BDH2 Human

3-Hydroxybutyrate Dehydrogenase, Type 2 Human Recombinant
Cat. No.
BT7883
Source
Escherichia Coli.
Synonyms
3-hydroxybutyrate dehydrogenase type 2, FLJ13261, PRO20933, SDR15C1, UCPA-OR, UNQ6308, dehydrogenase/reductase (SDR family) member 6, Oxidoreductase UCPA, DHRS6, R-beta-hydroxybutyrate dehydrogenase, EFA6R, EC 1.1.1.30.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 95% as determined by SDS-PAGE.
Usage
THE BioTeks products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

BDH2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 265 amino acids (1-245a.a.) and having a molecular mass of 28.8kDa.
BDH2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
BDH2, a member of the short-chain dehydrogenases/reductases (SDR) family, plays a crucial role in the peripheral utilization of 3-hydroxybutyrate. Its cytoplasmic localization, NAD+ dependence, and kinetic parameters enable it to convert high levels of circulating 3-hydroxybutyrate into acetoacetate in the presence of a high oxidized NAD+ ratio.
Description
Produced in E. coli, our BDH2 is a non-glycosylated, single polypeptide chain comprising 265 amino acids (1-245a.a.) with a molecular weight of 28.8 kDa. It features a 20 amino acid His-tag at the N-terminus and undergoes purification using proprietary chromatographic techniques.
Physical Appearance
Clear, sterile-filtered solution.
Formulation
The BDH2 protein solution is provided at a concentration of 1 mg/ml in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 0.1 M NaCl, and 10% glycerol.
Purity
Purity exceeds 95% as determined by SDS-PAGE analysis.
Stability
For optimal storage, maintain the product at 4°C if it will be used within 2-4 weeks. For long-term storage, freeze the product at -20°C. Avoid repeated freeze-thaw cycles.
Synonyms
3-hydroxybutyrate dehydrogenase type 2, FLJ13261, PRO20933, SDR15C1, UCPA-OR, UNQ6308, dehydrogenase/reductase (SDR family) member 6, Oxidoreductase UCPA, DHRS6, R-beta-hydroxybutyrate dehydrogenase, EFA6R, EC 1.1.1.30.
Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MGRLDGKVII LTAAAQGIGQ AAALAFAREG AKVIATDINE SKLQELEKYP GIQTRVLDVT KKKQIDQFAN EVERLDVLFN VAGFVHHGTV LDCEEKDWDF SMNLNVRSMY LMIKAFLPKM LAQKSGNIIN MSSVASSVKG VVNRCVYSTT KAAVIGLTKS VAADFIQQGI RCNCVCPGTV DTPSLQERIQ ARGNPEEARN DFLKRQKTGR FATAEEIAML CVYLASDESA YVTGNPVIID GGWSL

Product Science Overview

Structure and Expression

BDH2 is a single, non-glycosylated polypeptide chain composed of 265 amino acids, with a molecular mass of approximately 28.8 kDa . The recombinant form of this enzyme is typically expressed in Escherichia coli (E. coli) and is purified using proprietary chromatographic techniques . The enzyme is often tagged with a His-tag at the N-terminus to facilitate purification .

Function and Mechanism

BDH2 mediates the formation of 2,5-dihydroxybenzoic acid (2,5-DHBA), a siderophore that shares structural similarities with bacterial enterobactin . This function is crucial for iron assimilation and homeostasis, as 2,5-DHBA associates with lipocalin 2 (LCN2), playing a key role in iron metabolism . Additionally, BDH2 acts as a 3-hydroxybutyrate dehydrogenase, converting 3-hydroxybutyrate into acetoacetate, which is an essential step in ketone body metabolism .

Clinical and Research Applications

The recombinant form of BDH2 is used extensively in biochemical research to study its role in ketone body metabolism and iron homeostasis . It is also utilized in high-throughput screening assays and other experimental setups to understand its enzymatic properties and potential therapeutic applications .

Storage and Stability

BDH2 is typically stored at -20°C for long-term stability, and it is recommended to avoid freeze-thaw cycles to maintain its activity . When stored properly, the enzyme remains stable and retains its functional properties for extended periods .

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