Analytical Data
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Gene name
Ephrin-A5/EFNA5
- Application
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Alternative Names
AL-1 (EPH-related receptor tyrosine kinase ligand 7) (LERK-7)
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Species
Human
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Source
HEK293
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Tag
C- hFc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P52803
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Expression Region
21-203aa
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Molecular Weight
50.1 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
Related Products
Protein Description
Ephrin-A5, also known as EFNA5, is a member of the ephrin family, which plays a crucial role in cellular communication, particularly in the nervous system and during embryonic development. It serves as a ligand for Eph receptors, a subclass of receptor tyrosine kinases, and is involved in various biological processes, including neuronal guidance, cell migration, and tissue boundary formation. The interaction between Ephrin-A5 and its receptors mediates bidirectional signaling, influencing both the pre- and post-synaptic cells. Research has shown that Ephrin-A5 is critical for brain development and function, with implications in neuroplasticity and synaptic formation. Additionally, aberrations in Ephrin-A5 signaling have been linked to several neurological disorders and cancers, making it a potential therapeutic target. The recombinant protein version of Ephrin-A5 is often produced for experimental purposes, allowing researchers to study its interactions with Eph receptors and to explore its role in modulating cellular behaviors. Understanding the molecular mechanisms underpinning Ephrin-A5 function could provide insights into targeted therapies for diseases related to its dysregulation. Through the study of EFNA5 recombinant proteins, researchers aim to elucidate its precise roles in cellular interactions, signaling pathways, and physiological processes, ultimately fostering advancements in neuroscience and oncology.
