Product Pathways - Metabolism
Phospho-LDHA (Tyr10) Antibody #8176
|W||H M R||Endogenous||37||Rabbit|
Reactivity Key: H=Human M=Mouse R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
Phospho-LDHA (Tyr10) Antibody recognizes endogenous levels of LDHA protein only when phosphorylated at Tyr10.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Tyr10 of human LDHA protein. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from various cell lines using Phospho-LDHA (Tyr10) Antibody.
Western blot analysis of extracts from 293T cells transfected with a construct expressing DYKDDDDK-tagged wild-type (WT) full-length human LDHA (WT hLDHA-DDK) alone or in conjuction with full-length human FGFR1 (hFGFR1), using Phospho-LDHA (Tyr10) Antibody (upper) or DYKDDDDK Tag (9A3) Mouse mAb #8146 (lower). The DYKDDDDK-tagged WT hLDHA expression construct was kindly provided by Dr. Jing Chen at Emory University School of Medicine.
Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and NADH to lactate and NAD+. When the oxygen supply is too low for mitochondrial ATP production, this reaction recycles NADH generated in glycolysis to NAD+, which reenters glycolysis. The major form of LDH found in muscle cells is the A (LDHA) isozyme. The LDHA promoter contains HIF-1α binding sites (1). LDHA expression is induced under hypoxic conditions (2). During intensive and prolonged muscle exercise, lactate accumulates in muscle cells when the supply of oxygen does not meet demand. When oxygen levels return to normal, LDH converts lactate to pyruvate to generate ATP in the mitochondrial electron transport chain.
Recent studies indicate that LDHA is phosphorylated at Tyr10 and Tyr83 by the receptor tyrosine kinase FGFR1 (3). Phosphorylation at Tyr10 up-regulates the activity of LDHA and is found in a variety of human cancer cells (3). Results further suggest that tyrosine phosphorylation regulates the NADH/NAD+ redox homeostasis and thus promotes the Warburg effect and tumor cell growth (3).
- Semenza, G.L. et al. (1996) J Biol Chem 271, 32529-37.
- Semenza, G.L. (2007) Biochem J 405, 1-9.
- Fan, J. et al. (2011) Mol Cell Biol 31, 4938-50.
- Fan, J. et al. (2011) Mol Cell Biol 31, 4938-50. Applications: Western Blotting
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For Research Use Only. Not For Use In Diagnostic Procedures.