Analytical Data
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Gene name
FcgBP
- Application
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Alternative Names
FcgBP；IgGFc-binding Protein
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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
Q9Y6R7
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Expression Region
471-690aa
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AA Sequence
VCRAQGDPHYTTFDGRRYDMMGTCSYTMVELCSEDDTLPAFSVEAKNEHRGSRRVSYVGLVTVRAYSHSVSLTRGEVGFVLVDNQRSRLPVSLSEGRLRVYQSGPRAVVELVFGLVVTYDWDCQLALSLPARFQDQVCGLCGNYNGDPADDFLTPDGALAPDAVEFASSWKLDDGDYLCEDGCQNNCPACTPGQAQHYEGDRLCGMLTKLDGPFAVCHDT
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Molecular Weight
31.1 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
FcgBP, or Fc gamma binding protein, is a crucial component in the immune response, primarily involved in the regulation of antibody-mediated functions. It binds to the Fc region of IgG antibodies, playing a significant role in modulating immune cell activities, including phagocytosis, antibody-dependent cellular cytotoxicity, and immune complex clearance. Over the years, research has expanded our understanding of FcgBP's structural characteristics, binding affinities, and functional implications in both health and disease. The recombinant expression of FcgBP allows for in-depth studies, aiding in the elucidation of its mechanisms of action. These studies are particularly relevant in the context of autoimmune diseases, infections, and therapeutic antibody development, as targeting FcgBP can potentially improve treatment outcomes by enhancing the efficacy of therapeutic antibodies or by regulating unwanted immune responses. Furthermore, recombinant FcgBP can serve as a valuable tool in drug delivery systems and vaccine development, facilitating targeted therapy strategies. Overall, the exploration and manipulation of FcgBP hold great promise for advancing immunotherapeutic approaches and improving our understanding of immune regulation.
