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The protein encoded by LDHA catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis. Additionally we are shipping Lactate Dehydrogenase A Antibodies (273) and Lactate Dehydrogenase A Proteins (58) and many more products for this protein.
Showing 9 out of 42 products:
hCINAP determines self-renewal of colorectal cancer stem cells by facilitating LDHA phosphorylation.
the results of the present study demonstrated that miR199a3p can inhibit LDHA expression by downregulating Sp1 (show PSG1 ELISA Kits), and provided mechanistic evidence supporting the existence of a novel miR199a3p/Sp1 (show PSG1 ELISA Kits)/LDHA axis and its critical contribution to aerobic glycolysis in testicular cancer cells.
High LDHA expression is associated with Non-Small Cell Lung Cancer.
This is the first study from this highly prevalent region of Head neck cancer showing that serum LDH could be regarded as a biomarker for malignant and premalignant conditions of the head and neck.
High LDH expression is associated with small cell lung cancer.
The PFK2 expression along with LDH-4 were observed to be increased ~2-fold (P < 0.001) in 0.5 mM ammonia treated brain slices.
miR (show MLXIP ELISA Kits)-199a-3p is a major metabolic regulator in tumor suppression and miR (show MLXIP ELISA Kits)-199a-3p may downregulate metabolic genes (LDHA, PGK1 (show PGK1 ELISA Kits), MCT1 (show CMA1 ELISA Kits), TIGAR) through the transcription factor Sp1 (show SP1 ELISA Kits).
The expression of LDH (show LLDH ELISA Kits)-5 and hypoxia-inducible factor (HIF) 1alpha (show HIF1A ELISA Kits) in Non-Hodgkin's lymphoma, was examined.
Results show that LDHA is highly expressed in triple negative breast cancer (TNBC) and correlated with a poor outcome. Its 3'UTR is targeted by miR-34a. Also, LDHA along with PDL1 seem to act as ceRNAs to promote the expression and function of each other through regulation of miR-34a in TNBC.
LDHA siRNA can inhibit cell proliferation, induce apoptosis, reduce invasion and migration in renal cell carcinoma (show MOK ELISA Kits) cells.
Dynamic changes of LDH and HBDH activities may be useful in diagnosis of non-thermal low voltage electrical injury and in estimation of post injury intervals.
The release of lactate dehydrogenase A (LDHA) from degenerating neurons drives central nervous system (CNS) angiogenesis.
Hair follicle stem cells maintain a metabolic state that allows them to remain dormant and yet quickly respond to appropriate proliferative stimuli mediated by LDH-A signaling.
Results revealed that beta-arrestin-1 (show ARRB1 ELISA Kits) regulates lactate metabolism to contribute to beta2-adrenergic receptor (show ADRB2 ELISA Kits) functions in improved memory formation.
The authors identified lactate dehydrogenase (LDH) as a new functional target of AMPKalpha1.
LDHA-associated lactic acid accumulation in melanomas inhibits tumor surveillance by T and natural killer cells.
lactate dehydrogenase A (LDHA) is induced in activated T cells to support aerobic glycolysis but promotes IFN-gamma (show IFNG ELISA Kits) expression independently of its 3'UTR (show UTS2R ELISA Kits).
LDHA is a direct target of miR-34a in regulating glucose metabolism and tumor growth in breast cancer.
Findings suggest that RANKL protein-induced lactate dehydrogenase (LDH) activation stimulates glycolytic and mitochondrial respiratory metabolism via transcription factor NFATc1 signaling.
We propose a profibrotic feed forward loop, in which radiation induces LDHA expression and lactate production, which can lead to further activation of TGF-beta (show TGFB1 ELISA Kits) to drive the fibrotic process.
High LDH-A expression is associated with metastases in breast tumors.
These findings indicated that heat shock (HS)-induced autophagy regulates lactate secretion by inhibiting apoptosis and increasing mRNA transcript and protein levels of SLC2A3 (show SLC2A3 ELISA Kits), LDHA, and SLC16A1 (show SLC16A1 ELISA Kits), which suggests that HS-induced autophagy may enhance lactate secretion by sertoli cells.
The NADH-cofactor binding site of pig heart LDH is involved in the interaction with acidic phospholipids, in the pig skeletal muscle LDH, neither the cofactor binding site nor the subunit interfacing areas seem to be involved in the interaction.
Both LDHA and COPB1 were highly expressed in porcine skeletal muscle tissues, implying their potential regulatory function of muscle development.
Molecular characterization and expression pattern of the equine lactate dehydrogenase A genes
The protein encoded by this gene catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis. The protein is found predominantly in muscle tissue and belongs to the lactate dehydrogenase family. Mutations in this gene have been linked to exertional myoglobinuria. Multiple transcript variants encoding different isoforms have been found for this gene. The human genome contains several non-transcribed pseudogenes of this gene.
L-lactate dehydrogenase A chain
, LDH muscle subunit
, cell proliferation-inducing gene 19 protein
, lactate dehydrogenase M
, proliferation-inducing gene 19
, renal carcinoma antigen NY-REN-59
, lactate dehydrogenase-M
, lactate dehydrogenase A
, lactate dehydrogenase 1, A chain
, lactate dehydrogenase A4
, lactate dehydrogenase-A
, lactate dehydrogenase A-like
, lactate dehydrogenase A1
, lactate dehydrogenase C
, L-lactic acid dehydrogenase
, M(A)-type lactate dehydrogenase