Analytical Data
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Gene name
GITR
- Application
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Alternative Names
TNFRSF18; AITR; Tumor Necrosis Factor Receptor Superfamily 18; Glucocorticoid-induced TNFR-related protein; Activation-inducible TNFR family receptor
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Species
Human
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Source
HEK293
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Tag
C- hFc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y5U5
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Expression Region
26-162aa
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Molecular Weight
40.8
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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
GITR (Glucocorticoid-Induced Tumor Necrosis Factor Receptor-related protein) is a costimulatory molecule predominantly expressed on T cells and other immune cells. It plays a critical role in modulating immune responses, particularly in enhancing T cell activation and proliferation, which makes it a valuable target for cancer immunotherapy. Research has shown that GITR signaling can promote antitumor immunity while also regulating peripheral tolerance, thereby preventing autoimmune responses. The development of GITR agonists has gained traction in recent years, aiming to harness this pathway to improve the efficacy of existing cancer treatments and develop novel therapeutic strategies. Recombinant GITR proteins are being investigated for their potential to enhance immune responses against tumors and to serve as biomarkers for patient stratification in immunotherapy. Understanding the structural and functional aspects of GITR is essential for the design of effective GITR-targeted therapies. Studies involving the recombinant expression and characterization of GITR proteins can provide insights into their immunological functions and pave the way for new clinical applications in oncology. Overall, GITR research holds promise for advancing our understanding of immune modulation and improving cancer treatment outcomes.
