SHMT2 Protein, Human

The SHMT2 protein catalyzes the cleavage of serine to produce 5,10-methylenetetrahydrofolate for purine synthesis. It binds to mitochondrial DNA and participates in target protein deubiquitination via the BRISC complex. SHMT2 Protein, Human is the recombinant human-derived SHMT2 protein, expressed by E. coli , with tag free. The total length of SHMT2 Protein, Human is 476 a.a., .

SHMT2, a versatile enzyme, serves a crucial role in cellular metabolism by catalyzing the cleavage of serine to glycine while concurrently producing 5,10-methylenetetrahydrofolate, an essential intermediate in purine biosynthesis. This process is pivotal for generating one-carbon units, with serine acting as the major contributor to folate-associated one-carbon metabolism. SHMT2's involvement extends to mitochondrial thymidylate biosynthesis, where it aids in preventing uracil accumulation in mtDNA. Additionally, it plays a crucial role in mitochondrial translation by producing 5,10-methylenetetrahydrofolate, a methyl donor essential for the modification of mitochondrial tRNAs. Beyond its mitochondrial functions, SHMT2 participates in the deubiquitination of target proteins as a component of the BRISC complex, demonstrating its multifaceted contributions to cellular processes.

Human

E. coli

Tag Free

P34897 (S29-H504)

6472

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.