Eph receptor A4 (EPHA4) pTyr596 Rabbit Polyclonal Antibody
CAT#: AP55848PU-N
Eph receptor A4 (EPHA4) pTyr596 rabbit polyclonal antibody, Aff - Purified
Size: 50 ul
Need it in bulk or conjugated?
Get a free quote
CNY 2,250.00
货期*
2周
规格
Specifications
Product Data | |
Applications | WB |
Recommend Dilution | Western blot: 1:500~1:1000. |
Reactivity | Human, Mouse |
Host | Rabbit |
Clonality | Polyclonal |
Immunogen | Peptide sequence around phosphorylation site of tyrosine 596 (R-T-Y(p)-V-D) derived from Human EPHA4 (KLH-conjugated) |
Specificity | The antibody detects endogenous levels of EPHA4 only when phosphorylated at tyrosine 596 |
Formulation | Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol State: Aff - Purified State: Liquid Ig fraction |
Concentration | lot specific |
Purification | Affinity chromatography using epitope-specific peptide |
Conjugation | Unconjugated |
Storage Condition | Upon receipt, store undiluted (in aliquots) at -20°C. Avoid repeated freezing and thawing. |
Predicted Protein Size | 110 kDa |
Gene Name | EPH receptor A4 |
Database Link | |
Background | Receptor tyrosine kinase which binds membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI-anchored ephrin-A and transmembrane ephrin-B ligands including EFNA1 and EFNB3. Upon activation by ephrin ligands, modulates cell morphology and integrin-dependent cell adhesion through regulation of the Rac, Rap and Rho GTPases activity. |
Synonyms | HEK8, SEK, TYRO1, Ephrin type-A receptor 4 |
Reference Data |
Documents
Product Manuals |
FAQs |
SDS |
Resources
抗体相关资料 |
Customer
Reviews
Loading...