Analytical Data
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Gene name
NDST1
- Application
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Alternative Names
Glucosaminyl N-deacetylase/N-sulfotransferase 1 ;NDST-1N-heparan sulfate sulfotransferase 1 ;N-HSST 1[Heparan sulfate]-glucosamine N-sulfotransferase 1 ;HSNST 1 2 domains:Heparan sulfate N-deacetylase 1 (EC:3.-.-.-)Heparan sulfate N-sulfotransferase 1 (EC:2.8.2.-)
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P52848
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Expression Region
40-556aa
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Molecular Weight
73.5 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
NDST1 (N-deacetylase/N-sulfotransferase 1) is an essential enzyme involved in the biosynthesis of heparan sulfate, a significant glycosaminoglycan that plays crucial roles in various biological processes, including cell signaling, development, and tissue repair. Mutations in the NDST1 gene have been associated with a rare genetic disorder known as Schwartz-Jampel syndrome, characterized by skeletal anomalies, muscle stiffness, and other developmental issues. Understanding the structure and function of NDST1 is vital for elucidating its role in heparan sulfate synthesis and the pathophysiology of associated disorders. Recent studies have focused on the expression and purification of recombinant NDST1 to investigate its enzymatic activity and substrate specificity. By employing advanced biochemical techniques and structural biology approaches, researchers aim to uncover the molecular mechanisms underlying NDST1 function and its contributions to cellular signaling pathways. The insights gained from these studies may pave the way for novel therapeutic strategies targeting diseases linked to NDST1 dysfunction and improve our understanding of glycosaminoglycan biology.
