Analytical Data
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Gene name
HLA-A
- Application
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Alternative Names
/
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Species
Human
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Source
E. coli
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Tag
N- His-B2M
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A0A140T913
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Expression Region
25-299aa
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Molecular Weight
48.8 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
Related Products
Protein Description
The study of HLA-A recombinant proteins is rooted in the pivotal role that Human Leukocyte Antigen (HLA) molecules play in the immune response and organ transplantation. HLA-A is a critical class I molecule, responsible for presenting endogenous peptides to CD8+ T cells, thus facilitating the detection of infected or malignant cells by the immune system. Understanding the structural and functional characteristics of HLA-A is essential for improving transplant compatibility and developing effective immunotherapies. Researchers have focused on producing recombinant HLA-A proteins to study their antigen-binding properties, interactions with T cell receptors, and implications in autoimmune diseases and cancer. These recombinant proteins serve as valuable tools for vaccine development, as they can help identify epitopes that elicit robust immune responses. Additionally, the exploration of HLA-A variants can provide insights into population genetics and disease susceptibility, ultimately aiding in personalized medicine approaches. Advances in protein engineering and expression systems have enabled the production of high-purity HLA-A recombinant proteins, making them readily accessible for various biomedical applications. Thus, the research on HLA-A recombinant proteins is vital for enhancing our understanding of immune mechanisms and improving therapeutic strategies in transplantation and cancer immunotherapy.
