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SHMT1 encodes the cellular form of serine hydroxymethyltransferase, a pyridoxal phosphate-containing enzyme that catalyzes the reversible conversion of serine and tetrahydrofolate to glycine and 5,10-methylene tetrahydrofolate. Additionally we are shipping serine Hydroxymethyltransferase 1 (Soluble) Antibodies (69) and serine Hydroxymethyltransferase 1 (Soluble) Kits (5) and many more products for this protein.
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Methylene tetrahydrofolate reductase (MTHFR (show MTHFR Proteins)) C677T, 5-methyltetrahydrofolate homocysteine methyltransferase (MTR (show MTR Proteins)) A2756G and 5- methyltetrahydrofolate homocysteine methyltransferase reductase (MTRR (show MTRR Proteins)) A66G were shown to be positively associatiated with homocysteine, while nonvegetarian diet, serine hydroxymethyltransferase 1 (SHMT1) C1420T and TYMS (show TYMS Proteins) 5'-UTR 28 bp tandem repeat exhibited negative association with homocysteine.
The one-carbon donor formate generally rescues cells from SHMT inhibition, but paradoxically increases the inhibitor's cytotoxicity in diffuse large B-cell lymphoma (DLBCL); this effect is rooted in defective glycine uptake in DLBCL cell lines, rendering them uniquely dependent upon SHMT enzymatic activity to meet glycine demand.
The present study, using both case-control and family-based triad approach is the first report to demonstrate parental association of SHMT1 C1420T variant in conferring NTD risk in the fetus.
SHMT1 controls the expression of pro-oncogenic inflammatory cytokines by regulating sialic acid Neu5Ac to promote ovarian cancer tumor growth and migration.
Site-directed mutagenesis experiments on SHMT1 demonstrate that selective enzyme inhibition relies on the presence of a cysteine residue at the active site of SHMT1 (Cys204) that is absent in SHMT2 (show SHMT2 Proteins).
SHMT1 C1420T polymorphism contributes to the risk of non-Hodgkin.
we identified SHMT1 as a target gene of miR (show MLXIP Proteins)-198. In conclusion, miR (show MLXIP Proteins)-198 suppressed proliferation of lung adenocarcinoma cells both in vitro and in vivo by directly targeting SHMT1.
an association between MTRR (show MTRR Proteins) 66 and SHMT1 1420 polymorphisms and spaceflight-induced vision changes
our meta-analysis suggested that the SHMT1 C1420T polymorphism was associated with decreased risk of breast cancer.
SHMT1 knockdown in lung cancer cells leads to cell cycle arrest and to p53 (show TP53 Proteins)-dependent apoptosis.
Shmt1 and dietary folate deficiency influence metabolic markers of homocysteine remethylation in mice.
SHMT1 and TYMS (show TYMS Proteins) localization to the nucleus is essential to prevent uracil accumulation in DNA
Data show that Shmt1 hemizygosity was associated with increased risk for intestinal cancer in Apc (show APC Proteins)(min)(/+) mice through a gene-by-diet interaction.
These results provide evidence that disruption of Shmt1 expression causes NTDs by impairing thymidylate biosynthesis and shows that changes in the expression of genes that encode folate-dependent enzymes may be key determinates of NTD risk.
Shmt1 (SHMT1), but not Srr (show SRR Proteins), is likely to be one of the genetic components regulating prepulse inhibition in mice and possibly relevant to human schizophrenia.
mitochondrial SHMT-derived one-carbon units are essential for folate-mediated one-carbon metabolism in the cytoplasm
SHMT1 and SHMT2 (show SHMT2 Proteins) are functionally redundant in nuclear de novo thymidylate biosynthesis
we have expressed, characterized, and determined the crystal structures of rabbit cytosolic serine hydroxymethyltransferase T254A and T254C mutant forms, in the absence and presence of substrates.
SHM1 and SHM2 operate in a redundant manner in one-carbon metabolism of nonphotorespiring cells with a high demand of one-carbon units.
The senescence is initiated in shm1-1 under photorespiratory conditions. Transcription of the senescence marker SAG12 is enhanced in shm1-1.
Structural modeling of SHM1, SHM2, and SHM4 presented features that may explain the activity differences between the mitochondrial and cytosolic isozymes.
The characterization and expression of SHMT1 in A. thaliana. [SHMT1]
SHM1 expression is required for mitochondrial serine hydroxymethyltransferase (show SHMT2 Proteins) activity and proper function of the C2 cycle during growth in ambient air.
SHMT1 interacts with GLU1 and this interaction is necessary for photorespiratory serine hydroxymethyltransferase (SHMT) activity.
This gene encodes the cellular form of serine hydroxymethyltransferase, a pyridoxal phosphate-containing enzyme that catalyzes the reversible conversion of serine and tetrahydrofolate to glycine and 5,10-methylene tetrahydrofolate. This reaction provides one carbon units for synthesis of methionine, thymidylate, and purines in the cytoplasm. This gene is located within the Smith-Magenis syndrome region on chromosome 17. Alternative splicing of this gene results in 2 transcript variants encoding 2 different isoforms. Additional transcript variants have been described, but their biological validity has not been determined.
serine hydroxymethyltransferase, cytosolic
, serine hydroxymethyltransferase 1 (soluble)
, glycine hydroxymethyltransferase
, serine methylase
, cytoplasmic serine hydroxymethyltransferase
, cytosolic serine hydroxymethyltransferase
, serine hydroxymethyl transferase
, serine hydroxymethyltransferase 2 (mitochondrial)