- CITATIONS: 1
|Application ||WB, IHC-P, E|
|Other Accession||Q5E9P9, NP_004160.3, NP_683718.1, P35623|
|Calculated MW||53083 Da|
|Antigen Region||19-47 aa|
|Other Names||Serine hydroxymethyltransferase, cytosolic, SHMT, Glycine hydroxymethyltransferase, Serine methylase, SHMT1|
|Target/Specificity||This SHMT1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 19-47 amino acids from the N-terminal region of human SHMT1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||SHMT1 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Interconversion of serine and glycine (PubMed:8505317, PubMed:24698160).|
Provided below are standard protocols that you may find useful for product applications.
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.
Porter, K.E., et al. Environ. Res. 110(6):580-587(2010)
Summers, C.M., et al. Birth Defects Res. Part A Clin. Mol. Teratol. 88(8):679-688(2010)
Vijayakrishnan, J., et al. Haematologica 95(8):1405-1414(2010)
Levine, A.J., et al. Cancer Epidemiol. Biomarkers Prev. 19(7):1812-1821(2010)
Jugessur, A., et al. PLoS ONE 5 (7), E11493 (2010) :
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