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AB89274

Anti-UGT2B15 antibody

4

(1 Review)

|

(4 Publications)

Mouse Polyclonal UGT2B15 antibody. Carrier free. Suitable for WB and reacts with Human samples. Cited in 4 publications. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human UGT2B15.

View Alternative Names

UGT2B8, UGT2B15, UDP-glucuronosyltransferase 2B15, UDPGT 2B15, HLUG4, UDP-glucuronosyltransferase 2B8, UDPGTh-3, UDPGT 2B8

1 Images
Western blot - Anti-UGT2B15 antibody (AB89274)
  • WB

Unknown

Western blot - Anti-UGT2B15 antibody (AB89274)

All lanes:

Western blot - Anti-UGT2B15 antibody (ab89274) at 1 µg/mL

All lanes:

Human liver lysate at 50 µg

Predicted band size: 61 kDa

Observed band size: 55 kDa

true

Key facts

Host species

Mouse

Clonality

Polyclonal

Isotype

IgG

Carrier free

Yes

Reacts with

Human

Applications

WB

applications

Immunogen

Recombinant Full Length Protein corresponding to Human UGT2B15.

P54855

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
pH: 7.4 Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

UGT2B15 also known as UDP-glucuronosyltransferase 2B15 plays an important role in the glucuronidation process. This enzyme belongs to the UDP-glycosyltransferase family and facilitates the attachment of glucuronic acid to small lipophilic molecules making them more water-soluble. UGT2B15 has a mass of approximately 56 kDa and finds its expression mainly in the liver but also in other tissues such as the prostate and testis. This distribution suggests its importance in the metabolism of various endogenous and exogenous compounds.
Biological function summary

Enzymes like UGT2B15 are important in the detoxification of substances. UGT2B15 facilitates the metabolism and clearance of steroid hormones including androgens and nonsteroids such as drugs. It does not operate as part of a larger complex but works individually to modify substrates. This process converts lipophilic drugs and hormones into more excretable forms aiding in homeostasis.

Pathways

UGT2B15 functions within important metabolic pathways such as steroid metabolism and drug detoxification pathways. In these pathways it interacts with other UGT family members such as UGT2B17 to ensure the efficient metabolism of various substrates. Their actions help regulate steroid levels and detoxify therapeutic drugs keeping physiological functions balanced by preventing the accumulation of potentially harmful compounds.

Researchers associate UGT2B15 with conditions like prostate cancer and drug resistance. Altered expression or function of this enzyme may contribute to the development and progression of prostate cancer by affecting androgen metabolism. Additionally UGT2B15 plays a role in drug resistance often seen in therapies involving anti-cancer agents that require metabolic activation for clearance. Its activity connects with related proteins such as UGT2B17 influencing the progression and treatment responses in these conditions.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

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 : 16595710, PubMed : 18719240, PubMed : 23288867, PubMed : 7835232, PubMed : 9295060). Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds (PubMed : 7835232). Catalyzes the glucuronidation of endogenous steroid hormones such as androgens (testosterone, androsterone) and estrogens (estradiol, epiestradiol, estriol, catechol estrogens) (PubMed : 16595710, PubMed : 18719240, PubMed : 23288867, PubMed : 7835232, PubMed : 9295060). Displays glucuronidation activity toward several classes of xenobiotic substrates, including phenolic compounds (eugenol, 4-nitrophenol, 4-hydroxybiphenyl) and phenylpropanoids (naringenin, coumarins) (PubMed : 7835232). Catalyzes the glucuronidation of monoterpenoid alcohols such as borneol, menthol and isomenthol, a class of natural compounds used in essential oils (By similarity).
See full target information UGT2B15

Publications (4)

Recent publications for all applications. Explore the full list and refine your search

Cancers 15: PubMed38136265

2023

Androgen Receptor/AP-1 Activates Transcription to Promote Esophageal Squamous Cell Carcinoma Invasion.

Applications

Unspecified application

Species

Unspecified reactive species

Jiahui Cai,Furong Huang,Wenyan Gao,Tongyang Gong,Hongyan Chen,Zhihua Liu

The Prostate 80:1223-1232 PubMed33258507

2020

AKR1C3 mediates pan-AR antagonist resistance in castration-resistant prostate cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Jennifer R Hertzog,Zhuming Zhang,Gilles Bignan,Peter J Connolly,Jason E Heindl,Christopher J Janetopoulos,Brent A Rupnow,Theresa M McDevitt

ACS pharmacology & translational science 2:453-467 PubMed32259077

2019

Revealing Metabolic Liabilities of Ralaniten To Enhance Novel Androgen Receptor Targeted Therapies.

Applications

Unspecified application

Species

Unspecified reactive species

Jon K Obst,Jun Wang,Kunzhong Jian,David E Williams,Amy H Tien,Nasrin Mawji,Teresa Tam,Yu Chi Yang,Raymond J Andersen,Kim N Chi,Bruce Montgomery,Marianne D Sadar

BMC cancer 17:463 PubMed28673330

2017

UDP-glucuronosyltransferases and biochemical recurrence in prostate cancer progression.

Applications

IHC-P

Species

Human

Delores J Grant,Zinan Chen,Lauren E Howard,Emily Wiggins,Amanda De Hoedt,Adriana C Vidal,Skyla T Carney,Jill Squires,Clara E Magyar,Jiaoti Huang,Stephen J Freedland
View all publications

Product promise

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