Analytical Data
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Gene name
NAAA
- Application
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Alternative Names
NAAA；ASAHL；PLT；；N-acylethanolamine-hydrolyzing acid amidase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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
1-359aa
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AA Sequence
MRTADREARPGLPSLLLLLLAGAGLSAASPPAAPRFNVSLDSVPELRWLPVLRHYDLDLVRAAMAQVIGDRVPKWVHVLIGKVVLELERFLPQPFTGEIRGMCDFMNLSLADCLLVNLAYESSVFCTSIVAQDSRGHIYHGRNLDYPFGNVLRKLTVDVQFLKNGQIAFTGTTFIGYVGLWTGQSPHKFTVSGDERDKGWWWENAIAALFRRHIPVSWLIRATLSESENFEAAVGKLAKTPLIADVYYIVGGTSPREGVVITRNRDGPADIWPLDPLNGAWFRVETNYDHWKPAPKEDDRRTSAIKALNATGQANLSLEALFQILSVVPVYNNFTIYTTVMSAGSPDKYMTRIRNPSRK
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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
NAAA (N-acylated amino acid amidohydrolase) is a serine hydrolase enzyme that plays a critical role in lipid metabolism by hydrolyzing N-acyl amino acids and contributing to the regulation of N-acylsphingosines, which are bioactive lipids involved in various cellular processes. Research into NAAA has gained momentum due to its potential implications in health and disease, particularly concerning metabolic disorders, inflammation, and pain signaling. Dysregulation of NAAA activity has been associated with several pathological conditions, including obesity, cardiovascular diseases, and cancer. Thus, understanding the structure and function of NAAA, as well as developing recombinant forms of the enzyme, is pivotal for elucidating its biological significance and exploring therapeutic applications. Recombinant NAAA proteins are being studied for their biochemical properties and potential as drug targets or therapeutic agents. Advances in recombinant DNA technology allow for the production of highly pure and active enzyme preparations, facilitating detailed studies of enzyme kinetics, substrate specificity, and inhibitor interactions. Furthermore, the potential development of NAAA inhibitors or modulators could lead to novel treatments for conditions driven by its dysregulation. The integration of structural biology techniques, such as X-ray crystallography and NMR spectroscopy, with biochemical assays, continues to provide valuable insights into the molecular mechanisms of NAAA function and regulation, thereby enhancing our understanding of its role in disease and opening avenues for targeted therapies. Overall, research on recombinant NAAA proteins is poised to contribute significantly to the fields of biochemistry and pharmacology, underscoring the enzyme's importance in both basic research and clinical applications.
