CBR3 Antibody (YA2395)
(Synonyms: CBR3; Carbonyl reductase [NADPH] 3; NADPH-dependent carbonyl reductase 3)CBR3 Antibody (YA2395) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to CBR3.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB
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Reactivity :
Human
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Formulation:
Supplied in 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.01% Sodium azide and 0.05% BSA
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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|---|---|
| Dilution Ratio | 1:500-1:1000 |
Product Details
CBR3 Antibody (YA2395) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to CBR3.
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Host Rabbit
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Clonality Recombinant,Monoclonal
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Species ReactivityHuman
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Observed Molecular WeightObserved band size: 31 kDaNote: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 31 kDa
A synthetic peptide of human CBR3
Endogenous
Affinity Purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.01% Sodium azide and 0.05% BSA
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
Carbonyl reductase 3 (CBR3) is a member of the short-chain dehydrogenase/reductase (SDR) superfamily and functions as a monomeric NADPH-dependent oxidoreductase that catalyzes the reduction of biologically and pharmacologically active carbonyl compounds to their corresponding alcohols[1][2]. Mechanistically, CBR3 participates in carbonyl detoxification and xenobiotic metabolism, processes that regulate the cellular handling of endogenous reactive carbonyls and therapeutic agents[3][4]. The gene was mapped to chromosome 21q22.2 and is closely linked to CBR1, supporting its classification within the monomeric carbonyl reductase family while indicating a distinct genetic locus and regulatory context[1]. In disease-relevant settings, CBR3 has attracted attention because genetic variation alters enzymatic activity toward pharmacologically important substrates, including anthracycline-related compounds, thereby influencing interindividual differences in drug metabolism[2][5]. Compared with the closely related isoform CBR1, CBR3 exhibits distinct functional properties and substrate-recognition characteristics, indicating nonredundant biological roles despite substantial sequence similarity[4][6]. Experimental studies further demonstrated that the common CBR3 V244M variant encodes enzymes with different catalytic efficiencies and NADP (H) -dependent kinetic properties, making this polymorphism a useful model for investigating carbonyl reduction pathways and pharmacogenomic mechanisms[2]. Regulation of CBR3 expression by the oxidative stress-responsive transcription factor Nrf2 additionally links this enzyme to cellular redox adaptation and xenobiotic response networks[3].
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Subcellular Localization
Cytoplasm
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Expression
Tissue_specificity:Detected in ovary, pancreas, intestine, colon, kidney, brain, thymus, lung, heart, liver, spleen, leukocyte, prostate and testis -
SwissProt ID
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Synonyms
CBR3; Carbonyl reductase [NADPH] 3; NADPH-dependent carbonyl reductase 3
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Research Field
Signal Transduction
Documentation
References
[1]. Watanabe K, et al. Mapping of a novel human carbonyl reductase, CBR3, and ribosomal pseudogenes to human chromosome 21q22.2. Genomics. 1998 Aug 15;52(1):95-100. [Content Brief]
[2]. Lakhman SS, et al. Functional significance of a natural allelic variant of human carbonyl reductase 3 (CBR3). Drug Metab Dispos. 2005 Feb;33(2):254-7. [Content Brief]
[3]. Ebert B, et al. Regulation of human carbonyl reductase 3 (CBR3; SDR21C2) expression by Nrf2 in cultured cancer cells. Biochemistry. 2010 Oct 5;49(39):8499-511. [Content Brief]
[4]. Miura T, et al. Different functions between human monomeric carbonyl reductase 3 and carbonyl reductase 1. Mol Cell Biochem. 2008 Aug;315(1-2):113-21. [Content Brief]
[5]. Bains OS, et al. Naturally occurring variants of human CBR3 alter anthracycline in vitro metabolism. J Pharmacol Exp Ther. 2010 Mar;332(3):755-63. [Content Brief]
[6]. Pilka ES, et al. Structural basis for substrate specificity in human monomeric carbonyl reductases. PLoS One. 2009 Oct 20;4(10):e7113. [Content Brief]