Analytical Data
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Gene name
Caspase-8/CASP8 subunit p18
- Application
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Alternative Names
CAP4; FLICE; MACH; MCH5; Cysteinyl Aspartate Specific Proteinases 8; Apoptotic cysteine protease; FADD-homologous ICE/ced-3-like protease; MORT1-associated ced-3 homolog
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q9JHX4
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Expression Region
Tyr8~Val197
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Molecular Weight
27kDa
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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
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Protein Description
Caspase-8 (CASP8) is a pivotal cysteine protease that plays a crucial role in apoptosis, inflammation, and immune response. It is a key initiator caspase, primarily involved in the extrinsic apoptotic signaling pathway triggered by death receptors. The active form of Caspase-8 exists as a heterotetramer composed of two large subunits (p18) and two small subunits (p10). Research focusing on the recombinant p18 subunit of Caspase-8 is essential for understanding its structure-function relationship, regulatory mechanisms, and potential therapeutic applications. The recombinant p18 protein can be utilized to elucidate its role in apoptotic pathways and to investigate how mutations or dysregulation in its expression contribute to various diseases, including cancer and autoimmune disorders. Moreover, studying the p18 subunit offers insights into the design of specific inhibitors that could modulate its activity for therapeutic purposes. Given the importance of Caspase-8 in both cell death and survival pathways, advancements in recombinant protein technologies provide a valuable platform for drug discovery and the development of novel treatment strategies targeting apoptotic dysregulation.
