Lactate dehydrogenase (LDH, EC1.1.1.27) is a glycolytic enzyme composed of four subunits with molecular weight of 130-140KDa. It exists in the cytoplasm of all tissues and cells in the body, and the content of kidney is higher. There are six forms of LDH isoenzyme, which can be separated by electrophoresis, and its distribution has obvious tissue specificity. LDH can catalyze the reversible transformation of pyruvate and lactate. It is an important enzyme involved in the anaerobic glycolysis and gluconeogenesis. The normal range of LDH in human serum is 135-215u / L. when endocrine disorders or overworked, LDH is easy to be low, which can be repaired after conditioning; the high level of LDH is due to pleural and ascites caused by pulmonary infarction, malignant anemia, shock and tumor metastasis, which is more serious.

LDH is one of the most widely used enzymes in the diagnosis of myocardial infarction, acute liver injury, liver cancer, lung cancer and leukemia. LDH catalyzes the reaction between pyruvate and NADH, which makes the absorbance of reaction solution change at 340nm, so as to achieve the detection purpose.

Our company's LDH is a recombinant product of type D gene, with high purity and good activity.

[Product Description]

Dosage form: white freeze-dried powder, or liquid

Preservation buffer: Tris-cl buffer, pH7.5

Enzyme activity: ≥ 200U/mg

Activity unit: the amount of enzyme required to consume 1 umol of NADH per minute at pH7.5 and 37 ℃, which is 1 unit.

essential information:

Source: gene recombinant expression

Molecular weight: 40kDa (SDS-PAGE detection)

purity: ≥ 90% (SDS-PAGE detection)

Storage conditions: freeze dried powder at 4 ℃ or a long time at - 20 ℃

Transportation conditions: ice bag with low temperature

Safety tips: it is strictly prohibited to use for human experiments