Recombinant Human Medium-Chain Specific Acyl-Coa Dehydrogenase, Mitochondrial (ACADM) Protein (His)

Name: Recombinant Human Medium-Chain Specific Acyl-Coa Dehydrogenase, Mitochondrial (ACADM) Protein (His)
Brand: Beta LifeScience
SKU: BLC-09521P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Medium-Chain Specific Acyl-Coa Dehydrogenase, Mitochondrial (ACADM) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P11310
Target Symbol	ACADM
Synonyms	ACAD 1; ACAD1; Acadm; ACADM_HUMAN; Acyl coenzyme A dehydrogenase; Acyl coenzyme A dehydrogenase C 4 to C 12 straight chain; FLJ18227; FLJ93013; FLJ99884; MCAD; MCADH; Medium chain acyl CoA dehydrogenase; Medium chain fatty acyl CoA dehydrogenase ; Medium chain specific acyl CoA dehydrogenase; Medium chain specific acyl CoA dehydrogenase mitochondrial; Medium-chain specific acyl-CoA dehydrogenase; mitochondrial
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	KANRQREPGLGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYKN
Expression Range	26-421aa
Protein Length	Full Length of Mature Protein
Mol. Weight	47.6kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Medium-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA. Electron transfer flavoprotein (ETF) is the electron acceptor that transfers electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase). Among the different mitochondrial acyl-CoA dehydrogenases, medium-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 6 to 12 carbons long primary chains.
Subcellular Location	Mitochondrion matrix.
Protein Families	Acyl-CoA dehydrogenase family
Database References	HGNC: 89 OMIM: 201450 KEGG: hsa:34 STRING: 9606.ENSP00000409612 UniGene: PMID: 27856190 17 VUS (37%; 7 in ACADM, 9 in GALT, and 1 in PAH) were reclassified from uncertain (6 to benign or likely benign and 11 to pathogenic or likely pathogenic). We identified common types of missing information that would have helped make a definitive classification and categorized this information by ease and cost to obtain PMID: 27308838 Subjects with neonatal symptoms, or neonatal abnormal labs, or neonatal triggers were more likely to have at least one copy of the severe c.985A>G ACADM gene mutation PMID: 27477829 Exclusively breastfed neonates with MCAD are at risk for early metabolic decompensation. As breastfeeding rates increase, close management of feeding difficulties is essential for all neonates awaiting newborn screening results PMID: 27148938 The in silico structural changes in medium-chain acyl-CoA dehydrogenase (hMCAD) p.K329E variant protein affect the disturbed oligomeric profile, thermal stability, and conformational flexibility, with respect to the wild-type. PMID: 27976856 LCHAD and MCAD are differentially expressed in maternal and fetal tissues during normal late pregnancy, which may represent a metabolic adaptation in response to physiological maternal dyslipidemia during late pregnancy. PMID: 27871288 Study determined three mutations (p.R53C, p.R281S and p.G362E) in MCAD protein predisposing for MCAD deficiency which seems to be unique to Japanese population. PMID: 26947917 our study demonstrates that not all mutations identified in children with abnormal NBS profiles suggestive of MCAD deficiency result in a total loss in MCAD activity and function PMID: 24966162 The c.600-18G > A variant activates a cryptic splice site, which competes with the natural splice site. PMID: 26223887 mutations in the ACADM gene lower the temperature threshold at which medium-chain acyl-CoA dehydrogenase deficiency loss-of-function occurs. PMID: 24718418 Segregation studies in the Gypsy families showed that 93/123 relatives were carriers of the acyl-coenzyme A dehydrogenase G985 allele, suggesting its high prevalence in this ethnic group. PMID: 23829193 Identify an ACADM founder mutation for MCADD in Saudi Arabian population. PMID: 20567907 This supports that c.1161A>G is a functional SNP, which leads to higher MCAD expression, perhaps due to improved splicing. This study is a proof of principle that synonymous SNPs are not neutral. PMID: 23810226 medium chain acyl-CoA dehydrogenase involve in the metabolism of phenylbutyrate. PMID: 23141465 Subjects with variant ACADM genotypes and residual MCAD enzyme activities <10% should be considered to have the same risks as patients with classical ACADM genotypes PMID: 22630369 The octanoyl-CoA oxidation rate, therefore, allows a risk assessment at birth and the identification of new ACADM genotypes associated with asymptomatic disease variants. PMID: 23028790 A novel variant in the Medium-Chain Acyl-CoA Dehydrogenase (MCAD) gene was identified in a Greek cohort of neonates with suspected MCAD deficiency. PMID: 22683754 physiological concentrations of flavin adenine dinucleotide resulted in a spectacular enhancement of the thermal stabilities of MCADH and prevented enzymatic activity loss PMID: 21968293 The mutation in Medium-chain acyl-CoA dehydrogenase deficiency is the first report of the c.461T>G mutation in the acyl-CoA dehydrogenase gene. PMID: 21239873 classification of genotypes with at least one variant of unknown significance in individuals who are carriers of, or affected with, MCAD deficiency of the following genotypes: c.985A>G/wildtype, c.199T>C/c.985A>G and c.985A>G/c.985A>G PMID: 20434380 MCAD is induced by PGC-1 in an ERRalpha-dependent manner PMID: 12522104 Interference between PPARA and ERRalpha and RXRA complex heterodimer and the nuclear receptor site of MCAD PMID: 12914524 single arginine residue is essential for the binding of electron transferring flavoprotein to MCAD, but the single histidine residue, although involved, is not PMID: 14692513 first molecular identification of MCADD in an Arab patient and the first reported splice mutation in the MCAD gene that has been functionally characterized PMID: 15171999 Two novel rare mutations, R256T and K364R, have been investigated to assess how far the biochemical properties of the mutant proteins correlate with the clinical phenotype of medium chain acyl-CoA dehydrogenase deficiency. PMID: 16128823 analysis of MCAD deficiency (homozygous at c.985A>G (K329E)) complicated by acute liver failure in pregnancy [case report] PMID: 17186412 Measurement of MCAD activity in leukocytes or lymphocytes using phenylpropionyl-CoA as a substrate can be regarded as the gold standard to diagnose MCAD deficiency upon initial positive screening test results. PMID: 18188679 Six novel and seven previously reported medium chain acyl-CoA dehydrogenase mutations were detected in newborns with medium chain acyl-CoA dehydrogenase deficiency. PMID: 18241067 Ethnic-specific homozygous adenin/guanine substitution in an ACADM birth prevalence from a large-scale United Kingdom newborn screening study. PMID: 18927092 study indicates that c.449-452delCTGA represents a common mutation in Japanese patients with medium-chain acyl-CoA dehydrogenase deficiency (MCADD) PMID: 19064330 Protein misfolding of MCAD protein is the molecular basis in medium-chain acyl-CoA dehydrogenase deficiency. PMID: 19224950 In the medium-chain acyl-CoA dehydrogenase, the 985G mutant and 985A normal alleles had allelic frequencies of 0.0020 and 0.9980, respectively. PMID: 19551636 Meta-analysis and HuGE review of genotype prevalence, gene-disease association, gene-gene interaction, and healthcare-related. (HuGE Navigator) PMID: 11263545

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.