|Application ||WB, LCI|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||108127 Da|
|Other Names||Ephrin type-A receptor 1, hEpha1, EPH tyrosine kinase, EPH tyrosine kinase 1, Erythropoietin-producing hepatoma receptor, Tyrosine-protein kinase receptor EPH, EPHA1, EPH, EPHT, EPHT1|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)KKEPRQLELTWAGSR, corresponding to amino acid residues 457-471 of human EphA1 (Accession P21709). Extracellular, N-terminus.|
|Peptide Confirmation||Confirmed by mass-spectrography and amino acid analysis.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.8 mg/ml.|
|Buffer After Reconstitution||Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.|
|Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Storage After Reconstitution||The reconstituted solution can be stored at 4ºC for up to 2 weeks. For longer periods, small aliquots should be stored at -20ºC or below. Avoid multiple freezing and thawing. The further dilutions should be made using a carrier protein such as BSA (1%). Centrifuge all antibody preparations before use (10000 × g 5 min).|
|Control Antigen Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Control Antigen Reconstitution||100 µl DDW.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||1 µg peptide per 1 µg antibody.|
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Provided below are standard protocols that you may find useful for product applications.
Eph receptors are the largest family of receptor tyrosine kinases (RTKs). EphA receptors (EphA1-10) bind ephrinA ligands which are GPI-linked proteins and EphB receptors (EphB1-6) bind ephrinB ligands which are membrane protein with one transmembrane domain1,2. Within each subfamily, interactions between receptor and ligand are promiscuous. In addition, Eph receptors can also bind ephrins from the other class2. Forward and reverse signaling through Eph receptors is a unique characteristic to this RTK since ephrins are physically linked to the plasma membrane3. Structurally, Eph receptors contain an extracellular ligand-binding domain, a transmembrane domain and an intracellular C-terminal domain responsible for intracellular signaling1. Forward Eph receptor signaling involves autophosphorylation of the receptor via a tyrosine kinase domain, as well as phosphorylation of other proteins. Known effectors of the forward signaling include Src kinase and Ras/Rho GTPases2. Much less is known about the reverse signaling mediated by Eph receptors. Besides from acting independently, Eph receptors can also signal in concert with other receptors. For example, Eph receptors cooperate with FGF receptor, NMDA ligand-gated ion channel and chemokine G-protein coupled receptor2. Biological activities attributed to the Eph receptor-ephrin signaling module include establishing neuronal connections, mediating neuronal plasticity and repair following neuronal injury2,4. Eph receptors may also have a role in the immune system5. Eph receptors are expressed in the developing nervous system, and in the adult brain. It is also detected in the pancreas, intestine, bone and lymphocytes. In cancer cells, Eph receptors and ephrins are overexpressed2,6,7. They are also implicated in neurodegenerative disorders like Alzheimer’s disease1. Abgent is pleased to offer a highly specific antibody directed against an extracellular epitope of human EphA1. Anti-EphA1 (extracellular) antibody (#AG1283) can be used in western blot, immunocytochemistry and indirect flow cytometry applications. It has been designed to recognize EphA1 from rat, mouse, and human samples.
References 1. Chen, Y. et al. (2012) Cell. Signal. 24, 606. 2. Pasquale, E.B. (2008) Cell 133, 38. 3. Pasquale, E.B. (2005) Mol. Cell Biol. 6, 462. 4. Du, J. et al. (2007) Curr. Pharm. Des. 13, 2507. 5. Wu, J. and Luo, H. (2005) Curr. Opin. Hematol. 12, 292. 6. Ireton, R.C. and Chen, J. (2005) Curr. Cancer Drug Targets 5, 149. 7. Noren, N.K. and Pasquale, E.B. (2007) Cancer Res. 67, 3994.
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