Analytical Data
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Gene name
APOD
- Application
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Alternative Names
Apo-D
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P05090
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Expression Region
Gln21~Ser189
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Molecular Weight
23kDa
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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
APOD, or Apolipoprotein D, is a member of the apolipoprotein family, primarily known for its role in lipid metabolism and transport. It has gained significant attention in recent years due to its implications in various physiological and pathological processes, including neurodegenerative diseases, cancer, and metabolic disorders. APOD's ability to bind and transport lipids suggests it may play a crucial role in maintaining cellular homeostasis and influencing signaling pathways. Research into the structural and functional aspects of recombinant APOD protein has been crucial in uncovering its mechanisms of action and potential therapeutic applications. By employing techniques such as X-ray crystallography and nuclear magnetic resonance, scientists aim to elucidate the protein's three-dimensional structure, which is vital for understanding its function at the molecular level. Moreover, the development of recombinant APOD allows for the study of its interactions with other biomolecules, advancing our knowledge of its role in health and disease. These studies not only provide insight into APOD's biological functions but also open avenues for its potential use as a biomarker or therapeutic target in conditions where its expression is altered. Understanding APOD's role could lead to innovative strategies in treating diseases linked with lipid dysregulation and neuroinflammation, thereby highlighting the importance of this protein in biomedical research.
