Analytical Data
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Gene name
GALNT1
- Application
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Alternative Names
GALNAC T1; GalNAc transferase 1; GalNAc-T1; GALNT 1; GALNT1; GALT1_HUMAN; Polypeptide GalNAc transferase 1; Polypeptide N acetylgalactosaminyltransferase 1; Polypeptide N-acetylgalactosaminyltransferase 1 soluble form; pp GaNTase 1; pp-GaNTase 1; Protein UDP acetylgalactosaminyltransferase 1
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q10472
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Expression Region
1-105aa
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AA Sequence
MRKFAYCKVVLATSLIWVLLDMFLLLYFSECNKCDEKKERGLPAGDVLEPVQKPHEGPGEMGKPVVIPKEDQEKMKEMFKINQFNLMASEMIALNRSLPDVRLEG
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Molecular Weight
38.4 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
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Protein Description
GALNT1 (Polypeptide N-Acetylgalactosaminyltransferase 1) is an enzyme involved in the post-translational modification of proteins through O-glycosylation, specifically by adding N-acetylgalactosamine (GalNAc) to serine or threonine residues on target proteins. This modification plays a crucial role in various biological processes, including cell signaling, adhesion, and immune responses. Recent studies have highlighted the importance of GALNT1 in developmental biology and its implications in diseases, such as cancer and congenital disorders. Aberrant glycosylation patterns associated with GALNT1 dysregulation have been linked to tumor progression and metastasis, making it a potential biomarker for cancer diagnostics and therapy. The recombinant production of GALNT1 is fundamental for understanding its enzymatic mechanisms and functional roles in glycosylation. Researchers aim to elucidate the structure-function relationship of GALNT1 through overexpression in suitable host systems, enabling the investigation of its activity, stability, and interactions with substrate proteins. Additionally, characterizing GALNT1 in a recombinant format provides a platform for high-throughput screening of small molecules or inhibitors that can modulate its activity, offering insights into therapeutic avenues for diseases related to glycosylation anomalies. Ultimately, the study of GALNT1 through recombinant protein research holds promise for advancing our knowledge of glycosylation and its impact on health and disease.
