Analytical Data
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Gene name
KLRG1
- Application
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Alternative Names
Killer cell lectin like receptor G1; KLRG1
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Species
Cynomolgus
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Source
HEK293
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Tag
N-Avi;N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A0A2K5WAP9
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Expression Region
L60-P189
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Molecular Weight
22-25 kDa and 26-31 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
KLRG1, or Killer Cell Lectin-like Receptor G1, is an immunoreceptor predominantly expressed on the surface of various immune cells, including natural killer (NK) cells and T cells. Its role as an inhibitory receptor has drawn considerable interest in immunology, particularly regarding its involvement in the regulation of immune responses and potential implications in cancer immunotherapy. Research has indicated that KLRG1 can modulate the function and lifespan of effector T cells, influencing their ability to persist in the tumor microenvironment and respond to cancer cells. Additionally, KLRG1 expression has been associated with the exhaustion of T cells, a state that diminishes their effectiveness in fighting tumors. Understanding KLRG1's structure and function is crucial for developing innovative therapies that can enhance immune responses against malignancies. Researchers have been focused on producing recombinant KLRG1 proteins for detailed studies on its ligand interactions and signaling pathways, which could unveil new therapeutic targets. The characterization of KLRG1 through recombinant protein technology offers insights into its functional role in immune modulation, paving the way for novel strategies in cancer treatment by either blocking its inhibitory signals or utilizing it to improve the efficacy of existing therapies.
