Analytical Data
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Gene name
Fcgr3
- Application
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Alternative Names
Fcgr3；CD16B；FCG3；FCGR3；Low affinity immunoglobulin gamma Fc region receptor III-B
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Species
Mouse
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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
P08508
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Expression Region
31-215aa
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AA Sequence
ALPKAVVKLDPPWIQVLKEDMVTLMCEGTHNPGNSSTQWFHNGRSIRSQVQASYTFKATVNDSGEYRCQMEQTRLSDPVDLGVISDWLLLQTPQRVFLEGETITLRCHSWRNKLLNRISFFHNEKSVRYHHYKSNFSIPKANHSHSGDYYCKGSLGSTQHQSKPVTITVQDPATTSSISLVWYHT
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Molecular Weight
37.2 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
FcγRIII, also known as CD16, is a low-affinity receptor for the Fc region of immunoglobulin G (IgG) antibodies and plays a crucial role in the immune response by mediating antibody-dependent cellular cytotoxicity (ADCC). This receptor is primarily expressed on natural killer (NK) cells, macrophages, and some types of dendritic cells, making it essential for targeting and eliminating pathogens and tumor cells. The study of recombinant FcγRIII proteins has gained significant attention due to their potential therapeutic applications, particularly in antibody-based therapies for cancer and infectious diseases. By producing and characterizing recombinant FcγRIII, researchers aim to explore its binding affinity, specificity for different IgG subclasses, and role in immune signaling pathways. Additionally, engineered variants of FcγRIII can be utilized to enhance the efficacy of therapeutic antibodies by improving their ability to engage immune effector cells. Understanding the structural and functional properties of FcγRIII can thus inform the design of more effective immunotherapies, paving the way for novel treatments that harness the immune system's power against malignancies and infections. The advances in recombinant technology and biochemical analysis facilitate a deeper comprehension of FcγRIII, providing insights into its mechanisms and guiding the development of next-generation therapeutic strategies.
