Analytical Data
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Gene name
GALNT14
- Application
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Alternative Names
Polypeptide GalNAc transferase 14 ;GalNAc-T14 ;pp-GaNTase 14Protein-UDP acetylgalactosaminyltransferase 14UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14
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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
Q96FL9
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Expression Region
1-552aa
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Molecular Weight
80.3 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
GALNT14, a member of the Golgi N-acetylgalactosaminyltransferase family, plays a crucial role in the initiation of O-glycosylation, a post-translational modification that significantly influences protein function, stability, and cell signaling. Alterations in GALNT14 expression and activity have been linked to various diseases, including cancer, where aberrant glycosylation patterns can contribute to tumor progression and metastasis. The study of GALNT14 recombinant proteins is essential for understanding its enzymatic properties and substrate specificity, which can elucidate its biological functions and the pathways it regulates. By generating recombinant GALNT14, researchers can investigate its role in glycosylation processes and how it interacts with different substrates. Furthermore, the development of monoclonal antibodies against GALNT14 can be valuable for clinical diagnostics and therapeutic applications. Ongoing research aims to explore the potential of targeting GALNT14 for cancer treatment and to unravel the complex mechanisms by which it influences cellular behavior, ultimately contributing to the development of novel therapeutic strategies in oncology and beyond.
