Anti-LDHB (C-terminal half) polyclonal antibody

Rabbit Anti-Human LDHB polyclonal antibody for WB, IHC-P. L-lactate dehydrogenase B chain (EC 1.1.1.27; UniProt P07195; also known as Epididymis secretory protein Li 281, Lactate dehydrogenase H chain, LDH-B, LDH-H, LDH heart subunit, Renal carcinoma antigen NY-REN-46) is encoded by the LDHB (also known as LDHBD, TRG-5, HEL-S-281) gene (Gene ID 3945) in human. Originally described by Otto Warburg and now commonly known as the Warburg effect refers to the phenomenon that many tumor cells use aerobic glycolysis instead of mitochondrial respiration for energy production to support cell growth and proliferation. Enzymes involved in the complex network of metabolic pathways are therefore being studied as potential targets for cancer treatment. Lactate dehydrogenase (LDH) is a tetrameric enzyme composed of two different subunits, LDHA and LDHB, which can assemble into five different combinations (LDH1 is comprised of four LDHB subunits; LDH2 contains three LDHB and one LDHA subunit; LDH3 contains two LDHB and two LDHA subunits; LDH4 contains one LDHB and three LDHA subunits; LDH5 contains four LDHA subunits). LDHB is ubiquitously expressed and the predominant isoform in heart muscle, while LDHA is the predominant isoform in skeletal muscle and other highly glycolytic tissues. LDH catalyzes the reversible conversion of pyruvate into lactate. An upregulation of LDH therefore reduces the oxygen dependency and ensures an efficient anaerobic/glycolytic metabolism in tumor cells. Serum LDHB levels, for example, are reported to elevate in lung cancer patients and progressively increase with the clinical stage of non-small cell lung cancer (NSCLC).

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