Analytical Data
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Gene name
JAM-B/CD322
- Application
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Alternative Names
CD322; JAM-B; JAMB; VE-JAM; VEJAM; Junctional adhesion molecule B; Vascular endothelial junction-associated molecule
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q3MHC0
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Expression Region
Thr57~Asp233
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Molecular Weight
31kDa
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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
JAM-B (Junctional Adhesion Molecule B) is a member of the JAM family of immunoglobulin-like proteins, primarily expressed in endothelial cells and various immune cells. It plays a crucial role in mediating cell adhesion, facilitating leukocyte transmigration, and maintaining the integrity of blood-brain and blood-tissue barriers. The interaction of JAM-B with CD322, its receptor, is significant in the context of immune response and vascular biology. Research into JAM-B/CD322 recombinant proteins has gained momentum due to their potential implications in inflammatory diseases, cancer metastasis, and tissue repair processes. Understanding the structural and functional properties of these proteins could provide insights into their role in health and disease. Studies have shown that manipulating the JAM-B/CD322 interactions may help modulate immune responses and improve therapeutic strategies for conditions such as autoimmune disorders or tumor progression. The exploration of JAM-B/CD322 recombinant proteins not only aids in elucidating their biological functions but also holds promise for the development of novel biomolecules with therapeutic applications, thus making it a significant focus in molecular biology and translational research.
