Analytical Data
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Gene name
HLA-DMB
- Application
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Alternative Names
MHC class II antigen DMB Really interesting new gene 7 protein DMB, RING7
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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 90% as determined by SDS-PAGE.
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Uniprot
P28068
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Expression Region
19-218aa
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Molecular Weight
26.4 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
HLA-DMB is a crucial component of the major histocompatibility complex (MHC) class II molecules, playing a significant role in the immune response by facilitating the loading of peptide antigens onto MHC class II dimers for presentation to CD4+ T cells. The proper functioning and stability of MHC class II molecules rely heavily on HLA-DMB's interaction with HLA-DP, HLA-DQ, and HLA-DR molecules. Research on HLA-DMB recombinant proteins has gained momentum due to its implications in various immune-related disorders, including autoimmune diseases, infectious diseases, and cancer. Investigations into HLA-DMB's structure, dynamics, and stability can lead to a better understanding of its role in antigen presentation and its potential impact on T cell activation. Additionally, HLA-DMB's polymorphisms and their influence on immune responses are of great interest, particularly in personalized medicine, where tailoring immunotherapies based on individual genetic backgrounds could enhance treatment efficacy. The production of recombinant HLA-DMB proteins enables detailed biochemical and biophysical studies, providing insights into its mechanism of action and interactions with other molecular partners in the immune system. Consequently, understanding HLA-DMB at a molecular level could pave the way for novel therapeutic strategies to modulate immune responses in various clinical contexts.











