Purified Protein in ready-to-use SDS sample buffer.
Attributs du produit
EphA R8 selective antibodies were generated against a peptide taken from the human protein. The EphA R8-selective antibodies are affinity purified on an immobilized antigen based affinity matrix, the isolated antibodies were then stabilized in antibody stabilization buffer for long-term storage. The EphA R8-selective antibodies are fully characterized for applications in western blotting and ELISA at the recommended dilutions. antibodies-online.com provides EphA8 Western blot positive control samples in SDS-PAGE sample buffer.
EPHA8
Origine: Rat
Hôte: Levure
Recombinant
> 90 %
ELISA
Indications d'application
Antibodies were tested in ELISA and western blotting applications at 1:500 dilution using ABIN1686536 samples. Antibody dilutions for these antibodies are for reference only, investigators are expected to determine the optimal conditions. Application of this antibody in other protocols has not yet tested. WB: > 1:500 IMM & IP pull-down assays: n.d. IHC: n.d. Investigators using this antibody in protocols other than listed above can request a complimentary sample of this antibody. n.d. not necessarily means the antibody is not suitable for that application, it simply means we have not yet characterized the antibody for that application.
Restrictions
For Research Use only
Format
Liquid
Buffer
For 5 applications, volume varies from 100-200 μL in reduced SDS-PAGE sample buffer.
The Ephrin receptors represent the largest group of Receptor Tyrosine Kinases, comprising of 14 members and divided in two subclasses (class A & B ephrin ligands) based on their abilities to bind and activate each other, and on sequence conservation. Ephrin-A (EFNA) class is anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) classes are trans-membrane proteins. Ephrins interact with a variety of membrane receptors that respond to chemokines, neurotransmitters or growth factors. Eph receptors are involved in central nervous system function and development, and in the modulation of different types of nociception. Eph receptors and their ligands play important roles in the regulation of cancer cell migration and invasion and are key regulators of axon guidance. They function in a variety of signaling modes by transducing signals from the cell exterior to the interior through ligand-induced activation of their kinase domain. Ephrin type-A receptor 8 is a protein that in humans is encoded by the EphA R8 gene. EphA8/Eek receptors play a role in axonal path-finding during development of the mammalian nervous system. Ligand-mediated activation of the EphA8 receptor regulates cell adhesion and migration. The tyrosine kinase domain of EphA R8 is important for inducing neurite outgrowth in the absence of ligand stimulation. This receptor is capable of inducing a sustained increase in MAPK (mitogen-activated protein kinase) activity by relocalizing from the cytoplasm to the nucleus in response to EphA R8 transfection, thus promoting neurite outgrowth in neuronal cells. Two major auto phosphorylation sites in EphA r8, Tyr-615 and Tyr-838, are demonstrated by two-dimensional phosphopeptide mapping analysis. Cell attachment responses are attenuated by overexpression of wild type EphA R8 receptor but to less extent by EphA R8 mutants lacking phosphorylation at either Tyr-615 or Tyr-838. The gene for EphA R8 is present on chromosome 1p36.1