Ephrin Type A Receptor 1 (EPHA1) antibody

Details for Product No. ABIN149243
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Antigen
Synonyms EPH, EPHT, EPHT1, 5730453L17Rik, AL033318, Eph, Esk, EPHA9
Reactivity
Human
(44), (6), (1)
Host
Goat
(30), (15)
Clonality
Polyclonal
Application
Western Blotting (WB), ELISA
(45), (31), (17), (14), (9), (6), (5), (3), (1)
Pubmed 9 references available
Catalog no. ABIN149243
Quantity 50 µg
Price
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Immunogen Recombinant fragment (extracellular domain) (Human). Expressed in NSO cells.
Isotype IgG
Specificity The antibody will recognize recombinant human EphA1 by immunoblotting and ELISA. By immunoblotting and ELISA, the antibody shows approximately 40% cross-reactivity with recombinant mouse EphA3, mouse EphA8, mouse EphA4, rat EphA5 and 10% cross-reactivity
Purification Immunogen affinity purified
Alternative Name EPHA1
Background EphA1 (the antigen to this antibody) is also known as Eph and Esk and binds to ephrin-A1. To date, at least 14 members of the Eph receptor family and a family of 8 ligands have been identified. Ligands of Eph family receptors are structurally related membrane-bound proteins that can be subdivided into two major subclasses, ephrin-A and ephrin-B (Gale et al.). Ligands in the ephrin-A subclass, including the prototype family member ephrin-A1 (B61), are membrane associated through glycosyl phosphatidyl-inositol linkages, whereas ephrin-B subclass consists of ligands with transmembrane domains. The general role of the Eph family is in mediating repulsive cell-cell interaction, as suggested by studies of axonal guidance (Cheng et al., Drescher et al., Nakamoto et al., and Henkemeyer et al.) And neural crest cell migration (Krull et al., Smith et al., and Wang et al.).
Application Notes I-ELISA: Use at a concentration of 0.5-1.0 ug/ml. WB (colorimetric): Use at a concentration of 0.1-0.2 ug/ml. Not tested in other applications. Optimal dilutions/concentrations should be determined by the end user.
Restrictions For Research Use only
Buffer 0.01M Na phosphate, 0.15M NaCl, pH7.6
Preservative Sodium azide, Thimerosal (Merthiolate)
Storage 4 °C
General Fraser, Keynes, Lumsden: "Segmentation in the chick embryo hindbrain is defined by cell lineage restrictions." in: Nature, Vol. 344, Issue 6265, pp. 431-5, 1990 (PubMed).

Drescher, Kremoser, Handwerker et al.: "In vitro guidance of retinal ganglion cell axons by RAGS, a 25 kDa tectal protein related to ligands for Eph receptor tyrosine kinases." in: Cell, Vol. 82, Issue 3, pp. 359-70, 1995 (PubMed).

Cheng, Nakamoto, Bergemann et al.: "Complementary gradients in expression and binding of ELF-1 and Mek4 in development of the topographic retinotectal projection map." in: Cell, Vol. 82, Issue 3, pp. 371-81, 1995 (PubMed).

Henkemeyer, Orioli, Henderson et al.: "Nuk controls pathfinding of commissural axons in the mammalian central nervous system." in: Cell, Vol. 86, Issue 1, pp. 35-46, 1996 (PubMed).

Gale, Holland, Valenzuela et al.: "Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis." in: Neuron, Vol. 17, Issue 1, pp. 9-19, 1996 (PubMed).

Nakamoto, Cheng, Friedman et al.: "Topographically specific effects of ELF-1 on retinal axon guidance in vitro and retinal axon mapping in vivo." in: Cell, Vol. 86, Issue 5, pp. 755-66, 1996 (PubMed).

Wang, Anderson: "Eph family transmembrane ligands can mediate repulsive guidance of trunk neural crest migration and motor axon outgrowth." in: Neuron, Vol. 18, Issue 3, pp. 383-96, 1997 (PubMed).

Smith, Robinson, Patel et al.: "The EphA4 and EphB1 receptor tyrosine kinases and ephrin-B2 ligand regulate targeted migration of branchial neural crest cells." in: Current biology : CB, Vol. 7, Issue 8, pp. 561-70, 1997 (PubMed).

Krull, Lansford, Gale et al.: "Interactions of Eph-related receptors and ligands confer rostrocaudal pattern to trunk neural crest migration." in: Current biology : CB, Vol. 7, Issue 8, pp. 571-80, 1997 (PubMed).

Hosts (30), (15)
Reactivities (44), (6), (1)
Applications (45), (31), (17), (14), (9), (6), (5), (3), (1)
Epitopes (7), (4), (2), (2), (2), (1), (1), (1), (1), (1), (1)
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