Analytical Data
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Gene name
DDIT4
- Application
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Alternative Names
DDIT4；REDD1；RTP801;DNA damage-inducible transcript 4 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
Q9NX09
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Expression Region
1-232aa
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AA Sequence
MPSLWDRFSS SSTSSSPSSL PRTPTPDRPP RSAWGSATRE EGFDRSTSLE SSDCESLDSS NSGFGPEEDT AYLDGVSLPD FELLSDPEDE HLCANLMQLL QESLAQARLG SRRPARLLMP SQLVSQVGKE LLRLAYSEPC GLRGALLDVC VEQGKSCHSV GQLALDPSLV PTFQLTLVLR LDSRLWPKIQ GLFSSANSPF LPGFSQSLTL STGFRVIKKK LYSSEQLLIE EC
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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
DDIT4 (DNA Damage Inducible Transcript 4), also known as REDD1 (Regulated in Development and DNA Damage Responses 1), plays a crucial role in cellular responses to stress and is implicated in various physiological processes, including metabolism, cell growth, and apoptosis. Its expression is regulated in response to hypoxia, nutrient deprivation, and DNA damage, positioning it as a significant player in the cellular adaptation mechanisms. Research into DDIT4 is particularly relevant in the context of cancer, as its aberrant regulation has been linked to tumor progression and resistance to therapy. Additionally, DDIT4 modulates the mTOR (mechanistic target of rapamycin) signaling pathway, which is essential for cellular growth and proliferation, making it a potential target for therapeutic intervention. Recent studies have focused on elucidating the molecular mechanisms underpinning DDIT4 function and its interactions with other pathways. The recombinant protein form of DDIT4 is of great interest because it allows for detailed structural and functional analyses. Understanding the biophysical properties and biological activities of recombinant DDIT4 can facilitate insights into its role in disease states, paving the way for novel therapeutic approaches. Overall, the study of recombinant DDIT4 protein represents a promising avenue for advancing our understanding of cellular stress responses and their implications in cancer and other pathologies.
