Analytical Data
-
Gene name
FcgR4/CD16-2
-
简介
The FcγR4/CD16-2 protein is an IgG receptor with moderate affinity for IgG2a and IgG2b. It recognizes virus-specific IgG, triggers antibody-dependent cellular cytotoxicity, and provides protection against fatal influenza infection. FcgR4/CD16-2 Protein, Mouse (HEK293, His-Avi) is the recombinant mouse-derived FcgR4/CD16-2 protein, expressed by HEK293 , with C-Avi, C-His labeled tag.
- Application
-
Alternative Names
Low affinity immunoglobulin gamma Fc region receptor IV; CD16-2; FcgammaRIV; Fcrl3
-
Species
Mouse
-
Source
HEK293
-
Tag
C-Avi;C-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
A0A0B4J1G0
-
Expression Region
Q19-Q203
-
Protein Length
Partial
-
Molecular Weight
25-35 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
FcgR4, also known as CD16-2, is a critical receptor involved in the immune response, particularly in the recognition and elimination of pathogens by immune cells. It is predominantly expressed on natural killer (NK) cells, macrophages, and certain subsets of T cells, facilitating antibody-dependent cellular cytotoxicity (ADCC) and phagocytosis. The study of FcgR4/CD16-2 has gained attention due to its potential implications in various therapeutic areas, including cancer immunotherapy, autoimmune diseases, and infectious diseases. The receptor's ability to bind to the Fc portion of immunoglobulins enables the modulation of immune responses, making it an attractive target for designing monoclonal antibodies and enhancing their efficacy. Recent research has focused on the structural and functional characterization of recombinant FcgR4 proteins to understand their binding affinities and signaling pathways. This knowledge is crucial for developing strategies to improve antibody-mediated effector functions and to explore the therapeutic potential of engineered FcgR4/CD16-2 variants. The generation of FcgR4/CD16-2 recombinant proteins also allows for the exploration of their interactions with different classes of antibodies and other immune regulators, providing insights into the complexities of the immune system and the development of novel immunotherapies.
