Analytical Data
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Gene name
APOD
- Application
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Alternative Names
Apolipoprotein D(Apo-D)(ApoD)
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Species
Mouse
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P51910
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Expression Region
21-189aa
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Molecular Weight
26.9 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
CUTC (C-terminal Ubiquitin-like domain-containing protein) is a protein that has garnered attention in the field of molecular biology due to its potential role in cellular processes and disease mechanisms. Emerging research suggests that CUTC may participate in protein degradation pathways, potentially influencing the regulation of various cellular functions. The protein's unique structural features, including its ubiquitin-like domain, imply a possible involvement in protein-protein interactions and signaling pathways, making it a candidate for studies on cancer and neurodegenerative diseases. The understanding of CUTC's structure and function is critical for elucidating its biological role and therapeutic potential. Recent advances in recombinant protein technology have enabled the production of CUTC in sufficient quantities for functional studies, paving the way for in-depth investigations into its mechanisms of action. These studies may not only contribute to our understanding of fundamental biological processes but also provide insights into its potential as a biomarker or therapeutic target in various diseases. As researchers continue to uncover the complexities surrounding CUTC, the protein's significance in health and disease remains a promising area for exploration.
