Analytical Data
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Gene name
CD320
- Application
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Alternative Names
8D6; 8D6A; CD320 Antigen; TCblR; FDC-signaling molecule 8D6; Transcobalamin receptor
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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
Q9NPF0
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Expression Region
Ser36~Tyr229
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Molecular Weight
30kDa
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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
CD320 is a receptor protein primarily known for its role in the metabolism of vitamin B12, playing a crucial part in cellular uptake and utilization of this essential vitamin. Research indicates that CD320 facilitates the transport of vitamin B12 across the cell membrane, thereby influencing various physiological functions, including DNA synthesis and the maintenance of neurological health. The exploration of CD320 and its recombinant protein form has gained increasing attention due to its potential implications in clinical nutrition, particularly in conditions characterized by vitamin B12 deficiency. Furthermore, understanding the structural and functional characteristics of CD320 can provide insights into its regulatory mechanisms in cellular processes. Studies have also highlighted the receptor's involvement in immune responses and inflammation, indicating that recombinant CD320 could have therapeutic applications in various diseases. The recombinant form of CD320 can be utilized in research settings to investigate its binding affinity to different forms of vitamin B12 and other ligands, aiding in the development of targeted interventions for metabolic disorders. Therefore, ongoing research into CD320's structure and functions not only enhances our understanding of vitamin B12 metabolism but also holds promise for novel therapeutic strategies to combat related health issues.
