Recombinant Human UGT1A1 protein (denatured)
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Recombinant Human UGT1A1 protein (denatured) is a Human Fragment protein, in the 25 to 490 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
View Alternative Names
GNT1, UGT1, UGT1A1, UDP-glucuronosyltransferase 1A1, Bilirubin-specific UDPGT isozyme 1, UDP-glucuronosyltransferase 1-1, UDP-glucuronosyltransferase 1A isoform 1, hUG-BR1, UDPGT 1-1, UGT1*1, UGT1-01, UGT1.1
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human UGT1A1 protein (denatured) (AB202607)
15% SDS-PAGE analysis of ab202607 (3μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
UGT1A1 contributes to the detoxification processes by mediating the conjugation of bilirubin a byproduct of red blood cell breakdown. This enzyme is part of the UGT1 complex which includes several enzymes sharing a similar expression pattern and function. Through its activity UGT1A1 helps maintain homeostasis and prevents the buildup of potentially toxic substances in the organism.
Pathways
UGT1A1 is a significant component of the glucuronidation pathway. This pathway is essential for phase II metabolism in the liver working alongside other proteins like UGT1A6 and UGT1A9. The glucuronidation pathway transforms hydrophobic compounds into hydrophilic derivatives for easier elimination. Additionally UGT1A1 activity affects hormone metabolism particularly in the pathways involving estrogen and thyroid hormones.
Specifications
Form
Liquid
Additional notes
ab202607 was purified by conventional chromatography techniques
General info
Function
Isoform 1. UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed : 12181437, PubMed : 15472229, PubMed : 18004206, PubMed : 18004212, PubMed : 18719240, PubMed : 19830808, PubMed : 23288867). Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds (PubMed : 12181437, PubMed : 18004206, PubMed : 18004212). Catalyzes the glucuronidation of endogenous estrogen hormones such as estradiol, estrone and estriol (PubMed : 15472229, PubMed : 18719240, PubMed : 23288867). Involved in the glucuronidation of bilirubin, a degradation product occurring in the normal catabolic pathway that breaks down heme in vertebrates (PubMed : 17187418, PubMed : 18004206, PubMed : 19830808, PubMed : 24525562). Also catalyzes the glucuronidation the isoflavones genistein, daidzein, glycitein, formononetin, biochanin A and prunetin, which are phytoestrogens with anticancer and cardiovascular properties (PubMed : 18052087, PubMed : 19545173). Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonist losartan, a drug which can inhibit the effect of angiotensin II (PubMed : 18674515). Involved in the biotransformation of 7-ethyl-10-hydroxycamptothecin (SN-38), the pharmacologically active metabolite of the anticancer drug irinotecan (PubMed : 12181437, PubMed : 18004212, PubMed : 20610558).. Isoform 2. Lacks UGT glucuronidation activity but acts as a negative regulator of isoform 1.
Sequence similarities
Belongs to the UDP-glycosyltransferase family.
Target data
Product promise
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