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Description
Mammalian serine hydroxymethyltransferase (SHMT) is a tetrameric, pyridoxal phosphate (PLP)-dependent enzyme that catalyzes the reversible interconversion of serine and tetrahydrofolate to glycine and methylenetetrahydrofolate in the cytoplasm (cSHMT, SHMT1) and mitochondria (mSHMT, SHMT2). cSHMT preferentially supplies one-carbon units for thymidylate biosynthesis, depletes methylenetetrahydrofolate pools for S-adenosylmethionine (SAM) synthesis by synthesizing serine, sequesters 5-methyltetrahydrofolate, and inhibits SAM synthesis.
Specifications
Specifications
| Antigen | SHMT2 |
| Applications | Immunocytochemistry, Immunofluorescence, Immunohistochemistry (Paraffin), Western Blot |
| Classification | Polyclonal |
| Concentration | 0.2 mg/mL |
| Conjugate | Unconjugated |
| Formulation | PBS with 50% glycerol and 0.1% sodium azide; pH 7.3 |
| Gene | SHMT2 |
| Gene Accession No. | P34897, Q9CZN7 |
| Gene Alias | GLYA, Serine methylase, SHMT, SHMT2 |
| Gene Symbols | SHMT2 |
| Show More |
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