Browse our anti-MLYCD (MLYCD) Antibodies

Full name:
anti-Malonyl CoA Decarboxylase Antibodies (MLYCD)
On www.antibodies-online.com are 14 Malonyl CoA Decarboxylase (MLYCD) Antibodies from 7 different suppliers available. Additionally we are shipping MLYCD Proteins (5) and MLYCD Kits (4) and many more products for this protein. A total of 25 MLYCD products are currently listed.
Synonyms:
AI324784, Mcd
list all antibodies Gene Name GeneID UniProt
MLYCD 23417 O95822
MLYCD 56690 Q99J39
MLYCD 85239 Q920F5

Show all species

Show all synonyms

Most Popular Reactivities for anti-MLYCD (MLYCD) Antibodies

Select your species and application

anti-Human MLYCD Antibodies:

anti-Mouse (Murine) MLYCD Antibodies:

anti-Rat (Rattus) MLYCD Antibodies:

All available anti-MLYCD Antibodies

Go to our pre-filtered search.

Top referenced anti-MLYCD Antibodies

  1. Human Polyclonal MLYCD Primary Antibody for WB - ABIN525162 : Kulkarni, Salehzadeh, Fritz, Zierath, Krook, Osler: Mitochondrial regulators of fatty acid metabolism reflect metabolic dysfunction in type 2 diabetes mellitus. in Metabolism: clinical and experimental 2012 (PubMed)

More Antibodies against MLYCD Interaction Partners

Human Malonyl CoA Decarboxylase (MLYCD) interaction partners

  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.

  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.

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

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

  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.

  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

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

  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.

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

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

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

  1. Decreased fat oxidation in MCD(-/-) mice resulted in the accumulation of lipid intermediates in peripheral tissues, but this was not associated with a worsening of age-associated insulin (show INS Antibodies) resistance and, conversely, improved longevity.

  2. 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.

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

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

  5. 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

  6. 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.

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

MLYCD Antigen Profile

Antigen 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.

Alternative names and synonyms associated with MLYCD

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

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
Selected quality suppliers for anti-MLYCD (MLYCD) Antibodies
Did you look for something else?