Analytical Data
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Gene name
CRADD
- Application
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Alternative Names
CRADD；RAIDD;Death domain-containing Protein CRADD
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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
P78560
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Expression Region
1-199aa
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AA Sequence
MEARDKQVLRSLRLELGAEVLVEGLVLQYLYQEGILTENHIQEINAQTTGLRKTMLLLDILPSRGPKAFDTFLDSLQEFPWVREKLKKAREEAMTDLPAGDRLTGIPSHILNSSPSDRQINQLAQRLGPEWEPMVLSLGLSQTDIYRCKANHPHNVQSQVVEAFIRWRQRFGKQATFQSLHNGLRAVEVDPSLLLHMLE
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Molecular Weight
38.7kDa
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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
CRADD, or Caspase Recruitment Domain-containing protein, plays a crucial role in the regulation of apoptosis and cellular stress responses. As a vital adaptor protein, CRADD facilitates the recruitment and activation of caspases, the executioners of programmed cell death. Studies have shown that dysregulation of CRADD can contribute to various pathologies, including cancer and neurodegenerative diseases, by either promoting excessive cell death or enabling survival in the presence of stressors. Given its pivotal role in these processes, researchers have focused on understanding the structural and functional properties of CRADD, aiming to uncover its mechanisms of action. Recent advances in recombinant protein technologies have enabled the production of CRADD in vitro, allowing for detailed biochemical and biophysical analyses. This includes investigating its interactions with other proteins and signaling pathways, which are crucial for elucidating its functions in cellular homeostasis. Furthermore, the study of CRADD recombinant protein has potential therapeutic implications, as targeting its interactions could provide new strategies for modulating apoptosis in various diseases. By exploring CRADD's role as a signaling hub in cell death pathways, researchers hope to develop innovative treatments that can either inhibit excessive apoptosis or promote cell survival in contexts where it is beneficial. Overall, the ongoing research on CRADD not only enhances our understanding of fundamental biological processes but also opens avenues for novel therapeutic approaches in disease management.
