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
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 85% as determined by SDS-PAGE.
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Uniprot
P57087
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Expression Region
Glu74~Ser250
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Molecular Weight
28kDa
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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 immunoglobulin superfamily and plays a critical role in cell adhesion and tight junction formation, particularly in endothelial and epithelial cells. Research has increasingly focused on JAM-B due to its involvement in various physiological and pathological processes, including inflammation, immune responses, and tumor metastasis. Another critical protein, CD322, is often identified as a receptor for JAM-B, facilitating intercellular communication and influencing leukocyte migration. The reconstitution of JAM-B/CD322 recombinant proteins aims to elucidate their structure-function relationships and understand their roles in cellular interactions and signaling pathways. This research holds potential implications for therapeutic strategies targeting inflammatory diseases and cancer, as modulation of JAM-B/CD322 interactions may alter disease progression or enhance tissue repair mechanisms. Overall, the study of JAM-B/CD322 recombinant proteins contributes to a greater understanding of cell adhesion mechanisms in health and disease, paving the way for novel biomedical applications.
