Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
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 (249) and Lactate Dehydrogenase A Proteins (56) and many more products for this protein.
Showing 10 out of 33 products:
Molecular characterization and expression pattern of the equine lactate dehydrogenase A genes
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.
LDHA phosphorylation and activation provide pro-invasive, anti-anoikis and pro-metastatic advantages to cancer cells, suggesting that Y10 phosphorylation of LDHA may represent a promising therapeutic target and a prognostic marker for metastatic human cancers.
miR (show MLXIP ELISA Kits)-30a-5p may function as a tumor suppressor in breast cancer through the inhibition of LDHA expression and glycolysis.
Overexpression of LDHA can be a marker of poor prognosis in cholangiocarcinoma patients
LDHA-associated lactic acid accumulation in melanomas inhibits tumor surveillance by T and natural killer cells.
Data indicate that lactate dehydrogenase A (LDHA) is involved in the transcription of histone 2B gene.
LDHA downregulation is involved in the apoptotic effect of diallyl trisulfide in triple-negative breast cancer.
this study shows that low levels of LDH correlate to a better anti-CTLA-4 (show CTLA4 ELISA Kits) immunotherapy response and survival in advanced melanoma patients
alternative isoforms of LDH in cancer cells produce lactic acid, when LDHA is silenced or inhibited
Overexpression of PKM2 and LDH5 associates with key clinicopathological features and unfavourable prognosis in tongue squamous cell carcinoma.
These results suggest LDH-A and/or lactate as common elements at the cross-road between cancer cell metabolism, tumor progression and inflammation
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.
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 (show MLXIP ELISA Kits)-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.
PGC-1alpha (show PPARGC1A ELISA Kits) reduces the expression of LDH A and one of its regulators, the transcription factor myelocytomatosis oncogene (show MYC ELISA Kits).
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 (show COPB1 ELISA Kits) were highly expressed in porcine skeletal muscle tissues, implying their potential regulatory function of muscle development.
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.
lactate dehydrogenase A1
, L-lactate dehydrogenase A chain
, LDH muscle subunit
, lactate dehydrogenase C
, lactate dehydrogenase-A
, L-lactic acid dehydrogenase
, lactate dehydrogenase A
, M(A)-type lactate dehydrogenase
, lactate dehydrogenase-M
, cell proliferation-inducing gene 19 protein
, lactate dehydrogenase M
, proliferation-inducing gene 19
, renal carcinoma antigen NY-REN-59
, lactate dehydrogenase 1, A chain
, lactate dehydrogenase A4
, lactate dehydrogenase A-like