with a mature soluble form consisting of residues 56-101. Epiregulin acts like other EGF family members by binding to and activating the tyrosine kinase ErbB family receptors (ErbB1-ErbB4). Epiregulin has a broad specificity, but this ligand seems to preferentially activate heterodimeric receptor complexes. Epiregulin inhibits the growth of several epithelial tumor cells and stimulates the growth of fibroblasts and other types of cells. Its expression is upregulated in a number of carcinoma cell lines. Epiregulin is also an autocrine growth factor in human epidermal keratinocytes, and involved in the early stages of pregnancy, regulating the attachment of the blastocyst to the uterine epithelium during the implantation process.
Epiregulin is a member of EGF (epidermal growth factor) family. All members of the EGF family are synthesized as transmembrane precursors and converted to soluble forms by proteolytic cleavage. Epiregulin was originally purified from the mouse fibroblast-derived tumor cell line NIH3T3/T7. Mouse epiregulin cDNA encodes a transmembrane precursorof 162 amino acids with a mature soluble form consisting of residues 56-101. Epiregulin acts like other EGF family members by binding to and activating the tyrosine kinase ErbB family receptors (ErbB1-ErbB4). Epiregulin has a broad specificity, but this ligand seems to preferentially activate heterodimeric receptor complexes. Epiregulin inhibits the growth of several epithelial tumor cells and stimulates the growth of fibroblasts and other types of cells. Its expression is upregulated in a number of carcinoma cell lines. Epiregulin is also an autocrine growth factor in human epidermal keratinocytes, and involved in the early stages of pregnancy, regulating the attachment of the blastocyst to the uterine epithelium during the implantation process.
Nota de análisis
The biological activity is measured by its ability to stimulate the 3H-thymidine incorporation in a mouse fibroblast cell line, Balb/3T3.
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
Eyeshields, Gloves, type N95 (US)
Certificados de análisis (COA)
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K Hashimoto
Journal of dermatological science, 24 Suppl 1, S46-S50 (2001-01-04)
Various kinds of growth factors are involved in the regulation of human keratinocyte function. Among them, the epidermal growth factor (EGF) family and the transforming growth factor-beta (TGF-beta) family play central roles, providing dual-mode regulation of keratinocyte growth through the
H Toyoda et al.
FEBS letters, 377(3), 403-407 (1995-12-27)
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