Analytical Data
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Gene name
GALGT
- Application
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Alternative Names
B4GALNT1. GALGT. SIAT2
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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
Q00973
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Expression Region
1-328aa
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AA Sequence
MWLGRRALCALVLLLACASLGLLYASTRDAPGLRLPLAPWAPPQSPRRPELPDLAPEPRYAHIPVRIKEQVVGLLAWNNCSCESSGGGLPLPFQKQVRAIDLTKAFDPAELRAASATREQEFQAFLSRSQSPADQLLIAPANSPLQYPLQGVEVQPLRSILVPGLSLQAASGQEVYQVNLTASLGTWDVAGEVTGVTLTGEGQADLTLVSPGLDQLNRQLQLVTYSSRSYQTNTADTGARPGWRDGQAGQTEKNQKGWSGQMAEGMGGIWAMARAVQPHNGCFNWTSRARGRKGAFVHLGLEQARGKPEPWVCLPFRPTVGGPRKRLV
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Molecular Weight
61.9 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
GALGT, or Galactosyltransferase, is an important enzyme involved in the glycosylation process, where sugar molecules are added to proteins and lipids, impacting their stability, localization, and function. The study of GALGT and its recombinant protein has gained attention due to its critical role in various biological processes, including cell signaling, immune response, and the development of certain diseases. A deeper understanding of GALGT can provide insights into its structure-function relationships and the mechanisms underlying glycosylation. Researchers have been interested in expressing and purifying recombinant GALGT to explore its enzymatic activity, substrate specificity, and potential applications in biotechnology and medicine, such as targeted drug delivery and cancer therapy. By utilizing recombinant DNA technology to produce GALGT in various host systems, scientists aim to characterize this enzyme's kinetics and regulatory mechanisms, which could lead to advancements in therapeutic strategies and the development of novel glycoproteins with enhanced medicinal properties. Overall, the investigation of GALGT recombination not only enriches our comprehension of glycosylation but also opens new avenues for biopharmaceutical innovation.











