LDHB Mouse
L-lactate dehydrogenase B chain, LDH-B, LDH heart subunit, LDH-H, Ldh-2, Ldh2, Ldhb.
Sterile filtered colorless solution.
Greater than 95.0% as determined by SDS-PAGE.
Description
LDHB Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-334 a.a) and having a molecular mass of 39kDa.
LDHB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
L-lactate dehydrogenase B chain, LDH-B, LDH heart subunit, LDH-H, Ldh-2, Ldh2, Ldhb.
MGSSHHHHHH SSGLVPRGSH MGSMATLKEK LIASVADDEA AVPNNKITVV GVGQVGMACA ISILGKSLAD ELALVDVLED KLKGEMMDLQ HGSLFLQTPK IVADKDYSVT ANSKIVVVTA GVRQQEGESR LNLVQRNVNV FKFIIPQIVK YSPDCTIIVV SNPVDILTYV TWKLSGLPKH RVIGSGCNLD SARFRYLMAE KLGIHPSSCH GWILGEHGDS SVAVWSGVNV AGVSLQELNP EMGTDNDSEN WKEVHKMVVD SAYEVIKLKG YTNWAIGLSV ADLIESMLKN LSRIHPVSTM VKGMYGIENE VFLSLPCILN ARGLTSVINQ KLKDDEVAQL RKSADTLWDI QKDLKDL.
Product Science Overview
Lactate Dehydrogenase B (LDH-B) is an enzyme that plays a crucial role in the metabolic pathway of glycolysis. It is one of the isoforms of lactate dehydrogenase, which catalyzes the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+. The recombinant form of LDH-B from mice is often used in research to study its structure, function, and role in various biological processes.
LDH-B is a protein encoded by the Ldhb gene in mice. The enzyme is composed of 334 amino acids and has a molecular weight of approximately 36 kDa. It is expressed in various tissues, with high levels found in the heart and skeletal muscles. The enzyme operates as a tetramer, with each subunit contributing to the overall catalytic activity.
The primary function of LDH-B is to catalyze the conversion of L-lactate to pyruvate, a key step in anaerobic glycolysis. This reaction is crucial for maintaining the balance of NADH and NAD+ in cells, which is essential for various metabolic processes. The enzyme’s activity is regulated by several factors, including substrate availability, pH, and the presence of inhibitors or activators.
Recombinant LDH-B from mice is typically produced using Escherichia coli (E. coli) expression systems. The gene encoding LDH-B is cloned into a suitable expression vector, which is then introduced into E. coli cells. The bacteria are cultured under conditions that promote the expression of the recombinant protein. After expression, the protein is purified using techniques such as affinity chromatography to achieve high purity levels (>95%) and low endotoxin levels (<1 EU/µg) .
Recombinant LDH-B is widely used in biochemical and physiological research. Some of its key applications include:
- Enzyme Kinetics: Studying the catalytic properties and kinetics of LDH-B to understand its role in metabolic pathways.
- Drug Screening: Evaluating potential inhibitors or activators of LDH-B as therapeutic agents for conditions related to metabolic dysregulation.
- Structural Biology: Investigating the three-dimensional structure of LDH-B to gain insights into its function and interaction with other molecules.
- Disease Models: Using recombinant LDH-B to study its involvement in diseases such as cancer, where altered metabolism is a hallmark.
