EPH Receptor A2 (EPHA2) (Extracellular Domain), (AA 1-535) (Active) protein (His tag)

Details zu Produkt Nr. ABIN2008014, Anbieter: Anmelden zum Anzeigen
Proteinname
  • EPHA2
  • epha2
  • MGC89505
  • ARCC2
  • CTPA
  • CTPP1
  • CTRCT6
  • ECK
  • AW545284
  • Eck
  • Myk2
  • Sek-2
  • Sek2
  • EPH receptor A2
  • EphA2
  • epoxide hydrolase
  • Eph receptor A2
  • EPHA2
  • epha2
  • ephA2
  • Epha2
Proteineigenschaft
Extracellular Domain, AA 1-535
3
2
1
1
1
1
1
1
1
1
1
1
1
1
Spezies
Maus
13
4
Quelle
Human Cells
6
2
2
2
2
2
1
Protein-Typ
Recombinant
Biologische Aktivität
Active
Aufreinigungstag / Konjugat
Dieses EPH Receptor A2 Protein ist gelabelt mit His tag.
Applikation
Functional Studies (Func), SDS-PAGE (SDS)
Optionen
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Produktmerkmale The secreted recombinant mouse EPHA2 consists of 523 amino acids and has a predicted molecular mass of 58 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rmEPHA2 is approximately 65 kDa due to glycosylation.

Protein Structure: A DNA sequence encoding the mouse EPHA2 (NP_034269.2) extracellular domain (Met 1-Asn 535) was expressed, fused with a polyhistidine tag at the C-terminus.
Predicted N-Term: Gln 24
Reinheit > 98 % as determined by SDS-PAGE
Endotoxin-Niveau < 1.0 EU per μg of the protein as determined by the LAL method
ProductDetails: Biological Activity Comment Measured by its binding ability in a functional ELISA.
1. Immobilized mouse EphA2 at 2μg/ml (100 μl/well) can bind mouse EphrinA1 with a linear range of 0.16-20 ng/ml.
2. Immobilized mouse EphA2 at 2 μg/ml (100 μl/well) can bind human EphrinA1 with a linear range of 0.8-20 ng/ml.
Hintergrund Synonyms: AW545284,Eck,Myk2,Sek-2,Sek2
Molekulargewicht 58 kDa, 65 kDa
NCBI Accession NP_034269
Forschungsgebiet Signaling
Pathways RTK Signalweg
Applikationshinweise Optimal working dilution should be determined by the investigator.
Beschränkungen Nur für Forschungszwecke einsetzbar
Format Lyophilized
Buffer Lyophilized from sterile 20 mM Tris, 150 mM NaCl, pH 7.5
Normally 5 % - 8 % trehalose, mannitol and 0.01 % Tween80 are added as protectants before lyophilization.
Handhabung Avoid repeated freeze-thaw cycles. It is recommended that the protein be aliquoted for optimal storage.
Lagerung -20 °C,-80 °C
Informationen zur Lagerung Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Shipping: In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Haltbarkeit 12 months
Bilder des Herstellers
 image for EPH Receptor A2 (EPHA2) (Extracellular Domain), (AA 1-535) (Active) protein (His tag) (ABIN2008014) EPH Receptor A2 (EPHA2) (Extracellular Domain), (AA 1-535) (Active) protein (His tag)
Allgemeine Veröffentlichungen Zhang, Njauw, Park, Naruse, Asano, Tsao: "EphA2 is an essential mediator of UV radiation-induced apoptosis." in: Cancer research, Vol. 68, Issue 6, pp. 1691-6, 2008 (PubMed).

Rikova, Guo, Zeng, Possemato, Yu, Haack, Nardone, Lee, Reeves, Li, Hu, Tan, Stokes, Sullivan, Mitchell, Wetzel, Macneill, Ren, Yuan, Bakalarski, Villen, Kornhauser, Smith, Li, Zhou, Gygi, Gu et al.: "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. ..." in: Cell, Vol. 131, Issue 6, pp. 1190-203, 2007 (PubMed).

Gerhard, Wagner, Feingold, Shenmen, Grouse, Schuler, Klein, Old, Rasooly, Good, Guyer, Peck, Derge, Lipman, Collins, Jang, Sherry, Feolo, Misquitta, Lee, Rotmistrovsky, Greenhut, Schaefer, Buetow et al.: "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). ..." in: Genome research, Vol. 14, Issue 10B, pp. 2121-7, 2004 (PubMed).

Murai, Pasquale: "'Eph'ective signaling: forward, reverse and crosstalk." in: Journal of cell science, Vol. 116, Issue Pt 14, pp. 2823-32, 2003 (PubMed).

Nowakowski, Cronin, McRee, Knuth, Nelson, Pavletich, Rogers, Sang, Scheibe, Swanson, Thompson: "Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography." in: Structure (London, England : 1993), Vol. 10, Issue 12, pp. 1659-67, 2002 (PubMed).