Recombinant Human Methylmalonyl-Coa Mutase, Mitochondrial (MMUT) Protein (His)

Name: Recombinant Human Methylmalonyl-Coa Mutase, Mitochondrial (MMUT) Protein (His)
Brand: Beta LifeScience
SKU: BLC-02883P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human Methylmalonyl-Coa Mutase, Mitochondrial (MMUT) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P22033
Target Symbol	MMUT
Synonyms	MCM; Methylmalonyl CoA isomerase ; Methylmalonyl CoA mutase mitochondrial; Methylmalonyl Coenzyme A mutase; Methylmalonyl-CoA isomerase; Methylmalonyl-CoA mutase; mitochondrial; Mut; MUTA_HUMAN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	LHQQQPLHPEWAALAKKQLKGKNPEDLIWHTPEGISIKPLYSKRDTMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILELAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSGWSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTNDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVLAIDNTSVRNRQIEKLKKIKSSRDQALAERCLAALTECAASGDGNILALAVDASRARCTVGEITDALKKVFGEHKANDRMVSGAYRQEFGESKEITSAIKRVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSLGRPDILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLEKKQQSV
Expression Range	33-750aa
Protein Length	Full Length of Mature Protein
Mol. Weight	84.8 kDa
Research Area	Signal Transduction
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	Catalyzes the reversible isomerization of methylmalonyl-CoA (MMCoA) (generated from branched-chain amino acid metabolism and degradation of dietary odd chain fatty acids and cholesterol) to succinyl-CoA (3-carboxypropionyl-CoA), a key intermediate of the tricarboxylic acid cycle.
Subcellular Location	Mitochondrion matrix. Mitochondrion. Cytoplasm.
Protein Families	Methylmalonyl-CoA mutase family
Database References	HGNC: 7526 OMIM: 251000 KEGG: hsa:4594 STRING: 9606.ENSP00000274813 UniGene: PMID: 28943303 Study identified 41 novel mutations in patients with methylmalonic aciduria (MMA); most of them were missense mutations. The absence of MUT protein in most of the patient cell lines, suggesting protein instability as a major mechanism of deficiency in mut-type MMA. PMID: 27167370 A total of 54 different mutations in MUT were identified in 48 patients; 16 novel mutations were identified... In five patients, the NGS panel did not confirm the diagnosis made by complementation analysis. One of these patients was found to carry 2 novel mutations PMID: 27233228 we identified seven novel genetic variants: p.Leu549Pro, p.Glu564, p.Leu641Pro in MUT, p.Tyr206Cys in PCCB, p.His194Arg, p.Val298Met in BCKDHA and p.Glu286_Met290del in BCKDHB gene. In silico and/or eukaryotic expression studies confirmed pathogenic effect of all novel genetic variants PMID: 26830710 In methylmalonic acidemia,a total of 10 novel MUT mutations were detected in the Chinese population. c.729_730insTT (p.D244Lfs39) was the most frequent mutation. PMID: 26454439 Two novel mutations of the MUT gene, including c.581C>T (p.P194L) and c.1219A>T (p.N407Y), are associated with methylmalonic academia in a Chinese family. PMID: 27060300 Five different known mutations in either MUT or MMACHC genes were identified in seven of the eight Chinese patients with methyl malonic acidemia. PMID: 25982642 3 Patients with Isolated methylmalonic acidemia lacked methylmalonyl-CoA mutase (MCM) activity and had no MCM band, patients with the cobalamin defects had high MCM activity levels and an intense MCM band at about 83 kDa, in comparison to those in their parents. PMID: 26370686 a novel splice site mutation in intron 12 of the MUT gene is a potential highly pathogenic allele via inhibition of alternative splicing leading to Methylmalonic aciduria. PMID: 26449400 data stratify MUT missense mutations into categories of biochemical defects, including (1) reduced protein level due to misfolding, (2) increased thermolability, (3) impaired enzyme activity, and (4) reduced cofactor response in substrate turnover PMID: 25125334 This is the first description of a homozygous mutation in the N-terminal extended segment of the MCM apoenzyme. PMID: 24330302 Mutations in MUT cause methylmalonic acidemia. PMID: 24406457 Using alanine-scanning mutagenesis, we demonstrate that the switch III motif is critical for bidirectional signal transmission of the GTPase-activating protein activity of MCM and the chaperone functions of MeaB in the MeaB-MCM complex. PMID: 23873214 The contribution of Glu338 in human MCM to adenosylcobalamin Co-C bond labilization and catalysis was evaluated by substituting the residue with a glutamine, aspartate, or alanine. The MCM variants showed 16-, 330-, and 12-fold reductions in k(cat). PMID: 23311430 This work reveals that Mexican patients with MMA have new (p.V136F) as well as worldwide and hispanic reported mutations. The mutation R108C is the most frequent change (40% of total alleles) mainly in patients from Leon, Guanajuato PMID: 23045948 Pathogenicity of the human truncation mutant results from its inability to sequester adenosyltransferase (AdoCbl) for direct transfer to methylmalonyl-CoA mutase, resulting in holoenzyme formation and disease. PMID: 21604717 Methylmalonyl-CoA Mutase intronic variations causing aberrantly spliced messenger RNA is associated with propionic and methylmalonic acidemia. PMID: 17966092 MMAA acts as a chaperone of human MCM protein. PMID: 21138732 Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation. PMID: 20876572 CPS1, MUT, NOX4, and DPEP1 is associated with plasma homocysteine in healthy Women. PMID: 20031578 Seventeen MUT gene mutations were detected in 14 of the 21 methylmalonic acidemia patients, among them 8 mutations were novel. PMID: 19806564 Analysis of the prevalence and distribution of MCM mutations throughout the coding sequence in relation to the enzyme structure. PMID: 15643616 The MUT gene was sequenced in 160 patients with mut methylmalonic acidemia (MMA). Sequence analysis identified mutations in 96% of disease alleles. PMID: 16281286 p.Y100C, p.R108H, p.N366S, p.V633G, p.R694W, p.R694L and p.M700K mutations are associated with a mut(-) phenotype. PMID: 17113806 A case report is presented of kidney transplantation in MUT. PMID: 17401587 Mutations in methylmalonyl-CoA mutase is associated with methylmalonic acidemia PMID: 17410422 Novel mutation of the MCM gene (R727X)identified in a Japanese girl causing mild presentation of methylmalonic acidemia during infancy. PMID: 17445044 Long-term outcome in methylmalonic acidurias is influenced by the underlying genetic defects in MCM/MMAA/MMAB. PMID: 17597648 Crystal structure and mutagenesis of MUT: insight into the causes of metylamalonic aciduria. PMID: 17728257 Methylmalonic acidaemia: examination of genotype and biochemical data in 32 patients belonging to mut, cblA or cblB complementation group. PMID: 17957493 early hyperammonemia can lead to significant brain damage in methylmalonic acidemia PMID: 18940555 Mitochondrial dysfunction in MUT is reported. PMID: 19088183

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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.

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