Analytical Data
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Gene name
NAAA
- Application
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Alternative Names
ASAHL; PLT; N-Acylethanolamine-Hydrolyzing Acid Amidase; N-Acylsphingosine Amidohydrolase Like; Acid ceramidase-like protein
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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
Q02083
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Expression Region
Asp112~Lys359
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Molecular Weight
28kDa
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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
The study of the NAAA (N-acylethanolamine acid amidase) recombinant protein has garnered significant attention in recent years due to its potential implications in various physiological and pathological processes. NAAA is an important enzyme involved in the metabolism of bioactive lipids, specifically in the hydrolysis of N-acylethanolamines, which play crucial roles in modulating pain, inflammation, and neuroprotection. Dysregulation of NAAA activity has been associated with several health conditions, including neurodegenerative diseases, metabolic disorders, and pain syndromes. Recombinant production of NAAA allows for detailed characterization of its enzymatic properties, substrate specificity, and functional role in lipid metabolism. Furthermore, understanding the molecular mechanisms underlying NAAA's activity may lead to the development of novel therapeutic strategies targeting pain and inflammation. Advances in recombinant protein technology, such as the use of expression systems and purification methods, have facilitated the exploration of NAAA's structure-function relationships, paving the way for the design of inhibitors or modulators that could enhance its therapeutic potential. Consequently, research into NAAA recombinant protein not only contributes to our fundamental understanding of lipid signaling pathways but also holds promise for the development of innovative treatments for various diseases.
