Analytical Data
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Gene name
Ephrin-A4/EFNA4
- Application
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Alternative Names
Ephrin-A4; EPH-Related Receptor Tyrosine Kinase Ligand 4; LERK-4; EFNA4; EPLG4; LERK4
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Species
Human
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Source
HEK293
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Tag
C- His-Fc
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P52798
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Expression Region
26-171aa
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Protein Length
Partial
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Molecular Weight
44.3 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
Ephrin-A4 (EFNA4) is a member of the ephrin family, which plays a crucial role in cell communication, particularly in the development of the nervous system and cardiovascular structures. As a ligand for Eph receptors, Ephrin-A4 is involved in bidirectional signaling that regulates various biological processes, including cell migration, adhesion, and shape changes. Research has highlighted the importance of Ephrin-A4 in neurogenesis, where it influences axon guidance and neuronal positioning. Additionally, aberrations in Ephrin signaling have been linked to various pathological conditions, including cancer, where altered expression may affect tumor growth and metastasis. The recombinant protein form of Ephrin-A4 is critical for experimental studies, enabling researchers to investigate its interactions with Eph receptors and other cellular partners in vitro and in vivo. Such studies can elucidate its role in physiological and pathological processes and may offer insights into therapeutic targets for diseases associated with dysfunctional Eph-ephrin signaling. Understanding the functional dynamics of Ephrin-A4 through recombinant technology will advance our knowledge of its contributions to cellular behavior and provide a framework for exploring potential clinical applications.
