Rabbit Polyclonal MTHFD1 antibody. Carrier free. Suitable for WB and reacts with Mouse, Human samples. Cited in 4 publications. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human MTHFD1.
pH: 7.4
Constituents: 100% PBS
WB | |
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Human | Tested |
Mouse | Tested |
Species | Dilution info | Notes |
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Species Mouse | Dilution info 1.00000-5.00000 µg/mL | Notes - |
Species Human | Dilution info 1.00000-5.00000 µg/mL | Notes - |
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Trifunctional enzyme that catalyzes the interconversion of three forms of one-carbon-substituted tetrahydrofolate: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate, 5,10-methenyltetrahydrofolate and (6S)-10-formyltetrahydrofolate (PubMed:10828945, PubMed:18767138, PubMed:1881876). These derivatives of tetrahydrofolate are differentially required in nucleotide and amino acid biosynthesis, (6S)-10-formyltetrahydrofolate being required for purine biosynthesis while (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate is used for serine and methionine biosynthesis for instance (PubMed:18767138, PubMed:25633902).
MTHFC, MTHFD, MTHFD1, C1-THF synthase, Epididymis secretory sperm binding protein
Rabbit Polyclonal MTHFD1 antibody. Carrier free. Suitable for WB and reacts with Mouse, Human samples. Cited in 4 publications. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human MTHFD1.
pH: 7.4
Constituents: 100% PBS
The MTHFD1 protein also known as C1-THF synthase is a trifunctional enzyme involved in the folate metabolism. It has a mass of approximately 102 kDa and functions within the cytoplasm. MTHFD1 catalyzes three sequential activities: methylene-THF dehydrogenase methenyl-THF cyclohydrolase and formyl-THF synthetase. These enzymatic activities are fundamental for cellular one-carbon metabolism. This protein is widely expressed in various tissues including liver and fetal tissues reflecting its importance in cellular metabolism.
MTHFD1 plays a central role in folate-mediated one-carbon transfer reactions. It connects the cytoplasmic folate cycle to nucleotide biosynthesis and amino acid metabolism. As a multifunctional enzyme it is known to integrate with the cytosolic one-carbon metabolic complex allowing it to coordinate closely with other enzymes in the cycle. This function supports the synthesis of purines and thymidylate which are essential building blocks for DNA and RNA.
MTHFD1 integrates into the folate and methionine cycles important parts of cellular metabolism. It collaborates with enzymes such as SHMT1 in the biosynthesis of nucleotides. The folate cycle in which MTHFD1 participates provides one-carbon units necessary for methylation reactions and nucleotide synthesis playing a part in maintaining genomic stability. This partnership with the methionine cycle further indicates its influence on cellular methylation patterns impacting gene expression and protein function.
MTHFD1 has associations with certain conditions notably neural tube defects and cardiovascular disease. Mutations or polymorphisms in the MTHFD1 gene can disrupt the folate and methionine cycles leading to disturbed one-carbon metabolism. In neural tube defects low activity of MTHFD1 correlates with insufficient nucleotide biosynthesis and improper DNA methylation. In cardiovascular disease MTHFD1 interacts with homocysteine metabolism through its role in the methylation cycle influencing levels of this risk-associated amino acid.
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All lanes: Western blot - Anti-MTHFD1 antibody (ab103698) at 5 µg/mL
All lanes: Human liver tissue lysate at 50 µg
Predicted band size: 102 kDa
All lanes: Western blot - Anti-MTHFD1 antibody (ab103698) at 5 µg/mL
All lanes: Mouse liver tissue lysate at 50 µg
Predicted band size: 102 kDa
All lanes: Western blot - Anti-MTHFD1 antibody (ab103698) at 5 µg/mL
Lane 1: MTHFD1 transfected 293T cell lysate
Lane 2: Non-transfected 293T cell lysate
Predicted band size: 102 kDa
Image collected and cropped by CiteAb under a CC-BY license from the publication
MTHFD1 western blot using anti-MTHFD1 antibody ab103698. Publication image and figure legend from Kühl, I., Miranda, M., et al., 2017, Elife, PubMed 29132502.
ab103698 was used in this publication in western blot. This may not be the same as the application(s) guaranteed by Abcam. For a full list of applications guaranteed by Abcam for ab103698 please see the product overview.
Up-regulation of the enzymes of the mitochondrial 1C pathway happens before deficient OXPHOS is detectable in mouse heart.(A) Scheme of 1C pathway. Colored boxes: protein levels; red: increased, grey: not detected or not quantified. (B) Heatmaps showing the fold-change in transcript (left) and protein (right) levels in alphabetical order of L/L, cre and L/L mouse hearts of the 1C pathway; p<0.0001 in≥1 knockout strain. (C) Immunoblot of enzymes of the 1C pathway in total protein extracts from L/L, cre and L/L; Loading: tubulin. (D) Quantification of 1C donor metabolite levels in L/L, cre and L/L. Graphs represent mean ± SEM (*p<0.05, **p<0.01, ***p<0.001). (E) Time point analysis of protein levels of enzymes of the 1C pathway (top), and LRPPRC and VDAC (bottom) in Lrpprc knockout hearts compared to controls. Yellow line: average value of nuclear and mitochondrial encoded OXPHOS complex IV subunits. Adjusted p<0.05, except for VDAC. LRPPRC and VDAC protein levels at the different time points were verified by immunoblot presented in Figure 6—figure supplement 1.10.7554/eLife.30952.025Figure 6—source data 1.Determination of 1C pathway donor metabolites.Determination of 1C pathway donor metabolites.Steady-state LRPPRC protein levels at different time points in mitochondrial extracts from Lrpprc L/L, cre and L/L hearts; Loading: VDAC1.
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