Analytical Data
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Gene name
PTPRC/CD45RA
- Application
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Alternative Names
rHuReceptor-type tyrosine-protein phosphatase C/ CD45R0, His; B220; CD45 antigen; CD45; CD45R; LCA; L-CA; LY5; protein tyrosine phosphatase, receptor type, C; PTPRC; receptor-type tyrosine-protein phosphatase C; CD45R0
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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
P08575-8
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Expression Region
Q26-K482
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Molecular Weight
120-150 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
The CD8A-CD8B heterodimer is a crucial component in the immune system, primarily found on the surface of cytotoxic T lymphocytes (CTLs). This heterodimer consists of two distinct chains: CD8A and CD8B, both of which contribute to the recognition of major histocompatibility complex (MHC) class I molecules, facilitating the activation of CTLs against infected or malignant cells. Given its pivotal role in T cell-mediated immunity, the CD8A-CD8B heterodimer has garnered attention for its potential as a target in immunotherapy, particularly in cancer treatment. Research into the structure and function of this heterodimer has revealed insights into T cell development, activation, and differentiation. Advanced techniques, such as recombinant protein expression and purification, have enabled the production of soluble CD8A-CD8B heterodimers, allowing for detailed biochemical and biophysical characterization. Furthermore, studies have explored how variations in the expression levels of these proteins can influence immune responses, highlighting their importance in recognizing and eliminating tumor cells. Given that therapeutic strategies targeting the CD8A-CD8B heterodimer could enhance antitumor immunity, ongoing research aims to develop novel immunotherapeutics that harness this pathway to improve patient outcomes in various malignancies. The comprehensive understanding of CD8A-CD8B heterodimer functions and interactions will be instrumental in designing targeted therapies that may lead to more effective immune responses against cancer and other diseases.
