UGT1A1 Protein (Myc-DYKDDDDK Tag)
Quick Overview for UGT1A1 Protein (Myc-DYKDDDDK Tag) (ABIN2734988)
Target
See all UGT1A1 ProteinsProtein Type
Origin
Source
Application
Purity
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Purification tag / Conjugate
- This UGT1A1 protein is labelled with Myc-DYKDDDDK Tag.
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Characteristics
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- Recombinant human UGT1A1 protein expressed in HEK293 cells.
- Produced with end-sequenced ORF clone
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Application Notes
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Recombinant human proteins can be used for:
Native antigens for optimized antibody production
Positive controls in ELISA and other antibody assays -
Comment
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The tag is located at the C-terminal.
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Restrictions
- For Research Use only
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Concentration
- 50 μg/mL
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Buffer
- 25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10 % glycerol.
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Storage
- -80 °C
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Storage Comment
- Store at -80°C. Thaw on ice, aliquot to individual single-use tubes, and then re-freeze immediately. Only 2-3 freeze thaw cycles are recommended.
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- UGT1A1 (UDP Glucuronosyltransferase 1 Family, Polypeptide A1 (UGT1A1))
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Alternative Name
- Ugt1a1
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Background
- This gene encodes a UDP-glucuronosyltransferase, an enzyme of the glucuronidation pathway that transforms small lipophilic molecules, such as steroids, bilirubin, hormones, and drugs, into water-soluble, excretable metabolites. This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen unique alternate first exons followed by four common exons. Four of the alternate first exons are considered pseudogenes. Each of the remaining nine 5&apos exons may be spliced to the four common exons, resulting in nine proteins with different N-termini and identical C-termini. Each first exon encodes the substrate binding site, and is regulated by its own promoter. The preferred substrate of this enzyme is bilirubin, although it also has moderate activity with simple phenols, flavones, and C18 steroids. Mutations in this gene result in Crigler-Najjar syndromes types I and II and in Gilbert syndrome.
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Molecular Weight
- 57.1 kDa
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NCBI Accession
- NP_000454
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Pathways
- Steroid Hormone Biosynthesis, Regulation of Lipid Metabolism by PPARalpha
Target
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