Native Human Lactate Dehydrogenase 5

Molecule:

LDH5

Synonyms:

Lactate dehydrogenase 5, LDH-5, LD-5 Isoenzyme, LDH-5 Isoenzyme, 4M Isoenzyme

Species:

Human

Cat. No.:

CSI19687B pdf (datasheet)

Quantity/Size:

1,000 U

Description:

Lactate Dehydrogenase (LDH) catalyses the conversion of L-lactate and NAD+ to pyruvate and NADH in the final step of anaerobic glycolysis. Enzymatically active lactate dehydrogenase consists of four subunits (tetramer). The two most common subunits are the LDH-M and LDH-H peptides, named for their discovery in muscle and heart tissue, and encoded by the LDHA and LDHB genes, respectively. These two subunits can form five possible tetramers (isoenzymes): LDH-1 (4H), LDH-5 (4M), and the three mixed tetramers (LDH-2/3H1M, LDH-3/2H2M, LDH-4/1H3M). These five isoforms are enzymatically similar but show different tissue distribution. LDH-1 (heart), LDH-2 (reticuloendothelial system), LDH-3 (lung), LDH-4 (kidneys), and LDH-5 (liver and striated muscles). LDH-5 is believed to be an excellent indicator of active liver damage.

Concentration:

≥ 1.0 mg/mL (Coomassie)

CAS No:

9001-60-9

Data PDF:

CSI19687

Source:

Human liver

Formulation:

Liquid suspension in 3.1 M ammonium sulfate, 20 mM TRIS-chloride, 1 mM DTT, 1 mM EDTA, pH 8.3

Purity:

LDH-5: > 95% (Helena QuickGel® LD Isoenzyme Electrophoresis)

Biological Activity:

> 1,000 U/ml (Dimension Clinical Chemistry System) One unit will catalyze the oxidation of one micromole of L-lactate to pyruvate with simultaneous reduction of NAD+ to NADH per minute at 37°C and pH 9.4.

Specific Activity:

> 250 U/mg

Storage/Stability:

Store at 2-8 °C for at least 1 year. DO NOT FREEZE