Product Details

Purity

Greater than 90% as determined by SDS-PAGE.

Target Names

MLYCD

Uniprot No.

O95822

Research Area

others

Alternative Names

DCMC_HUMAN; hMCD; Malonyl CoA decarboxylase; Malonyl CoA decarboxylase mitochondrial; Malonyl coenzyme A decarboxylase; Malonyl-CoA decarboxylase; MCD; MGC59795; mitochondrial; Mlycd

Species

Homo sapiens (Human)

Source

E.coli

Expression Region

40-493aa

Target Protein Sequence

MDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAETAQRAELLGRLARGFGVDHGQVAEQSAGVLHLRQQQREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPDVREMNGVLKGMLSEWFSSGFLNLERVTWHSPCEVLQKISEAEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGEPLVVLHVALTGDISSNIQAIVKEHPPSETEEKNKITAAIFYSISLTQQGLQGVELGTFLIKRVVKELQREFPHLGVFSSLSPIPGFTKWLLGLLNSQTKEHGRNELFTDSECKEISEITGGPINETLKLLLSSSEWVQSEKLVRALQTPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVLWRINWMADVSLRGITGSCGLMANYRYFLEETGPNSTSYLGSKIIKASEQVLSLVAQFQKNSKL
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.

Mol. Weight

55.9kDa

Protein Length

Full Length of Mature Protein

Tag Info

N-terminal 10xHis-tagged and C-terminal Myc-tagged

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer

Tris-based buffer,50% glycerol

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

3-7 business days

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Description

Amino acids 40-493 form the expressed segment for recombinant Human MLYCD. The calculated molecular weight for this MLYCD protein is 55.9 kDa. This MLYCD protein is produced using e.coli expression system. The MLYCD gene fragment has been modified by fusing the N-terminal 10xHis tag and C-terminal Myc tag, providing convenience in detecting and purifying the recombinant MLYCD protein during the following stages.

Human malonyl-CoA decarboxylase (MLYCD) is a mitochondrial enzyme that catalyzes the conversion of malonyl-CoA to acetyl-CoA and carbon dioxide, playing a crucial role in fatty acid metabolism. By reducing malonyl-CoA levels, MLYCD alleviates its inhibitory effect on carnitine palmitoyltransferase 1 (CPT1), thus promoting fatty acid oxidation and mitochondrial energy production. MLYCD deficiency leads to the accumulation of malonyl-CoA, impairing fatty acid oxidation and causing symptoms such as cardiomyopathy, skeletal myopathy, and developmental delay. Research on MLYCD spans various areas, including lipid metabolism, mitochondrial function, and metabolic disorders, aiming to elucidate its role in health and disease and develop potential therapeutic strategies.

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

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
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
The MLYCD catalytic domain is structurally homologous to those of the GCN5-related N-acetyltransferase superfamily. PMID: 23791943
Structural asymmetry and disulfide bridges among subunits modulate the activity of human malonyl-CoA decarboxylase. PMID: 23482565
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
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
Malonyl-CoA decarboxylase deficiency may result from MLYCD mutations that result in protein mistargeting. PMID: 12955715
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
analysis of nine novel MLYCD mutations in patients with malonyl-coenzyme A decarboxylase deficiency PMID: 17186413
MCD silencing suppresses lipid uptake and enhances glucose uptake in primary human myotubes. PMID: 18314420
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

Hide All

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

Place an order now

I. Product details

Product name *

Code *

Size *

Quantity *

Message

II. Contact details

Name *

Email address *

Company/Organization

Phone

III. Ship To

Address *

City *

State/Province *

Zip/Post code *

Country *

Attn Name *

Phone# *

IV. Bill To Same as Shipping Address

Address *

City *

State/Province *

Zip/Post code *

Country *

Attn Name *

Phone# *

CAPTCHA verification *

Code	CSB-EP014646HU
MSDS	MSDS
Size	US$256
	Order now
Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel. Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP014646HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) O95822. Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP014646HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) O95822.
Have Questions?	Leave a Message or Start an on-line Chat

Recombinant Human Malonyl-CoA decarboxylase, mitochondrial (MLYCD)

Product Details

Related Products

Customer Reviews and Q&A

Target Background

×CloseMessage