LDHA, E.Coli Active
Escherichia Coli.
LDH-A, GSD11, LDH1, LDHM, PIG19, EC 1.1.1.27, lactate dehydrogenase M, LDH-M, LDH-1, L-lactate dehydrogenase A chain, LDH muscle subunit, Renal carcinoma antigen NY-REN-59, Cell proliferation-inducing gene 19 protein, LDHA.
Greater than 95.0% as determined by SDS-PAGE.
Description
LDHA E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (1-329) and having a molecular mass of 39.1 kDa.
LDHA E.Coli is fused to a 24 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
D-lactate dehydrogenase, also known as ldhA, is an enzyme belonging to the D-lactate dehydrogenase protein family. IDHA, a cytochrome, enhances the catalytic activity of ldhA. This enzyme uses two substrates, (D)-lactate and ferricytochrome c, to produce two end products: pyruvate and ferrocytochrome c.
Recombinant LDHA from E.Coli is a single, non-glycosylated polypeptide chain. It consists of 353 amino acids (amino acids 1-329) and has a molecular weight of 39.1 kDa.
This LDHA protein is fused to a 24 amino acid His-Tag at its N-terminus and is purified using proprietary chromatographic techniques.
LDHA E.Coli protein solution (1mg/ml) is supplied in a buffer of 20mM Tris-HCl (pH 8.0), 100mM NaCl, and 10% glycerol.
For extended storage, it is advisable to supplement with a carrier protein (0.1% HSA or BSA).
Minimize repeated freezing and thawing.
Purity is confirmed to be greater than 95.0% based on SDS-PAGE analysis.
Specific activity exceeds 200 units/mg. One unit is defined as the amount of enzyme that catalyzes the conversion of 1.0 umole of pyruvate to L-lactate and beta-NAD per minute at a pH of 7.5 and a temperature of 37 degrees Celsius.
LDH-A, GSD11, LDH1, LDHM, PIG19, EC 1.1.1.27, lactate dehydrogenase M, LDH-M, LDH-1, L-lactate dehydrogenase A chain, LDH muscle subunit, Renal carcinoma antigen NY-REN-59, Cell proliferation-inducing gene 19 protein, LDHA.
Escherichia Coli.
MGSSHHHHHH SSGLVPRGSH MGSHMKLAVY STKQYDKKYL QQVNESFGFE LEFFDFLLTE KTAKTANGCE AVCIFVNDDG SRPVLEELKK HGVKYIALRC AGFNNVDLDA AKELGLKVVR VPAYDPEAVA EHAIGMMMTL NRRIHRAYQR TRDANFSLEG LTGFTMYGKT AGVIGTGKIG VAMLRILKGF GMRLLAFDPY PSAAALELGV EYVDLPTLFS ESDVISLHCP LTPENYHLLN EAAFEQMKNG VMIVNTSRGA LIDSQAAIEA LKNQKIGSLG MDVYENERDL FFEDKSNDVI QDDVFRRLSA CHNVLFTGHQ AFLTAEALTS ISQTTLQNLS NLEKGETCPN ELV
Product Science Overview
Lactate Dehydrogenase A (LDHA) is a crucial enzyme involved in the metabolic pathway of glycolysis. It catalyzes the conversion of pyruvate to lactate while simultaneously oxidizing NADH to NAD+. This reaction is vital for anaerobic respiration, allowing cells to generate energy in the absence of oxygen. LDHA is particularly important in tissues that rely heavily on anaerobic glycolysis, such as muscle tissue.
LDHA is a member of the lactate dehydrogenase family, which includes several isoforms. The enzyme is a tetramer composed of four subunits, each with a molecular weight of approximately 36-39 kDa . The active site of LDHA binds to pyruvate and NADH, facilitating the transfer of electrons and the subsequent reduction of pyruvate to lactate.
Recombinant LDHA is produced using the bacterium Escherichia coli (E. coli) as a host organism. This method involves inserting the gene encoding LDHA into the E. coli genome, allowing the bacteria to express the enzyme. The recombinant protein is then purified using various chromatographic techniques to achieve high purity and bioactivity .
Recombinant LDHA has several applications in research and biotechnology:
- Biochemical Studies: It is used to study the enzyme’s kinetics, structure, and function.
- Drug Development: LDHA inhibitors are being explored as potential treatments for cancer, as cancer cells often rely on anaerobic glycolysis for energy production.
- Diagnostic Assays: LDHA levels are measured in clinical settings to diagnose and monitor conditions such as myocardial infarction, liver disease, and certain cancers.
The bioactivity of recombinant LDHA is measured by its ability to catalyze the reduction of pyruvate to lactate. Specific activity is typically reported in units per milligram of protein, with one unit defined as the amount of enzyme that converts one micromole of pyruvate to lactate per minute at a given pH and temperature . Recombinant LDHA is often supplied with a His-tag to facilitate purification and is stored under conditions that maintain its stability and activity .
