Analytical Data
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Gene name
GALNTL6
- Application
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Alternative Names
Polypeptide GalNAc transferase 17 (GalNAc-T17) (pp-GaNTase 17) (Protein-UDP acetylgalactosaminyltransferase 17) (Putative polypeptide N-acetylgalactosaminyltransferase 17) (polypeptide N-acetylgalactosaminyltransferase 17)
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q49A17
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Expression Region
29-601aa
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Molecular Weight
70.7 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
GALNTL6 (polypeptide N-acetylgalactosaminyltransferase-like 6) is a member of the GALNT family of enzymes, which play a crucial role in the initiation of O-glycosylation, a process essential for protein function and stability. The GALNTL6 gene is noteworthy for its potential involvement in various biological processes and diseases, including cancer and cell signaling. Previous studies have shown that altered expression of GALNT family members can significantly impact tumor progression and metastasis. However, the specific functions and mechanisms of GALNTL6 remain poorly understood, largely due to the lack of detailed characterization of the protein and its enzymatic activity. This has prompted researchers to investigate the recombinant expression of GALNTL6 to elucidate its biochemical properties and functional roles. Recombinant GALNTL6 produced in heterologous systems allows for the study of its glycosyltransferase activity and interactions with substrates, providing insights into its physiological and pathological relevance. Understanding GALNTL6’s function could reveal new therapeutic targets for cancer treatment and deepen our knowledge about the regulatory mechanisms of O-glycosylation in cellular processes. The ongoing research into GALNTL6 is aimed at clarifying its contributions to glycosylation pathways and its potential implications in cancer biology, thereby advancing the field of glycobiology and enhancing the development of targeted therapies.
