Analytical Data
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Gene name
NHLRC4
- Application
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Alternative Names
NHLRC4; NHL-repeat-containing protein 4
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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
P0CG21
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Expression Region
1-123 aa
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AA Sequence
MLGLEGPCWV GPGPDGGLAV SEEFGDVRLF GSARQPLGSL GGWTGHTFGC PAGICSNSEG NVIVADEQRR QVTLFPRAGP PICLVSEGLG QPLGVACAPQ GQLLVADAKD NSIKVYQGLK ELA
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Molecular Weight
12.6 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
NHLRC4 is a member of the NHL repeat-containing protein family and has garnered significant attention due to its involvement in various biological processes, particularly in the context of immune response and inflammation. Research has indicated that NHLRC4 plays a crucial role in the regulation of innate immunity, particularly in the activation of the NLRP3 inflammasome, which is vital for the host defense mechanism against pathogens. Mutations or dysregulation of NHLRC4 have been associated with certain autoimmune diseases, highlighting its potential as a therapeutic target. The recombinant form of NHLRC4 is being studied to elucidate its functional properties, interactions with other proteins, and its role in signaling pathways. Understanding the structural and biochemical characteristics of NHLRC4 could provide insights into its mechanism of action, opening avenues for the development of novel therapeutic strategies for inflammatory diseases and conditions associated with immune dysfunction. As such, the investigation of NHLRC4 recombinant protein is not only pivotal for basic research but also holds promise for clinical applications in the field of immunology and therapeutic interventions.
