Analytical Data
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Gene name
NT5C1B
- Application
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Alternative Names
AIRP; CN-IB; Autoimmune infertility-related protein
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Species
Mouse
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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
Q91YE9
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Expression Region
Arg261~Asn573
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Molecular Weight
39kDa
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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
NT5C1B, or Nicotinamide adenine dinucleotide (NAD)-binding protein, plays a crucial role in cellular metabolism, particularly in the synthesis and hydrolysis of nucleotides. This enzyme has garnered attention in the realm of biochemical research due to its involvement in various physiological processes, including the regulation of intracellular signaling pathways, cellular stress responses, and energy metabolism. Abnormalities in NT5C1B expression or function have been implicated in several diseases, including neurodegenerative disorders and certain types of cancer, highlighting its potential as a therapeutic target. The study of recombinant NT5C1B proteins enables scientists to dissect the enzyme's structure-function relationship, elucidate its catalytic mechanisms, and explore its interactions with other cellular components. By implementing advanced techniques such as X-ray crystallography and various biochemical assays, researchers aim to uncover the intricacies of NT5C1B's role in cellular processes. Understanding the fundamental biology of NT5C1B could pave the way for novel drug development and therapeutic strategies, ultimately contributing to the treatment of diseases related to nucleotide metabolism dysfunction. Given the enzyme's significant physiological implications and potential for clinical applications, continued research into recombinant NT5C1B proteins remains a vital area of interest within the biomedical community.
