Anti-SHMT Antibody, clone 4D2.1

Evaluated by Western Blotting in Raji cell lysate.

Western Blotting Analysis: A 1:1,000 dilution of this antibody detected SHMT in Raji cell lysate.

Anti-SHMT, clone 4D2.1, Cat. No. MABS1822, is a mouse monoclonal antibody that detects mitochondrial Serine hydroxymethyltransferase and has been tested for use in Immunohistochemistry (Paraffin) and Western Blotting.

Immunohistochemistry Analysis: A 1:50-250 dilution of this antibody from a representative lot detected SHMT in human colon, human liver, and human pancreas tissue sections.

Western Blotting Analysis: A 1:1,000 dilution from a representative lot detected SHMT in Jurkat cell lysate.

Research Category
Signaling

Clone 4D2.1 detects human mitochondrial Serine hydroxymethyltransferase. It targets an epitope within 107 amino acids from the C-terminal half.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Serine hydroxymethyltransferase, mitochondrial (UniProt: P34897; also known as EC: 2.1.2.1, SHMT, Glycine hydroxymethyltransferase, Serine methylase) is encoded by the SHMT2 gene (Gene ID: 6472) in human. SHMT is involved in the de novo mitochondrial thymidylate biosynthesis pathway via its role in glycine and tetrahydrofolate metabolism. Thymidylate biosynthesis is required to prevent uracil accumulation in mtDNA. SHMT catalyzes the reversible conversion of serine and glycine. It uses pyridoxal-5 -phosphate as a cofactor. SHMT is synthesized with a transit peptide (aa 1-29) that is needed for its mitochondrial translocation. In eukaryotes two forms of SHMT have been reported: cytosolic and mitochondrial. In the presence of bound pyridoxal 5′-phosphate it is present in a homotetrameric form and in the absence of pyridoxal 5′-phosphate it exists as a homodimer. Pyridoxal 5′-phosphate binding mediates an important conformation change, which is essential for its tetramerization. Three isoforms of SHMT have been reported that are produced by alternative splicing.

~56 kDa observed; 55.99 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

GST/His-tagged recombinant fragment corresponding to 107 amino acids from the C-terminal half of human mitochondrial Serine hydroxymethyltransferase.

Concentration: Please refer to lot specific datasheet.

Format: Purified

Protein G purified

Purified mouse monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.