Analytical Data
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Gene name
TNFRSF18
- Application
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Alternative Names
TNFRSF18；AITR；Tumor necrosis factor receptor superfamily member 18
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
QRPTGGPGCGPGRLLLGTGTDARCCRVHTTRCCRDYPGEECCSEWDCMCVQPEFHCGDPCCTTCRHHPCPPGQGVQSQGKFSFGFQCIDCASGTFSGGHEGHCKPWTDCTQFGFLTVFPGNKTHNAVCVPGSPPAEP
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Molecular Weight
40.8 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
TNFRSF18, also known as GITR (glucocorticoid-induced TNFR-related protein), is a member of the tumor necrosis factor receptor superfamily and plays a crucial role in immune regulation. It is primarily involved in the activation and survival of T cells, making it an attractive target for cancer immunotherapy. Research has shown that GITR can enhance the anti-tumor immune response by stimulating effector T cells and inhibiting regulatory T cells, which are often responsible for suppressing immune responses against tumors. Furthermore, soluble forms of TNFRSF18 have been explored for their potential therapeutic applications in modulating immune responses, particularly in autoimmune diseases and enhancing vaccine efficacy. The development of recombinant TNFRSF18 protein allows for detailed studies of its biological functions and therapeutic potential, paving the way for novel approaches in cancer treatment and immune modulation. Understanding the molecular mechanisms by which TNFRSF18 operates can significantly contribute to the development of targeted therapies that harness the immune system's power to fight cancer and other diseases. This ongoing research not only aims to elucidate the fundamental biology of GITR but also seeks to enhance its clinical applicability, offering hope for improved outcomes in patients with malignancies and immune-related disorders.
