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SHMT2 encodes the mitochondrial form of a pyridoxal phosphate-dependent enzyme that catalyzes the reversible reaction of serine and tetrahydrofolate to glycine and 5,10-methylene tetrahydrofolate.
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The one-carbon donor formate generally rescues cells from SHMT (show SHMT1 Proteins) 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 (show SHMT1 Proteins) enzymatic activity to meet glycine demand.
Our data confirm the heterogeneity of breast tumors at a functional proteomic level and dissects the relationship between metabolism-related proteins, pathological features and patient survival. These observations highlight the importance of SHMT2 and ASCT2 (show SLC1A5 Proteins) as valuable individual prognostic markers and potential targets for personalized breast cancer therapy
Data suggest that serine hydroxymethyltransferase 2 (SHMT2) may be a potential target in the treatment of hepatocellular carcinoma (HCC (show FAM126A Proteins)).
High SHMT2 expression is associated with idiopathic pulmonary fibrosis.
Site-directed mutagenesis experiments on SHMT1 (show SHMT1 Proteins) demonstrate that selective enzyme inhibition relies on the presence of a cysteine residue at the active site of SHMT1 (show SHMT1 Proteins) (Cys204) that is absent in SHMT2.
These results indicate that SHMT2 may be a valuable prognostic biomarker in ER-negative breast cancer cases
our results for the first time showed that miR (show MLXIP Proteins)-615-5p prevents proliferation and migration through negatively regulating SHMT2 in HCC (show FAM126A Proteins).
The SHMT-2 is the direct targets of miR (show MLXIP Proteins)-370 and miR (show MLXIP Proteins)-373, respectively, in human articular chondrocytes.
High SHMT2 expression increases glycine-dependent nucleotide synthesis leading to bladder cancer growth.
SHMT2 is required for glioblastoma multiforme cells to adapt to the tumour environment, but also renders these cells sensitive to glycine cleavage system inhibition
SHMT1 (show SHMT1 Proteins) and SHMT2 are functionally redundant in nuclear de novo thymidylate biosynthesis
This gene encodes the mitochondrial form of a pyridoxal phosphate-dependent enzyme that catalyzes the reversible reaction of serine and tetrahydrofolate to glycine and 5,10-methylene tetrahydrofolate. The encoded product is primarily responsible for glycine synthesis. The activity of the encoded protein has been suggested to be the primary source of intracellular glycine. The gene which encodes the cytosolic form of this enzyme is located on chromosome 17. Alternative splicing results in multiple transcript variants.
serine hydroxymethyltransferase 2 (mitochondrial)
, mitochondrial serine hydroxymethyltransferase
, serine hydroxymethyltransferase, mitochondrial
, GLY A+
, glycine auxotroph A, human complement for hamster
, glycine hydroxymethyltransferase
, serine aldolase
, serine hydroxymethylase
, serine methylase
, threonine aldolase