Analytical Data
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Gene name
Carnosine Dipeptidase 1/CNDP1
- Application
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Alternative Names
CN1; CPGL2; Beta-Ala-His Dipeptidase; Metallopeptidase M20; Carnosinase 1; Serum carnosinase; Glutamate Carboxypeptidase-Like Protein 2
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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 95% as determined by SDS-PAGE.
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Uniprot
Q96KN2
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Expression Region
Asp332~His507
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Molecular Weight
24kDa
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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
Carnosine Dipeptidase 1 (CNDP1) is an important enzyme involved in the metabolism of dipeptides, particularly carnosine, which is a natural antioxidant and has various physiological roles, including muscle endurance, neuroprotection, and potential anti-aging effects. The CNDP1 enzyme catalyzes the hydrolysis of carnosine into its constituent amino acids, thereby regulating the levels of this dipeptide in tissues. Recent studies have highlighted the significance of CNDP1 in various pathological conditions, such as diabetes and neurodegenerative diseases, suggesting that modulation of its activity could have therapeutic implications. The recombinant production of CNDP1 offers a valuable tool for understanding its biochemical properties and functional mechanisms. Researchers are keen on characterizing this enzyme to elucidate its role in physiological and pathological processes, as well as to explore potential applications in biomedical research and therapeutic interventions. By generating a stable source of CNDP1, scientists can investigate its substrate specificity, kinetic parameters, and regulatory mechanisms, which are crucial for developing novel strategies to manipulate its activity in disease contexts. Furthermore, CNDP1's involvement in modulating the effects of oxidative stress and inflammation positions it as a promising target for drug development aimed at enhancing healthspan and treating age-related disorders.
