Analytical Data
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Gene name
LRRC32
- Application
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Alternative Names
GARP; Glycoprotein A Repetitions Predominant; Garpin
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
G3XA59
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Expression Region
Gln400~Leu643
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Molecular Weight
30kDa
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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
LRRC32, also known as GARP (glycoprotein A repetitions predominant), is a membrane protein primarily expressed on regulatory T cells (Tregs) and has garnered significant attention in immunology research. This protein plays a crucial role in the immune system by regulating Treg function and stability, thereby modulating immune responses and maintaining self-tolerance. Its involvement in promoting the expression of latent TGF-β (transforming growth factor-beta) has implications for various pathological conditions, including autoimmunity, cancer, and transplant tolerance. The generation of recombinant LRRC32 protein has facilitated the study of its structural and functional properties, providing insights into its mechanism of action and potential therapeutic applications. Recent advancements in recombinant DNA technology have enabled the production of high-purity, biologically active LRRC32, which is essential for in vitro studies and clinical applications. Investigating LRRC32's interactions with TGF-β and other cellular components is crucial for understanding its role in Treg biology and its potential as a target for immunotherapy. Overall, the study of LRRC32 recombinant protein is paving the way for novel strategies in managing immune-related diseases through targeted therapies that modulate Treg activity.
