Analytical Data
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Gene name
TCblR/CD320
- Application
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Alternative Names
8D6 antigenFDC-signaling molecule 8D6 ;FDC-SM-8D6Transcobalamin receptor ;TCblR;; CD320
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Species
Human
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Source
E. coli
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Tag
N- GST
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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
36-231aa
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Molecular Weight
47.1 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
Related Products
Identification
Protein Description
TCblR/CD320 is a receptor that plays a crucial role in vitamin B12 uptake and transport, primarily in the context of cellular physiology and nutrition. Vitamin B12, also known as cobalamin, is essential for various biological processes, including DNA synthesis, red blood cell formation, and neurological function. The interaction between TCblR/CD320 and its ligand, transcobalamin II (TC), facilitates the cellular absorption of vitamin B12, thereby influencing systemic levels of this vital nutrient. Dysregulation of TCblR/CD320 has been implicated in several health issues, including anemia, neurological disorders, and developmental problems, highlighting its importance in both health and disease. Research into the recombinant expression of TCblR/CD320 protein not only aids in understanding the biochemical pathways associated with vitamin B12 transport but also provides insight into potential therapeutic targets for conditions arising from vitamin B12 deficiency. By generating and characterizing recombinant TCblR/CD320, scientists aim to elucidate its structure-function relationship, paving the way for the development of interventions that could enhance vitamin B12 bioavailability and mitigate the effects of related deficiencies. Moreover, this research has broad implications for nutritional science, cellular metabolism, and public health, emphasizing the need for continued investigation into the mechanisms governing vitamin B12 metabolism and the role of TCblR/CD320 as a functional component within this context.
