Analytical Data
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Gene name
NAGa
- Application
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Alternative Names
NAGa；N-acetylglucosamine-6-phosphate deacetylase
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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
P17050
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Expression Region
18-411aa
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AA Sequence
LDNGLLQTPPMGWLAWERFRCNINCDEDPKNCISEQLFMEMADRMAQDGW RDMGYTYLNIDDCWIGGRDASGRLMPDPKRFPHGIPFLADYVHSLGLKLG IYADMGNFTCMGYPGTTLDKVVQDAQTFAEWKVDMLKLDGCFSTPEERAQ GYPKMAAALNATGRPIAFSCSWPAYEGGLPPRVNYSLLADICNLWRNYDD IQDSWWSVLSILNWFVEHQDILQPVAGPGHWNDPDMLLIGNFGLSLEQSR AQMALWTVLAAPLLMSTDLRTISAQNMDILQNPLMIKINQDPLGIQGRRI HKEKSLIEVYMRPLSNKASALVFFSCRTDMPYRYHSSLGQLNFTGSVIYE AQDVYSGDIISGLRDETNFTVIINPSGVVMWYLYPIKNLEMSQQHHHHHH
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Molecular Weight
46 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
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Protein Description
NAGa, or N-acetyl-α-D-galactosaminidase, is an enzyme that plays a crucial role in the lysosomal degradation of glycoproteins and glycolipids. As a key component in the metabolic pathway of glycoproteins, it is intricately involved in various physiological processes, including cell signaling, immune response, and cellular interaction. Research into NAGa has gained significance due to its implications in several disorders, particularly lysosomal storage diseases, which arise from deficiencies in enzyme activity leading to the accumulation of substrates that the enzymes normally degrade. Previous studies have highlighted the potential of NAGa as a therapeutic target, especially with advances in protein engineering and recombinant DNA technology. The generation of recombinant NAGa offers the possibility of enzyme replacement therapies for affected individuals. Moreover, understanding its structure-function relationships can provide insights into its catalytic mechanism and substrate specificity, aiding in the design of inhibitors or modulators. Current research focuses on elucidating the detailed biochemical properties of NAGa, exploring its therapeutic potentials, and developing strategies for effective delivery of recombinant protein therapies. As advancements in biotechnological methods continue to evolve, the exploration of NAGa could pave the way for innovative treatments for lysosomal storage disorders and enhance our understanding of glycoprotein metabolism in health and disease.
