Analytical Data
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Gene name
GNS
- Application
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Alternative Names
GNS；N-acetylglucosamine-6-sulfatase
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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
P15586
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Expression Region
37-552aa
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AA Sequence
VFGVAAGTRRPNVVLLLTDDQDEVLGGMTPLKKTKALIGEMGMTFSSAYV PSALCCPSRASILTGKYPHNHHVVNNTLEGNCSSKSWQKIQEPNTFPAIL RSMCGYQTFFAGKYLNEYGAPDAGGLEHVPLGWSYWYALEKNSKYYNYTL SINGKARKHGENYSVDYLTDVLANVSLDFLDYKSNFEPFFMMIATPAPHS PWTAAPQYQKAFQNVFAPRNKNFNIHGTNKHWLIRQAKTPMTNSSIQFLD NAFRKRWQTLLSVDDLVEKLVKRLEFTGELNNTYIFYTSDNGYHTGQFSL PIDKRQLYEFDIKVPLLVRGPGIKPNQTSKMLVANIDLGPTILDIAGYDL NKTQMDGMSLLPILRGASNLTWRSDVLVEYQGEGRNVTDPTCPSLSPGVS QCFPDCVCEDAYNNTYACVRTMSALWNLQYCEFDDQEVFVEVYNLTADPD QITNIAKTIDPELLGKMNYRLMMLQSCSGPTCRTPGVFDPGYRFDPRLMF SNRGSVRTRRFSKHLLVDHHHHHH
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Molecular Weight
58 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
Related Products
Protein Description
GNS, or Glucosamine-6-sulfate N-acetyltransferase, is a pivotal enzyme involved in the biosynthesis of glycosaminoglycans, which are essential components of extracellular matrices and play critical roles in cellular signaling, tissue hydration, and structural integrity. Research into GNS and its recombinant proteins has garnered significant attention due to its potential implications in understanding various diseases, particularly those related to cartilage degradation and osteoarthritis. The ability to produce GNS as a recombinant protein allows for detailed biochemical characterization, functional studies, and the exploration of its enzymatic pathways. Furthermore, recombinant GNS can be leveraged for therapeutic applications, such as in drug development and regenerative medicine, by enhancing the understanding of glycosaminoglycan metabolism and its alterations in disease states. Advances in recombinant DNA technology have made it feasible to generate GNS proteins with specific modifications, enabling researchers to probe its structural and functional properties more effectively. This research not only contributes to the fundamental understanding of glycosaminoglycan biosynthesis but also opens new avenues for the development of targeted therapies in disorders associated with connective tissue dysfunction. As such, the study of recombinant GNS is positioned at the intersection of biochemistry, molecular biology, and therapeutic innovation, highlighting its significance in both basic research and clinical applications.
