SHMT2 Antibody (YA7793)
(Synonyms: GLYA; HEL-S-51e; NEDCASB; SHMT)SHMT2 Antibody (YA7793) is a Mouse-derived and non-conjugated IgG2a monoclonal antibody, targeting to SHMT2.
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Host:
Mouse
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Isotype:
IgG
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Application:
IHC-P
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Reactivity :
Human, Mouse, Rat
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Formulation:
Spplied in PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.
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Conjugation:
Non-conjugated
Applications
| Application |
IHC-P
IHC-P: Immunohistochemistry-Paraffin
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|---|---|
| Dilution Ratio | 1:150-500 |
Product Details
SHMT2 Antibody (YA7793) is a Mouse-derived and non-conjugated IgG2a monoclonal antibody, targeting to SHMT2.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman, Mouse, Rat
Full length human recombinant protein of human SHMT2 produced in E.coli.
Endogenous
Affinity purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Spplied in PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
SHMT2 (serine hydroxymethyltransferase 2) is the mitochondrial isoform of serine hydroxymethyltransferase and catalyzes the conversion of serine to glycine while generating one-carbon units that enter mitochondrial folate-mediated one-carbon metabolism[1][2]. This reaction supports nucleotide biosynthesis, methylation-related metabolism, redox homeostasis, and other anabolic processes required for cellular growth and proliferation[1][3][4]. Mechanistically, SHMT2 functions at the entry point of the mitochondrial serine catabolic pathway and supplies tetrahydrofolate-conjugated one-carbon units that contribute to downstream metabolic reactions and mitochondrial homeostasis[1][5]. Therefore, SHMT2 has emerged as a central regulator of mitochondrial one-carbon metabolism, a pathway increasingly linked to metabolic adaptation in rapidly proliferating cells and tumors[4][6]. In disease contexts, elevated SHMT2 expression has been reported across multiple cancers and is associated with tumor progression, cellular proliferation, and unfavorable clinical features[3][7][8]. Experimental studies further demonstrate that SHMT2 supports mitochondrial respiration and proliferation under metabolic stress conditions, whereas SHMT2 inhibition compromises mitochondrial function and suppresses tumor growth in vitro and in vivo[5][8][9]. Compared with the related cytosolic isoform SHMT1, which primarily operates in the cytoplasm, SHMT2 is localized to mitochondria and is considered the dominant enzyme driving serine catabolism and growth-associated one-carbon flux in many cancer models[2][7]. For experimental applications, SHMT2 has attracted substantial interest as a therapeutic target, and both small-molecule and RNA-based inhibitory strategies have shown the ability to disrupt SHMT2-dependent metabolism and reduce cancer cell viability or tumor progression in preclinical models[6][10].
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Subcellular Localization
Mitochondrion,Mitochondrion matrix, mitochondrion nucleoid,Mitochondrion inner membrane,Cytoplasm,Nucleus
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Isoforms & Post-Translational Modification
P34897 has three isomers: P34897-1: 55993 Da (predicted); P34897-2: 54863 Da (predicted); P34897-3: 53455 Da (predicted).
Succinylation at Lys-280 inhibits the hydroxymethyltransferase activity -
Subunit
Homotetramer; in the presence of bound pyridoxal 5'-phosphate (PubMed:25619277, PubMed:29180469)
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SwissProt ID
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Synonyms
GLYA; HEL-S-51e; NEDCASB; SHMT
Documentation
[1]. Minton DR, et al. Serine Catabolism by SHMT2 Is Required for Proper Mitochondrial Translation Initiation and Maintenance of Formylmethionyl-tRNAs. Mol Cell. 2018;69(4):610-621.e5. [Content Brief]
[2]. Lee SE, et al. Unraveling the role of the mitochondrial one-carbon pathway in undifferentiated thyroid cancer by multi-omics analyses. Nat Commun. 2024 Feb 8;15(1):1163. [Content Brief]
[3]. Zeng Y, et al. Roles of Mitochondrial Serine Hydroxymethyltransferase 2 (SHMT2) in Human Carcinogenesis. J Cancer. 2021;12(19):5888-5894. [Content Brief]
[4]. Dekhne AS, et al. Therapeutic Targeting of Mitochondrial One-Carbon Metabolism in Cancer. Mol Cancer Ther. 2020;19(11):2245-2255. [Content Brief]
[5]. Tsai PI, et al. PINK1 Phosphorylates MIC60/Mitofilin to Control Structural Plasticity of Mitochondrial Crista Junctions. Mol Cell. 2018 Mar 1;69(5):744-756.e6. [Content Brief]
[6]. Cuthbertson CR, et al. A Review of Small-Molecule Inhibitors of One-Carbon Enzymes: SHMT2 and MTHFD2 in the Spotlight. ACS Pharmacol Transl Sci. 2021;4(2):624-646. [Content Brief]
[7]. Liu Z, et al. Serine hydroxymethyltransferase 2 knockdown induces apoptosis in ccRCC by causing lysosomal membrane permeabilization via metabolic reprogramming. Cell Death Dis. 2023 Feb 20;14(2):144. [Content Brief]
[8]. Sun W, et al. Targeting serine-glycine-one-carbon metabolism as a vulnerability in cancers. Biomark Res. 2023 May 5;11(1):48. [Content Brief]
[9]. Liberati FR, et al. RNA-mediated inhibition of mitochondrial SHMT2 impairs cancer cell proliferation. Cell Death Discov. 2025 Aug 6;11(1):369. [Content Brief]
[10]. Newman AC, et al. One-carbon metabolism in cancer. Br J Cancer. 2017;116(12):1499-1504.