Analytical Data
-
Gene name
PVRIG
- Application
-
Alternative Names
CD112 receptor Short name: CD112R Poliovirus receptor-related immunoglobulin domain-containing protein C7orf15
-
Species
Human
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q6DKI7
-
Expression Region
1-326aa
-
Molecular Weight
50.3 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
PVRIG (programmed death receptor 1 ligand) is recognized as an important immunomodulatory protein that plays a critical role in regulating immune responses, particularly in the context of cancer and chronic infections. As a member of the B7 family of proteins, PVRIG interacts with its receptor, promoting inhibitory signals that can dampen T-cell activation and proliferation. This mechanism of action is particularly significant as it presents a novel target for cancer immunotherapy, where enhancing T-cell responses is crucial for effective tumor rejection. Recent studies have indicated that PVRIG expression is upregulated in various tumors, suggesting its potential role in immune evasion by cancer cells. Consequently, the research surrounding PVRIG has garnered attention for its implications in developing therapeutic strategies aimed at blocking its inhibitory signaling pathways, thereby reinvigorating T-cell function in the tumor microenvironment. Furthermore, understanding the structural characteristics and functional dynamics of PVRIG through recombinant protein studies could pave the way for the design of innovative drugs and combination therapies that enhance immune responses against cancer, making PVRIG an appealing target for future research and clinical applications.
