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Malonyl CoA Decarboxylase Proteins (MLYCD)

The product of MLYCD catalyzes the breakdown of malonyl-CoA to acetyl-CoA and carbon dioxide. Additionally we are shipping MLYCD Antibodies (14) and MLYCD Kits (4) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
MLYCD 23417 O95822
MLYCD 56690 Q99J39
Rat MLYCD MLYCD 85239 Q920F5
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Top MLYCD Proteins at antibodies-online.com

Showing 4 out of 4 products:

Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price Details
HOST_Escherichia coli (E. coli) Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 29 to 34 Days
$4,331.68
Details
HOST_Escherichia coli (E. coli) Mouse His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 29 to 34 Days
$4,331.68
Details
HOST_Wheat germ Human GST tag 10 μg Log in to see 9 Days
$405.71
Details
HOST_Human Human Un-conjugated   20 μg Log in to see 9 to 11 Days
$785.40
Details

MLYCD Proteins by Origin and Source

Origin Expressed in Conjugate
Human , ,
,
Mouse (Murine)

More Proteins for Malonyl CoA Decarboxylase (MLYCD) Interaction Partners

Human Malonyl CoA Decarboxylase (MLYCD) interaction partners

  1. The MLYCD catalytic domain is structurally homologous to those of the GCN5-related N-acetyltransferase superfamily.

  2. Structural asymmetry and disulfide bridges among subunits modulate the activity of human malonyl-CoA decarboxylase.

  3. Our case emphasizes the need for ongoing cardiac disease screening in patients with MCD deficiency and the benefits and limitations of current dietary interventions.

  4. 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

  5. Malonyl-CoA decarboxylase deficiency may result from MLYCD mutations that result in protein mistargeting.

  6. 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.

  7. analysis of nine novel MLYCD mutations in patients with malonyl-coenzyme A decarboxylase deficiency

  8. MCD silencing suppresses lipid uptake and enhances glucose uptake in primary human myotubes.

  9. Data suggest that increased expression of malonyl CoA decarboxylase, and the decreased expression of acetyl CoA carboxylase and 5'-AMP activated protein kinase (show PRKAA2 Proteins) are important regulators of the maturation of fatty acid oxidation in the newborn human heart.

Mouse (Murine) Malonyl CoA Decarboxylase (MLYCD) interaction partners

  1. MCD(-/-) mice consistently exhibited cardiac dysfunction and severe metabolic perturbations while on a high-fat, low carbohydrate diet of maternal milk and these gradually resolved post-weaning.

  2. Data indicate that a full-dosage of p53 (show TP53 Proteins) and an intact ribosomal protein-murine double minute 2 protein (Mdm2 (show MDM2 Proteins))-p53 (show TP53 Proteins) pathway are required for the induction of malonyl coA decarboxylase (MCD), a critical regulator of fatty acid oxidation.

  3. SIRT4 deacetylates and represses malonyl CoA decarboxylase, regulating malonyl coA levels.

  4. 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

  5. In vivo and ex vivo cardiac function is similar in wild-type and mcd-deficient mice; however, deletion of MCD markedly increases glucose oxidation and improves functional recovery of the heart after ischemia.

  6. Mcd deficiency is not detrimental to the heart in obesity in mice.

MLYCD Protein Profile

Protein Summary

The product of this gene catalyzes the breakdown of malonyl-CoA to acetyl-CoA and carbon dioxide. Malonyl-CoA is an intermediate in fatty acid biosynthesis, and also inhibits the transport of fatty acyl CoAs into mitochondria. Consequently, the encoded protein acts to increase the rate of fatty acid oxidation. It is found in mitochondria, peroxisomes, and the cytoplasm. Mutations in this gene result in malonyl-CoA decarboyxlase deficiency.

Gene names and symbols associated with MLYCD

  • MaLonyl CoA Decarboxylase (mlcd-1)
  • malonyl-CoA decarboxylase (MLYCD)
  • malonyl-CoA decarboxylase (Mlycd)
  • AI324784 protein
  • Mcd protein

Protein level used designations for MLYCD

MaLonyl CoA Decarboxylase family member (mlcd-1) , malonyl coenzyme A decarboxylase , malonyl-CoA decarboxylase, mitochondrial

GENE ID SPECIES
175597 Caenorhabditis elegans
23417 Homo sapiens
56690 Mus musculus
85239 Rattus norvegicus
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