LDHB Human, His

Lactate Dehydrogenase B Human Recombinant, His Tag
Cat. No.
BT11251
Source
Escherichia Coli.
Synonyms
LDH-H, TRG-5, L-lactate dehydrogenase B chain, LDH-B, EC=1.1.1.27, Renal carcinoma antigen NY-REN-46, LDHB.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's 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

LDHB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 354 amino acids (1-334 a.a.) and having a molecular mass of 38.8 kDa. The LDHB is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
LDHB, a member of the lactate dehydrogenase family, is an oxidoreductase enzyme. It catalyzes the reversible conversion of pyruvate to lactate, coupled with the interconversion of NADH and NAD+. LDHB is also known to oxidize hydroxybutyrate and is often referred to as Hydroxybutyrate Dehydrogenase (HBD). The LDH family includes LDH-A, LDH-B, and LDH-C. LDH enzymes serve as significant markers for germ cell tumors.
Description
Recombinant Human LDHB, produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 354 amino acids, including a 20 amino acid His-Tag fused at the N-terminus (1-334 a.a.), and has a molecular weight of 38.8 kDa. Purification is achieved through proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
LDHB Human solution is provided in a buffer containing 20mM Tris-HCl (pH 8), 1mM DTT, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For longer storage, freeze at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 95.0% using SDS-PAGE analysis.
Biological Activity
The specific activity is measured to be greater than 6 units/mg. One unit is defined as the amount of enzyme required to convert 1.0 micromole of pyruvate to L-lactate and beta-NAD per minute at a pH of 7.5 and a temperature of 37°C.
Synonyms
LDH-H, TRG-5, L-lactate dehydrogenase B chain, LDH-B, EC=1.1.1.27, Renal carcinoma antigen NY-REN-46, LDHB.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MATLKEKLIA PVAEEEATVP NNKITVVGVG QVGMACAISI LGKSLADELA LVDVLEDKLK GEMMDLQHGS LFLQTPKIVA DKDYSVTANS KIVVVTAGVR QQEGESRLNL VQRNVNVFKF IIPQIVKYSP DCIIIVVSNP VDILTYVTWK LSGLPKHRVI GSGCNLDSAR FRYLMAEKLG IHPSSCHGWI LGEHGDSSVA VWSGVNVAGV SLQELNPEMG TDNDSENWKE VHKMVVESAY EVIKLKGYTN WAIGLSVADL IESMLKNLSR IHPVSTMVKG MYGIENEVFL SLPCILNARG LTSVINQKLK DDEVAQLKKS ADTLWDIQKD LKDL.

Product Science Overview

Structure and Expression

The human recombinant LDHB with a His tag is a bioactive protein that corresponds to the amino acids 1-334 of the human LDHB . It is expressed in Escherichia coli (E. coli) and purified using conventional chromatography techniques . The His tag, typically located at the N-terminus, facilitates the purification process by allowing the protein to bind to nickel or cobalt ions during affinity chromatography .

Functionality and Activity

LDHB is an oxidoreductase enzyme that plays a pivotal role in cellular respiration and energy production. It is involved in the conversion of pyruvate to lactate, a critical step in anaerobic glycolysis, which allows cells to produce energy under low oxygen conditions . The specific activity of the recombinant LDHB is greater than 300 units/mg, where one unit converts 1.0 µmole of pyruvate to L-lactate and beta-NAD per minute at pH 7.5 at 37°C .

Applications

Recombinant LDHB is widely used in research to study metabolic pathways, enzyme kinetics, and cellular respiration. It serves as a powerful marker for germ cell tumors and is utilized in various biochemical assays . The His tag aids in the easy purification and detection of the protein, making it a valuable tool in laboratory settings .

Storage and Stability

For optimal stability, the recombinant LDHB should be stored at 4°C for short-term use and at -20°C for long-term storage. It is recommended to avoid freeze-thaw cycles to maintain the protein’s integrity . The protein is typically stored in a buffer containing 20 mM Tris-HCl (pH 8.0), 10% glycerol, and 1 mM DTT .

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