Analytical Data
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Gene name
VSIG4
- Application
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Alternative Names
V-set and immunoglobulin domain-containing protein 4; VSIG4; Protein Z39Ig; Z39IG; CRIg
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Species
Human
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Source
HEK293
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Tag
C-Avi;C-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y279-1
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Expression Region
R20-P283
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Molecular Weight
43-50 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
H-2Db and β2-microglobulin (β2M) are critical components of the major histocompatibility complex (MHC) class I molecules in mice, playing essential roles in the immune response by presenting peptide antigens to CD8+ T cells. The reconstitution of H-2Db with β2M in recombinant protein studies is crucial for understanding various aspects of immune system functioning, including T cell activation, antigen recognition, and the overall dynamics of adaptive immunity. The incorporation of β2M is necessary for the proper folding, stability, and expression of the H-2Db alpha chain, which is pivotal for functional MHC class I molecules. Research involving the recombinant expression of H-2Db and β2M facilitates detailed analyses of their interactions, the mechanisms of antigen presentation, and the implications for diseases, such as viral infections and cancer, where MHC class I molecules play a significant role. Moreover, recombinant proteins can be valuable tools for developing vaccines, studying T cell receptor binding, and designing immunotherapies. Understanding the structural and functional properties of the H-2Db/β2M complex allows researchers to explore novel therapeutic strategies to modulate immune responses. Through the investigation of these proteins, scientists can gain insights into the fundamental mechanisms of immune recognition and tolerance, contributing to advancements in immunology and biotechnology.
