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

Details for Product No. ABIN2008013, Supplier: Log in to see
Protein Name
  • 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
Protein Characteristics
Extracellular Domain, AA 1-535
3
2
1
1
1
1
1
1
1
1
1
1
Origin
Mouse (Murine)
13
3
Source
Human Cells
6
2
2
2
2
1
1
Protein Type
Recombinant
Biological Activity
Active
Purification tag / Conjugate
This EPH Receptor A2 protein is labelled with His tag.
Application
Functional Studies (Func), SDS-PAGE (SDS)
Options
Supplier
Log in to see
Supplier Product No.
Log in to see
Request

Get this product for free

It's quick and easy to submit your validation proposal. I want to validate this product

Learn more

Available images

Characteristics 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
Purity > 98 % as determined by SDS-PAGE
Endotoxin Level < 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.
Background Synonyms: AW545284,Eck,Myk2,Sek-2,Sek2
Molecular Weight 58 kDa, 65 kDa
NCBI Accession NP_034269
Research Area Signaling
Pathways RTK Signaling
Application Notes Optimal working dilution should be determined by the investigator.
Restrictions For Research Use only
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.
Handling Advice Avoid repeated freeze-thaw cycles. It is recommended that the protein be aliquoted for optimal storage.
Storage -20 °C,-80 °C
Storage Comment 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.
Expiry Date 12 months
Supplier Images
 image for EPH Receptor A2 (EPHA2) (Extracellular Domain), (AA 1-535) (Active) protein (His tag) (ABIN2008013) EPH Receptor A2 (EPHA2) (Extracellular Domain), (AA 1-535) (Active) protein (His tag)
Background publications 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).