Key Specifications Table
|CULT||Mouse||Male mouse submaxillary glands|
|Description||Epidermal growth factor (EGF), culture grade|
|Presentation||Lyophilized from a solution containing trace sodium acetate|
|Application||This Epidermal growth factor (EGF), culture grade product is available in a 100 µg format.|
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||Lyophilized: Stable for 2 years at 4°C from date of shipment.
Rehydrated: Stable for 2 months at -20°C. Aliquot to avoid repeated freezing and thawing.
|Material Size||100 µg|
|Reference overview||Application||Pub Med ID|
|Interplay of the proto-oncogene proteins CrkL and CrkII in insulin-like growth factor-I receptor-mediated signal transduction|
Koval, A. P., et al
J Biol Chem, 273:14780-7 (1998) 1998
|Replacement of tyrosine 1251 in the carboxyl terminus of the insulin-like growth factor-I receptor disrupts the actin cytoskeleton and inhibits proliferation and anchorage-independent growth.|
Blakesley, V A, et al.
J. Biol. Chem., 273: 18411-22 (1998) 1998
Insulin-like growth factor (IGF)-I signaling through the IGF-I receptor modulates cellular adhesion and proliferation and the transforming ability of cells overexpressing the IGF-I receptor. Tyrosine phosphorylation of intracellular proteins is essential for this transduction of the IGF-I-induced mitogenic and tumorigenic signals. IGF-I induces specific cytoskeletal structure and the phosphorylation of proteins in the associated focal adhesion complexes. The determination of the exact pathways emanating from the IGF-I receptor that are involved in mediating these signals will contribute greatly to the understanding of IGF-I action. We have previously shown that replacement of tyrosine residues 1250 and 1251 in the carboxyl terminus of the IGF-I receptor abrogates IGF-I-induced cellular proliferation and tumor formation in nude mice. In this study, replacement of either tyrosine 1250 or 1251 similarly reduces the cells ability to grow in an anchorage-independent manner. The actin cytoskeleton and cellular localization of vinculin are disrupted by replacement of tyrosine 1251. Tyrosine residues 1250 and 1251 are not essential for tyrosine phosphorylation of two known substrates; insulin receptor substrate-1 and SHC, nor association of known downstream adaptor proteins to these substrates. In addition, these mutant IGF-I receptors do not affect IGF-I-stimulated p42/p44 mitogen-activated protein kinase activation or phosphatidylinositol (PI) 3'-kinase activity. Thus, it appears that in fibroblasts expressing tyrosine 1250 and 1251 mutant IGF-I receptors, the signal transduction pathways impacting on mitogenesis and tumorigenesis do not occur exclusively through the PI 3'-kinase or mitogen-activated protein kinase pathways.
|The catalytic domain of protein kinase C chimeras modulates the affinity and targeting of phorbol ester-induced translocation|
Acs, P., et al
J Biol Chem, 272:22148-53 (1997) 1997
|Both the catalytic and regulatory domains of protein kinase C chimeras modulate the proliferative properties of NIH 3T3 cells|
Acs, P., et al
J Biol Chem, 272:28793-9 (1997) 1997
|Insulin-like growth factor-I stimulates tyrosine phosphorylation of endogenous c-Crk|
Beitner-Johnson, D. and LeRoith, D.
J Biol Chem, 270:5187-90 (1995) 1995
|Insulin stimulates the tyrosine phosphorylation of caveolin|
Mastick, C. C., et al
J Cell Biol, 129:1523-31 (1995) 1995
|35H, a sequence isolated as a protein kinase C binding protein, is a novel member of the adducin family.|
Dong, L, et al.
J. Biol. Chem., 270: 25534-40 (1995) 1995
We recently cloned a partial cDNA (35H) for a protein kinase C (PKC) binding protein from a rat kidney cDNA library and demonstrated that it is a PKC substrate in vitro (Chapline, C., Ramsay, K., Klauck, T., and Jaken, S. (1993) J. Biol. Chem. 268, 6858-6861). Additional library screening and 5' rapid amplification of cDNA ends were used to obtain the complete open reading frame. Amino acid sequence analysis, DNA sequence analysis, and Northern analysis indicate that 35H is a unique cDNA related to alpha-and beta-adducins. Antisera prepared to the 35H bacterial fusion protein recognized two polypeptides of 80 and 90 kDa on immunoblots of kidney homogenates and cultured renal proximal tubule epithelial cell extracts. The 35H-related proteins were similar to alpha- and beta-adducins in that they were preferentially recovered in the Triton X-100-insoluble (cytoskeletal, CSK) fraction of cell extracts and were predominantly localized to cell borders. Phorbol esters stimulated phosphorylation of CSK 35H proteins, thus emphasizing that sequences isolated according to PKC binding activity in vitro are also PKC substrates in vivo. The phosphorylated forms of the 35H proteins were preferentially recovered in the soluble fraction, thus demonstrating that phosphorylation regulates their CSK association and, thereby, their function in regulating cytoskeletal assemblies. We have isolated another PKC binding protein partial cDNA (clone 45) from a rat fibroblast library with substantial homology to alpha-adducin. Antisera raised against this expressed sequence recognized a protein of 120 kDa, the reported size of alpha-adducin, on immunoblots of renal proximal tubule epithelial cell extracts. A 120-kDa protein that cross-reacts with the clone 45 (alpha-adducin) antisera coprecipitated with 35H immunecomplexes, indicating that alpha-adducin associates with 35H proteins in vivo. Taken together, these results indicate that 35H is a new, widely expressed form of adducin capable of forming heterodimers with alpha-adducin. We propose naming this adducin homologue gamma-adducin.
|Phosphorylation of the human leukemia inhibitory factor (LIF) receptor by mitogen-activated protein kinase and the regulation of LIF receptor function by heterologous receptor activation|
Schiemann, W. P., et al
Proc Natl Acad Sci U S A, 92:5361-5 (1995) 1995
|Epidermal growth factor.|
In Vitro Cell. Dev. Biol., 23: 239-46 (1987) 1987