Analytical Data
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Gene name
GNPTG
- Application
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Alternative Names
GlcNAc-1-phosphotransferase subunit gamma;UDP-N-acetylglucosamine-1-phosphotransferase subunit gamma
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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
Q9UJJ9
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Expression Region
25-305aa
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AA Sequence
AKMKVVEEPNAFGVNNPFLPQASRLQAKRDPSPVSGPVHLFRLSGKCFSLVESTYKYEFCPFHNVTQHEQTFRWNAYSGILGIWHEWEIANNTFTGMWMRDGDACRSRSRQSKVELACGKSNRLAHVSEPSTCVYALTFETPLVCHPHALLVYPTLPEALQRQWDQVEQDLADELITPQGHEKLLRTLFEDAGYLKTPEENEPTQLEGGPDSLGFETLENCRKAHKELSKEIKRLKGLLTQHGIPYTRPTETSNLEHLGHETPRAKSPEQLRGDPGLRGSL
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Molecular Weight
38.7 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
Gnptg, or N-acetylglucosamine-1-phosphate transferase gamma subunit, plays a crucial role in lysosomal enzyme biogenesis by facilitating the phosphorylation of lysosomal enzymes, which is essential for their proper sorting and function. Mutations in the GNPTG gene have been linked to several lysosomal storage disorders, including mucolipidosis II and III, which are characterized by the accumulation of undegraded substrates in the lysosomes, leading to severe clinical manifestations such as cognitive impairment, organ dysfunction, and skeletal abnormalities. Understanding the molecular mechanisms underlying GNPTG function and its encoded protein is vital for developing potential therapeutic strategies for these genetic disorders. Additionally, recombinant GNPTG protein serves as a valuable tool for studying enzyme-enzyme interactions, understanding the phosphorylation process of lysosomal enzymes, and screening small-molecule inhibitors that may assist in the treatment of related disorders. Recent advances in protein expression and purification techniques have allowed for detailed structural and functional analyses of GNPTG, paving the way for potential gene therapy approaches and molecular interventions aimed at ameliorating the effects of GNPTG-related disease. As research in this area continues to evolve, the insights gained could one day lead to more effective treatments and improved quality of life for patients affected by lysosomal storage disorders caused by GNPTG mutations.
