Render Target: STATIC
Render Timestamp: 2024-11-04T10:36:13.047Z
Commit: 23cb9f61fe67e1e9093fd644a533c4ff516a6463
XML generation date: 2024-09-20 06:18:47.886
Product last modified at: 2024-05-30T07:08:01.248Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-LDHA (Tyr10) Antibody #8176

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  • WB

Inquiry Info. # 8176

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    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 37
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Phospho-LDHA (Tyr10) Antibody recognizes endogenous levels of LDHA protein only when phosphorylated at Tyr10.

    Species Reactivity:

    Human, Mouse, Rat

    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.

    Background

    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).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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