Polyclonal Rabbit DMGDH Antibody
- Known as:
- Polyclonal Rabbit DMGDH Antibody
- Catalog number:
- KA1072
- Product Quantity:
- 100ul
- Category:
- -
- Supplier:
- KareBay
- Gene target:
- Polyclonal Rabbit DMGDH Antibody
Related genes to: Polyclonal Rabbit DMGDH Antibody
- Gene:
- DMGDH NIH gene
- Name:
- dimethylglycine dehydrogenase
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 5q14.1
- Locus Type:
- gene with protein product
- Date approved:
- 2004-05-12
- Date modifiied:
- 2017-12-15
- Gene:
- SARDH NIH gene
- Name:
- sarcosine dehydrogenase
- Previous symbol:
- DMGDHL1
- Synonyms:
- SDH
- Chromosome:
- 9q34.2
- Locus Type:
- gene with protein product
- Date approved:
- 1998-03-02
- Date modifiied:
- 2016-10-05
Related products to: Polyclonal Rabbit DMGDH Antibody
Related articles to: Polyclonal Rabbit DMGDH Antibody
- This study provides a comprehensive tissue-specific transcriptomic analysis of mitochondrial genes associated with vitamin metabolism in buffalo. Using RNA-seq data from four post-pubertal female buffalo tissues (kidney, heart, brain, and ovary), we profiled 41 nuclear-encoded mitochondrial genes involved in the metabolism of B-complex vitamins, vitamins A, C, D, folate, choline, and one-carbon pathways. The kidney exhibited the highest expression of biotin-related genes (ACACB, PC, PCCA), supporting roles in fatty acid oxidation and gluconeogenesis, while the heart showed moderate expression, and the brain and ovary lower expression, consistent with their metabolic functions. In vitamin A metabolism, the kidney showed elevated transcription of AKR1B10 and BCO2 (retinoid detoxification), whereas the heart exhibited moderate RDH14 expression, and the brain and ovary showed minimal transcriptional activity. Vitamin D-related genes were highly expressed in the kidney (FDX1) and ovary (FDXR), with lower expression in heart and brain. Vitamin B6-associated genes were prominently expressed in the ovary (PLPBP) and kidney/brain (PNPO), with low expression in the heart. B12-processing genes (MMAA, MMAB, MMADHC) showed the highest expression in the kidney, followed by the heart. The thiamine transporter SLC25A19 was transcriptionally enriched in the ovary, with moderate expression in kidney and brain. Riboflavin metabolism genes (RFK, FLAD1, SLC25A32) were more highly expressed in the kidney and heart, while choline and betaine metabolism genes (DMGDH, CHDH, SARDH) and one-carbon metabolism genes (ALDH1L1, AMT, SFXN1) were predominantly expressed in the kidney. Overall, this transcriptomic evidence reveals organ-specific expression patterns of vitamin-dependent mitochondrial pathways in buffalo, offering insights for nutritional strategies to enhance livestock metabolic efficiency and contributing to the broader understanding of mammalian mitochondrial physiology. - Source: PubMed
Publication date: 2025/12/29
Sadeesh E MLahamge Madhuri SSingh PratikshaMohiddin Roshan - Through the analysis of EST database, we obtained one human EST (GenBank: H28856) which showed significant similarity with the partial coding sequence of rat dimethylglycine dehydrogenase gene. This EST was mapped to 9q34 due to 95.6% identity with one genomic sequence (GenBank: AC002295). A pair of primers (HRP-1/HRP-2) designed on the sequence of the EST were coupled with the primers (lambda gt10-5/lambda gt10-3) on the vector flanking cloning site respectively to amplify the 5' and 3' cDNA beyond the EST. New primers designed based on novel cDNA sequence overlapped with the sequence within EST H28856 were used for amplification with lambda gt10-5 and lambda gt10-3 by the similar way as above untill a complete ORF was obtained. Finally, a 1,970 bp sequence (termed as dimethylglycine dehydrogenase like gene isoform I, DMGDHL1a) containing a 1,428 bp complete coding sequence from the live cDNA library and 1,475 bp sequence (isoform II, termed as DMGDHL1b) containing a 1,296 bp complete coding sequence from the fetas live cDNA library were obtained. Fourteen exons were identified in isoform I and the first nine exons of isoform II which shared with isoform I could be determined too. The last 105 bp cDNA sequence of isoform II could not be found in the public database, indicating a very large intron (> 123 kb) existed between exon 9 and exon 10 of isoform II. DMGDHL1 showed highly homology on both cDNA and amino acid level with rat dimethylglycine dehydrogenase (60% identity in 135 bp and 35% identity in 436 residues respectively). It was reported that human sarcosinemia gene was mapped at 9q34. Therefore it could be a good candidate gene for the sarcosinemia. - Source: PubMed
