MLYCD Antibody

Code CSB-PA014646GA01HU
Size $600
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Product Details

Uniprot No.
Target Names
MLYCD
Alternative Names
DCMC_HUMAN antibody; hMCD antibody; Malonyl CoA decarboxylase antibody; Malonyl CoA decarboxylase mitochondrial antibody; Malonyl coenzyme A decarboxylase antibody; Malonyl-CoA decarboxylase antibody; MCD antibody; MGC59795 antibody; mitochondrial antibody; Mlycd antibody
Raised in
Rabbit
Species Reactivity
Human,Mouse,Rat
Immunogen
Human MLYCD
Immunogen Species
Homo sapiens (Human)
Isotype
IgG
Purification Method
Antigen Affinity purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
PBS with 0.02% Sodium Azide, 50% Glycerol, pH 7.3. -20°C, Avoid freeze / thaw cycles.
Tested Applications
ELISA,WB,IHC
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

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Target Background

Function
Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids. Plays a role in the metabolic balance between glucose and lipid oxidation in muscle independent of alterations in insulin signaling. May play a role in controlling the extent of ischemic injury by promoting glucose oxidation.
Gene References into Functions
  1. To identify the active site of MCD, molecular docking and molecular dynamics simulations were performed to explore the interactions of human mitochondrial MCD (HmMCD) and CoA derivatives. The findings reveal that the active site of HmMCD indeed resides in the prominent groove which resembles that of curacin A. PMID: 26948533
  2. Our result expands the phenotype of malonyl-CoA decarboxylase deficiency and suggests attentions should be paid to the mild form of disorders, for example, malonyl-CoA decarboxylase deficiency, which usually present a severe disease course. PMID: 26858006
  3. The MLYCD catalytic domain is structurally homologous to those of the GCN5-related N-acetyltransferase superfamily. PMID: 23791943
  4. Structural asymmetry and disulfide bridges among subunits modulate the activity of human malonyl-CoA decarboxylase. PMID: 23482565
  5. Our case emphasizes the need for ongoing cardiac disease screening in patients with MCD deficiency and the benefits and limitations of current dietary interventions. PMID: 22778304
  6. This study of fatty acid oxidation and malonyl-CoA decarboxylase identifies a critical role for metabolism in both the normal pulmonary circulation (hypoxic pulmonary vasoconstriction) and pulmonary hypertension PMID: 20702857
  7. Malonyl-CoA decarboxylase deficiency may result from MLYCD mutations that result in protein mistargeting. PMID: 12955715
  8. The concentration of malonyl-CoA is diminished in muscle after physical training, most likely because of PGC-1alpha-mediated increases in MCD expression and activity. PMID: 16434556
  9. analysis of nine novel MLYCD mutations in patients with malonyl-coenzyme A decarboxylase deficiency PMID: 17186413
  10. MCD silencing suppresses lipid uptake and enhances glucose uptake in primary human myotubes. PMID: 18314420
  11. Data suggest that increased expression of malonyl CoA decarboxylase, and the decreased expression of acetyl CoA carboxylase and 5'-AMP activated protein kinase are important regulators of the maturation of fatty acid oxidation in the newborn human heart. PMID: 18614968

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Involvement in disease
Malonyl-CoA decarboxylase deficiency (MLYCD deficiency)
Subcellular Location
Cytoplasm. Mitochondrion matrix. Peroxisome. Peroxisome matrix.
Tissue Specificity
Expressed in fibroblasts and hepatoblastoma cells (at protein level). Expressed strongly in heart, liver, skeletal muscle, kidney and pancreas. Expressed in myotubes. Expressed weakly in brain, placenta, spleen, thymus, testis, ovary and small intestine.
Database Links

HGNC: 7150

OMIM: 248360

KEGG: hsa:23417

STRING: 9606.ENSP00000262430

UniGene: Hs.644610

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