Analytical Data
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Gene name
DDIT3
- Application
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Alternative Names
DDIT3；CHOP；CHOP10；GADD153；DNA damage-inducible transcript 3 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
P35638
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Expression Region
1-169aa
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AA Sequence
MAAESLPFSF GTLSSWELEA WYEDLQEVLS SDENGGTYVS PPGNEEEESK IFTTLDPASL AWLTEEEPEP AEVTSTSQSP HSPDSSQSSL AQEEEEEDQG RTRKRKQSGH SPARAGKQRM KEKEQENERK VAQLAEENER LKQEIERLTR EVEATRRALI DRMVNLHQA
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Molecular Weight
19.1 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
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Protein Description
DDIT3, also known as C/EBP homologous protein (CHOP), is a transcription factor that plays a crucial role in cellular stress responses, particularly in the context of endoplasmic reticulum (ER) stress and apoptosis. Its expression is upregulated during conditions that provoke unfolded protein response (UPR), highlighting its involvement in maintaining cellular homeostasis. The significance of DDIT3 in various pathophysiological conditions, including cancer, metabolic disorders, and neurodegenerative diseases, has garnered substantial interest in the research community. Understanding the molecular mechanisms by which DDIT3 contributes to cell survival or death in response to stress is imperative for developing potential therapeutic strategies. Recent studies have focused on the functional characterization of DDIT3 in various biological contexts, exploring its role as a mediator of cell fate decisions and its interactions with different signaling pathways. Furthermore, the generation of recombinant DDIT3 proteins has facilitated in vitro studies, enabling researchers to dissect its functional domains and post-translational modifications. This line of research holds promise for identifying novel targets in disease states linked to DDIT3 dysregulation and may pave the way for innovative approaches in therapeutic interventions aimed at modulating its activity in diverse clinical settings.
