EPHA2 Human
EPH Receptor A2 Human Recombinant
Cat. No.
BT1964
Source
HEK 293.
Synonyms
EPHA2, EPH Receptor A2, ECK, Tyrosine-Protein Kinase Receptor ECK, EC 2.7.10.1, CTRCT6, ARCC2, CTPP1, CTPA, Epithelial Cell Receptor Protein Tyrosine Kinase, Ephrin Type-A Receptor 2, Soluble EPHA2 Variant 1, Epithelial Cell Kinase, EC 2.7.10, EphA2.
Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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In Stock 
Description
EPHA2 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Ala24-Glu530) containing a total of 515 amino acids, having a calculated molecular mass of 56.9kDa. The EPHA2 protein is fused to a 2 aa C-terminal linker and a 6 aa C-terminal His tag.
Product Specs
Introduction
EPHA2, or EPH Receptor A2, belongs to the ephrin receptor subfamily within the protein-tyrosine kinase family. This protein interacts with ephrin-A ligands. EPH and related receptors play crucial roles in developmental processes, particularly in the nervous system. EPH subfamily receptors typically possess a single kinase domain and an extracellular region comprising a cysteine-rich domain and two fibronectin type III repeats. Classification of ephrin receptors into two groups is based on the similarities in their extracellular domain sequences and their binding affinities for ephrin-A and ephrin-B ligands. Notably, mutations in the EPHA2 gene have been linked to specific hereditary cataract disorders.
Description
Recombinant Human EPHA2, produced in HEK cells, is a single-chain glycoprotein. It consists of 515 amino acids (Ala24-Glu530) with a 2-amino acid C-terminal linker and a 6-amino acid C-terminal His tag. This results in a calculated molecular weight of 56.9 kDa.
Physical Appearance
The product appears as a white powder following lyophilization (freeze-drying) and filtration.
Formulation
The EPHA2 protein undergoes filtration (0.4 μm) and lyophilization from a solution containing 0.5 mg/ml EPHA2 in phosphate-buffered saline with 5% (w/v) trehalose.
Solubility
To create a working stock solution, add deionized water to the lyophilized pellet, aiming for a concentration of approximately 0.5 mg/ml. Ensure complete dissolution of the pellet. Note: This product is not sterile. Before cell culture use, filter it through a sterile filter of appropriate pore size.
Stability
Store the lyophilized protein at -20°C. After reconstitution, aliquot the protein to minimize freeze-thaw cycles. Reconstituted EPHA2 remains stable at 4°C for a limited duration, showing no noticeable changes for up to two weeks.
Purity
Purity is determined to be greater than 95.0% via SDS-PAGE analysis.
Synonyms
EPHA2, EPH Receptor A2, ECK, Tyrosine-Protein Kinase Receptor ECK, EC 2.7.10.1, CTRCT6, ARCC2, CTPP1, CTPA, Epithelial Cell Receptor Protein Tyrosine Kinase, Ephrin Type-A Receptor 2, Soluble EPHA2 Variant 1, Epithelial Cell Kinase, EC 2.7.10, EphA2.
Source
HEK 293.
Amino Acid Sequence
AQGKEVVLLD FAAAGGELGW LTHPYGKGWD LMQNIMNDMP IYMYSVCNVM SGDQDNWLRT NWVYRGEAER IFIELKFTVR DCNSFPGGAS SCKETFNLYY AESDLDYGTN FQKRLFTKID TIAPDEITVS SDFEARHVKL NVEERSVGPL TRKGFYLAFQ DIGACVALLS VRVYYKKCPE LLQGLAHFPE TIAGSDAPSL ATVAGTCVDH AVVPPGGEEP RMHCAVDGEW LVPIGQCLCQ AGYEKVEDAC QACSPGFFKF EASESPCLEC PEHTLPSPEG ATSCECEEGF FRAPQDPASM PCTRPPSAPH YLTAVGMGAK VELRWTPPQD SGGREDIVYS VTCEQCWPES GECGPCEASV RYSEPPHGLT RTSVTVSDLE PHMNYTFTVE ARNGVSGLVT SRSFRTASVS INQTEPPKVR LEGRSTTSLS VSWSIPPPQQ SRVWKYEVTY RKKGDSNSYN VRRTEGFSVT LDDLAPDTTY LVQVQALTQE GQGAGSKVHE FQTLSPEKLH HHHHH.
Product Science Overview
Structure and Function
Biological Roles
EPHA2 plays a crucial role in regulating cell adhesion, differentiation, and migration. It is involved in various developmental processes, such as:
- Angiogenesis: Formation of new blood vessels.
- Early hindbrain development.
- Epithelial proliferation and branching morphogenesis during mammary gland development .
Additionally, EPHA2 has been shown to regulate tumor cell growth, migration, and invasiveness. It is frequently overexpressed and functionally altered in aggressive tumor cells, promoting metastatic characteristics .
Mechanism of Action
Applications
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