SHMT2/SHMT Antibody [H9N23] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat

Usage Information

Dilution
WB1:5000 IP1:30 IHC1:5000 IF1:1000 FCM1:500 - 1:12500

Application
WB, IP, IHC, IF, FCM

Reactivity
Human, Mouse, Rat

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
56 kDa 55 kDa,37 kDa, 124 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
SHMT2/SHMT Antibody [H9N23] detects endogenous levels of total SHMT2/SHMT protein.

Clone
H9N23

Synonym(s)
SHMT, Glycine hydroxymethyltransferase, Serine methylase, SHMT2

Background
SHMT2 is the mitochondrial isoform of serine hydroxymethyltransferase in the PLP-dependent SHMT family, where it catalyzes the reversible conversion of serine and tetrahydrofolate to glycine and 5,10‑methylenetetrahydrofolate and thereby supplies mitochondrial one‑carbon units that feed nucleotide synthesis, mitochondrial translation, and redox control. The enzyme functions as a homotetramer with a conserved active site built around pyridoxal 5′‑phosphate that binds serine, performs α‑carbon deprotonation, and transfers the one‑carbon unit onto tetrahydrofolate, generating 5,10‑methylenetetrahydrofolate that is subsequently processed by mitochondrial MTHFD enzymes and routed into de novo thymidylate and purine biosynthesis as well as formate export to the cytosolic folate cycle. Within the mitochondrial one‑carbon network, SHMT2 sits upstream of thymidylate synthase and purine biosynthetic reactions and is also required to generate the 5,10‑methylenetetrahydrofolate used for taurinomethyluridine modification at wobble positions of specific mitochondrial tRNAs, linking its catalytic activity directly to maintenance of mitochondrial DNA integrity and efficient mitochondrial translation. Loss or reduction of SHMT2 impairs mitochondrial folate accumulation and formate production, decreases mitochondrial membrane potential and basal respiration, and leads to accumulation of the purine intermediate AICAR, reduced purine nucleotide pools, and slowed proliferation, while overexpression increases proliferation and tumor growth and induces a glycine‑auxotrophic state in which exogenous glycine becomes critical to sustain nucleotide synthesis. In Lung, colorectal, hepatocellular, renal, and breast cancers, SHMT2 is upregulated and forms part of a broader one‑carbon metabolic rewiring that channels serine-derived one‑carbon units into nucleotide biosynthesis and NADPH generation, supports rapid DNA replication, and buffers oxidative stress, and pan‑cancer analyses correlate high SHMT2 expression with poor prognosis and proliferation‑associated transcriptional programs. SHMT2 also acts as a key enzymatic node in mitochondrial one‑carbon metabolism that is druggable with small‑molecule active‑site ligands and allosteric inhibitors, and preclinical work demonstrates that selective SHMT2 blockade depletes nucleotide pools, triggers DNA replication stress, and synergizes with antifolate or thymidylate synthase–targeted therapies.

Background

SHMT2 is the mitochondrial isoform of serine hydroxymethyltransferase in the PLP-dependent SHMT family, where it catalyzes the reversible conversion of serine and tetrahydrofolate to glycine and 5,10‑methylenetetrahydrofolate and thereby supplies mitochondrial one‑carbon units that feed nucleotide synthesis, mitochondrial translation, and redox control. The enzyme functions as a homotetramer with a conserved active site built around pyridoxal 5′‑phosphate that binds serine, performs α‑carbon deprotonation, and transfers the one‑carbon unit onto tetrahydrofolate, generating 5,10‑methylenetetrahydrofolate that is subsequently processed by mitochondrial MTHFD enzymes and routed into de novo thymidylate and purine biosynthesis as well as formate export to the cytosolic folate cycle. Within the mitochondrial one‑carbon network, SHMT2 sits upstream of thymidylate synthase and purine biosynthetic reactions and is also required to generate the 5,10‑methylenetetrahydrofolate used for taurinomethyluridine modification at wobble positions of specific mitochondrial tRNAs, linking its catalytic activity directly to maintenance of mitochondrial DNA integrity and efficient mitochondrial translation. Loss or reduction of SHMT2 impairs mitochondrial folate accumulation and formate production, decreases mitochondrial membrane potential and basal respiration, and leads to accumulation of the purine intermediate AICAR, reduced purine nucleotide pools, and slowed proliferation, while overexpression increases proliferation and tumor growth and induces a glycine‑auxotrophic state in which exogenous glycine becomes critical to sustain nucleotide synthesis. In Lung, colorectal, hepatocellular, renal, and breast cancers, SHMT2 is upregulated and forms part of a broader one‑carbon metabolic rewiring that channels serine-derived one‑carbon units into nucleotide biosynthesis and NADPH generation, supports rapid DNA replication, and buffers oxidative stress, and pan‑cancer analyses correlate high SHMT2 expression with poor prognosis and proliferation‑associated transcriptional programs. SHMT2 also acts as a key enzymatic node in mitochondrial one‑carbon metabolism that is druggable with small‑molecule active‑site ligands and allosteric inhibitors, and preclinical work demonstrates that selective SHMT2 blockade depletes nucleotide pools, triggers DNA replication stress, and synergizes with antifolate or thymidylate synthase–targeted therapies.

References
https://pubmed.ncbi.nlm.nih.gov/32903271/ https://pubmed.ncbi.nlm.nih.gov/33860190/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%