Product Name: EphA2 (769-775) pY772
Product Number: PE-04ALX90
Size: | 200 µg | | Price: | 41.00 |
| 1 mg | | $US | 82.00 |
| 5 mg | | | 194.00 |
Peptide Name: EphA2 (769-775) pY772
Product Use: Services as a blocking peptide for use with the EphA2-pY772 rabbit polyclonal antibody (Cat. No.: AB-PK607) that is also available from Kinexus. This phosphopeptide may also be useful as a substrate for screening the phosphatase activity of protein phosphatases. The peptide sequence is located in the protein kinase catalytic domain activation T-loop between subdomains VII and VIII. This is the major in vivo phosphorylation site in EphA2. Y772 phosphorylation is predicted to be stimulatory for phosphotransferase activity.
Peptide Production Method: Solid-phase peptide synthesis
Peptide Origin: Homo sapiens
Peptide Sequence: EAT-pY-TTS
Peptide Modifications N Terminus: Free amino
Peptide Modifications C Terminus: βAla-Cys
Peptide Modifications Other: Phosphorylated
Peptide Molecular Mass Calculated: 1025 Da
Peptide Purity Percent after Synthesis and Purification: >90
Peptide Appearance: White powder
Peptide Form: Solid
Storage Conditions: -20°C
Related Product 1: EphA2 - pY772 phosphosite-specific antibody (Cat. No.: AB-PK607) Scientific Background: EphA2 is a protein-tyrosine kinase of the TK group and Eph family. It is a receptor that displays promiscuous binding to membrane-bound ligands of the ephrin-A family on adjacent cells. It is activated by binding ephrin-A1, A2, A3, A4 or A5. Phosphorylation of Y735 increases phosphotranserase activity and interaction with PIK3R1. EphA2 activation regulates integrin-dependent adhesion, cellular migration, proliferation, and differentiation. EphA2 also participates in bone remodeling by directly regulating both osteoclastogenesis and osteoblastogenesis. EphA2 may be an oncoprotein (OP). Significantly elevated EphA2 expression has been observed in many types of human cancer and appears to be involved in mediating communication between RAS-PI3K/Akt and RAS-MAPK intracellular signalling pathways, which are both known to promote tumourigenesis. Additionally, EphA2 is required for UV-radiation induced apoptosis. UV-radiation is a potent carcinogen responsible for the development of melanoma. However, further characterization of melanoma cell lines revealed either a pro-apoptotic or anti-apoptotic role for EphA2 dependent upon the cellular context. Additionally, studies performed in breast cancer cell lines revealed a link between EphA2 expression levels and changes in cytoskeletal morphology and the recruitment of disintegrin and metalloprotease-10 (MMP10) enzymes, thus suggesting a role for theEphA2 protein in the promotion of tumour invasion and metastasis.