Analytical Data
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Gene name
EphA2
- Application
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Alternative Names
Ephrin type-A receptor 2; Epithelial cell kinase; EPHA2; ECK
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Species
Rat
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Source
HEK293
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Tag
C-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
D3ZBN3
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Expression Region
Q24-M536
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AA Sequence
QGKEVVLLDFAAMKGELGWLTHPYGKGWDLMQNIMNDMPIYMYSVCNVVSGDQDNWLRTNWVYREEAERIFIELKFTVRDCNSFPGGASSCKETFNLYYAESDVDYGTNFQKRQFTKIDTIAPDEITVSSDFEARNVKLNVEERMVGPLTRKGFYLAFQDIGACVALLSVRVYYKKCPEMLQSLARFPETIAVAVSDAQPLATVAGTCVDHAVVPYGGEGPLMHCTVDGEWLVPIGQCLCQEGYEKVEDACQACSPGFFKSEASESPCLQCPEHTLPSTEGATSCQCEEGYFRAPEDPLSMPCTRPPSAPHYLTAIGMGAKVELRWTAPQDTGGRKDIVYSVTCEQCWPESGECGSCEASVQYSEPPQALTRTSVTVSDLEPHMNYTFTVEARNGVSDLVNSRSFRTASVSINQTEPPKVRLEDRSTTSLSVAWSIPVPQQSRVWKYEVTYRKKGDANSYNVHRTDGFSVTLDGLAPGTTYLVQVQALTQEGQGAGSKVHEFQTLSTEGSATM
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Protein Length
Partial
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Molecular Weight
60-67 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
EphA2 is a receptor tyrosine kinase that plays a crucial role in various biological processes, including cell adhesion, migration, and differentiation. It is predominantly expressed in epithelial cells and has been implicated in several pathological conditions, particularly in cancer progression and metastasis. Abnormal EphA2 expression has been linked to tumor development and poor prognosis in various cancers, making it a potential therapeutic target. The study of EphA2 recombinant proteins is vital for understanding its functional roles and interactions at the molecular level. Researchers aim to develop EphA2-based biomarkers and therapeutic strategies by employing recombinant protein technology, which allows for the production of large quantities of purified protein for functional assays, crystallography, and structural biology studies. Investigating the structure and function of EphA2 can reveal insights into its signaling pathways and may lead to the identification of innovative treatments that inhibit its pro-tumorigenic effects. Additionally, recombinant EphA2 proteins can serve as valuable tools in the development of targeted therapies, including monoclonal antibodies and small molecule inhibitors, further advancing cancer treatment modalities. Thus, research into EphA2 recombinant proteins is critical for both basic and applied sciences, aimed at translating these findings into clinical benefits for patients with EphA2-related diseases.