Xia J HYu K PLiu C YPan QZheng DDai H P - Anti-mitochondrial antibodies (anti-M7) in sera from patients with dilated cardiomyopathy and myocarditis recognize, besides mitochondrial antigens, bacterial sarcosine dehydrogenase. The common target antigen was identified as the covalently bound FAD of mitochondrial and bacterial flavoenzymes. Thus, anti-M7-positive serum reacted on Western blots exclusively with covalently flavinylated enzymes. The antigenic specificity of anti-M7 sera was reproduced by an antiserum raised in rabbits with 6-hydroxy-D-nicotine oxidase. The heart mitochondrial membrane antigen recognized by anti-M7 serum was identified as the flavoprotein subunit of succinate dehydrogenase, the antigens in rat liver mitochondrial matrix as the flavoenzymes dimethylglycine dehydrogenase and sarcosine dehydrogenase. Anti-M7 serum contained a specific anti-flavoenzyme antibody fraction. Nanomolar concentrations of FAD and riboflavin inhibited the immune reaction on Western blots and in ELISA, and incubation with FAD-agarose depleted the anti-M7 activity of the serum. N-terminally deleted dimethylglycine dehydrogenase proteins were only immunoprecipitated by anti-M7 sera when the FAD was covalently incorporated. An affinity constant (KD) of 10(-8) M was established for the anti-flavoenzyme antibodies by competitive ELISA. Of patients with cardiomyopathy and myocarditis, 36% and 25%, respectively, were anti-flavoenzyme-positive by Western blot and ELISA, but only two of 15 patients with other heart diseases and none of 50 healthy controls. - Source: PubMed
Otto AStähle IKlein RBerg P APankuweit SBrandsch R - - Source: PubMed
Cook R JWagner C - Dimethylglycine dehydrogenase (EC 1.5.99.2) and sarcosine dehydrogenase (EC 1.5.99.1) are flavoproteins which catalyze the oxidative demethylation of dimethylglycine to sarcosine and sarcosine to glycine, respectively. During these reactions tightly bound tetrahydropteroylpentaglutamate (H4PteGlu5) is converted to 5,10-methylene tetrahydropteroylpentaglutamate (5,10-CH2-H4PteGlu5), although in the absence of H4PteGlu5, formaldehyde is produced. Single turnover studies using substrate levels of the enzyme (2.3 microM) showed pseudo-first-order kinetics, with apparent first-order rate constants of 0.084 and 0.14 s-1 at 23 and 48.3 microM dimethylglycine, respectively, for dimethylglycine dehydrogenase and 0.065 s-1 at 47.3 microM sarcosine for sarcosine dehydrogenase. The rates were identical in the absence or presence of bound tetrahydropteroylglutamate (H4PteGlu). Titration of the enzymes with substrate under anaerobic conditions did not disclose the presence of an intermediate semiquinone. The effect of dimethylglycine concentration upon the rate of the dimethylglycine dehydrogenase reaction under aerobic conditions showed nonsaturable kinetics suggesting a second low-affinity site for the substrate which increases the enzymatic rate. The Km for the high-affinity active site was 0.05 mM while direct binding for the low-affinity site could not be measured. Sarcosine and dimethylthetin are poor substrates for dimethylglycine dehydrogenase and methoxyacetic acid is a competitive inhibitor at low substrate concentrations. At high dimethylglycine concentrations, increasing the concentration of methoxyacetic acid produces an initial activation and then inhibition of dimethylglycine dehydrogenase activity. When these compounds were added in varying concentrations to the enzyme in the presence of dimethylglycine, their effects upon the rate of the reaction were consistent with the presence of a second low-affinity binding site on the enzyme which enhances the reaction rate. When sarcosine is used as the substrate for sarcosine dehydrogenase the kinetics are Michaelis-Menten with a Km of 0.5 mM for sarcosine. Also, methoxyacetic acid is a competitive inhibitor of sarcosine dehydrogenase with a Ki of 0.26 mM. In the absence of folate, substrate and product determinations indicated that 1 mol of formaldehyde and of sarcosine or glycine were produced for each mole of dimethylglycine or sarcosine consumed with the concomitant reduction of 1 mol of bound FAD. - Source: PubMed
Porter D HCook R JWagner C