Analytical Data
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Gene name
GALNS
- Application
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Alternative Names
CS; GAS; MPS4A; GALNAC6S; Chondroitin Sulfatase; Chondroitinase; Galactosamine(N-Acetyl)-6-Sulfate Sulfatase; Morquio Syndrome; Mucopolysaccharidosis Type IVA
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q571E4
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Expression Region
Asp168~Asp377
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Molecular Weight
27kDa
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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
GALNS (N-acetylgalactosamine-6-sulfatase) is an essential enzyme involved in the lysosomal degradation of glycosaminoglycans, specifically in the metabolism of keratan sulfate and dermatan sulfate. Mutations in the GALNS gene lead to a genetic disorder known as mucopolysaccharidosis type IVA (MPS IVA), or Morquio A syndrome, which is characterized by skeletal dysplasia, joint problems, and progressive functional impairments. The understanding of GALNS structure and function has been a significant focus in biomedical research due to its critical role in cellular metabolism and the disease’s impactful symptoms. Recent advancements in recombinant protein technology have facilitated the production of GALNS for therapeutic purposes, enabling researchers to explore enzyme replacement therapy (ERT) as a promising treatment avenue for patients suffering from MPS IVA. This approach aims to alleviate symptoms and improve quality of life by supplementing the deficient enzyme. Studies investigating the biochemical properties, activity, and stability of recombinant GALNS are essential to optimizing dosage, administration routes, and treatment regimens. Furthermore, understanding the enzyme's molecular interactions and degradation pathways can enhance our knowledge of lysosomal storage disorders, paving the way for the development of additional therapeutic strategies. As the field progresses, the ongoing research on GALNS recombinant proteins holds promise for improved outcomes in managing MPS IVA and potentially other similar lysosomal storage diseases.
