Analytical Data
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Gene name
Ephrin-B2/EFNB2
- Application
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Alternative Names
EPLG5; HTKL; Htk-L; LERK5; HTK Ligand; Ligand Of Eph-Related Kinase 5; Eph-Related Receptor Tyrosine Kinase Ligand 5
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 97% as determined by SDS-PAGE.
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Uniprot
P52799
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Expression Region
Phe42~Val333
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Protein Length
Partial
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Molecular Weight
38kDa
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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.
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Protein Description
Ephrin-B2 (EFNB2) is a member of the ephrin family, which plays crucial roles in cell-cell communication and signaling during embryonic development and in the nervous system. EFNB2 is particularly significant for its involvement in angiogenesis, neuronal guidance, and immune responses. It interacts with Eph receptors, triggering bidirectional signaling pathways that influence cell migration, adhesion, and tissue organization. Research has shown that alterations in EFNB2 expression can contribute to various pathological conditions, including cancer, where its role in tumor progression and metastasis has garnered interest. The recombinant production of Ephrin-B2 protein facilitates detailed studies on its structure-function relationships and provides a valuable tool for investigating its biological activities. By expressing EFNB2 in various cellular contexts, scientists aim to elucidate its mechanisms of action and its potential as a therapeutic target. Understanding Ephrin-B2's involvement in disease processes could open avenues for the development of novel therapies that modulate its activity, thus providing new strategies for treatment in conditions such as cancer and neurodegenerative diseases. Overall, the research on EFNB2 recombinant proteins not only enhances our comprehension of fundamental biological processes but also paves the way for innovative therapeutic approaches.
