YRP11256-01 [Polyclonal Antibody]
EPS15 Rabbit Polyclonal Antibody
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Species:   Rabbit
Applications:   IHC IF
Immunogen Range:   KLH conjugated synthetic peptide derived from human EPS15
Clonality:   Polyclonal Antibody
Isotype:   IgG
GENE ID:  
Swiss Prot:  
Synonyms:   AF 1P, AF 1p protein, AF1P, ALL1 fused gene from chromosome 1, Epidermal growth factor receptor pathway substrate 15, Epidermal growth factor receptor substrate 15, EPS 15, MLLT 5, MLLT5, Protein Eps 15, Protein Eps15, EPS15_HUMAN.
Purification:   Purified by Protein A.
Storage:   Aqueous buffered solution containing 100ug/ml BSA, 50% glycerol and 0.09% sodium azide. Store at -20℃ for 12 months
Background:   Elucidation of the mechanism by which receptor tyrosine kinases (RTKs) modulate cellular physiology in response to stimuli is critical to the understanding of growth regulation. Miscues in RTK signaling pathways can result in cellular transformation and ultimately in cancer. Two novel EGF receptor substrates designated EGF-receptor pathway substrates 8 and 15, or Eps8 and Eps15, have been described. Eps8 and Eps15 are proteins, respectively that become tyrosine phosphorylated subsequent to EGF stimulation. Overexpression of Eps15 in NIH/3T3 cells causes cellular transformation, implying involvement in the regulation of cell proliferation. Eps15 is capable of binding the amino terminal portion of Crk via a conserved proline-rich domain, characteristic of all Crk binding proteins (5). Overexpression of Eps8 in both fibroblasts and hematopoietic cells results in an increased mitogenic response to EGF. Eps8 has been shown to associate with the EGF receptor despite its lack of a functional SH2 domain. Further characterization suggests the protein has both a PH domain and a SH3 domain, the functional significance of which are not yet known.
Caculated MW:   /
Observed MW:   Refer to Figures
Applications:   IHC 1:100-1:500
IF 1:50-1:200
Reacitivity:   Human, Mouse, Rat
For research use only. Not intended for diagnostic or therapeutic use!
Additional information