SMYD2 Antibody
(Synonyms: Histone methyltransferase SMYD2; HSKM B; HSKM-B; HSKMB; KMT3C; Lysine N-methyltransferase 3C; MGC119305; N lysine methyltransferase SMYD2; N-lysine methyltransferase SMYD2; SET and MYND domain containing 2; SET and MYND domain containing protein 2; SET and MYND domain-containing protein 2; Smyd2; SMYD2_HUMAN; Zinc finger MYND domain containing 14; ZMYND14.)SMYD2 Antibody is a Rabbit-derived and non-conjugated polyclonal antibody, targeting to SMYD2.
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Host:
Mouse
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Application:
WB, IHC-P, IF-Tissue
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Reactivity :
Human, Mouse
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Formulation:
Supplied in 0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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IF-Tissue
IF-Tissue: Immunofluorescence-Tissue
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|---|---|---|---|
| Dilution Ratio | 1:500-2000 | 1:100-500 | 1:100-500 |
Product Details
SMYD2 Antibody is a Rabbit-derived and non-conjugated polyclonal antibody, targeting to SMYD2.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman, Mouse
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Observed Molecular WeightObserved band size: 50 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
Purified recombinant human KMT3C / SMYD2 protein fragments expressed in E.coli.
affinity chromatography.
Non-conjugated
Unmodified
Product Properties
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Appearance
Solution
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Formulation
Supplied in 0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.
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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
SMYD2 (SET and MYND domain-containing protein 2) is a lysine methyltransferase that catalyzes the methylation of both histone and non-histone proteins, regulating chromatin accessibility and transcriptional activity[1][2]. Mechanistically, SMYD2 facilitates signal transduction in key pathways, including BMP/SMAD, STAT3, and NF-κB, by methylating substrates such as BMPR2, STAT3, p65, and TRAF2[3][4][5][6]. In disease models, aberrant SMYD2 expression drives tumor progression in triple-negative breast cancer, gastrointestinal cancers, and non-small-cell lung cancer, and contributes to vascular and renal pathologies, including neointimal hyperplasia and polycystic kidney disease[7][8][9][10]. Compared with related isoforms such as SMYD1 and SMYD3, SMYD2 exhibits distinct substrate specificity and tissue distribution, showing cytoplasmic localization and preference for non-histone targets, which differentiates its regulatory roles[1][2][11]. For experimental applications, selective chemical probes and inhibitors such as LLY-507, AZ505, A-893, and BAY-598 have enabled precise interrogation of SMYD2 functions in vitro and in vivo, suppressing methylation-dependent activation of oncogenic and inflammatory pathways[6][12][13]. These inhibitors provide valuable tools for dissecting SMYD2-mediated epigenetic regulation and validating its therapeutic potential across multiple disease contexts[12][13].
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Subcellular Localization
Cytoplasm, cytosol; Nucleus
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Expression
Induction:Expression is repressed by CEBPA -
Isoforms & Post-Translational Modification
Q9NRG4 has 2 isomers: Q9NRG4-1: 49688 Da (predicted); Q9NRG4-2: 30964 Da (predicted).
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Subunit
Interacts with RNA polymerase II and HELZ. Interacts (via MYND-type zinc finger) with EPB41L3. Interacts (via SET domain) with p53/TP53. Interacts with RB1 and HSP90AA1
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SwissProt ID
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Synonyms
Histone methyltransferase SMYD2; HSKM B; HSKM-B; HSKMB; KMT3C; Lysine N-methyltransferase 3C; MGC119305; N lysine methyltransferase SMYD2; N-lysine methyltransferase SMYD2; SET and MYND domain containing 2; SET and MYND domain containing protein 2; SET and MYND domain-containing protein 2; Smyd2; SMYD2_HUMAN; Zinc finger MYND domain containing 14; ZMYND14.
Documentation
[1]. Yi X, et al. Histone methyltransferase SMYD2: ubiquitous regulator of disease. Clin Epigenetics. 2019 Aug 1;11(1):112. [Content Brief]
[2]. Padilla A, et al. Targeting Epigenetic Changes Mediated by Members of the SMYD Family of Lysine Methyltransferases. Molecules. 2023 Feb 20;28(4):2000. [Content Brief]
[3]. Gao S, et al. The lysine methyltransferase SMYD2 methylates the kinase domain of type II receptor BMPR2 and stimulates bone morphogenetic protein signaling. J Biol Chem. 2017 Jul 28;292(30):12702-12712. [Content Brief]
[4]. Su H, et al. Histone methyltransferase Smyd2 drives adipogenesis via regulating STAT3 phosphorylation. Cell Death Dis. 2022 Oct 21;13(10):890. [Content Brief]
[5]. Wu W, et al. SMYD2-mediated TRAF2 methylation promotes the NF-κB signaling pathways in inflammatory diseases. Clin Transl Med. 2021 Nov;11(11):e591. [Content Brief]
[6]. Sweis RF, et al. Discovery of A-893, A New Cell-Active Benzoxazinone Inhibitor of Lysine Methyltransferase SMYD2. ACS Med Chem Lett. 2015 Apr 29;6(6):695-700. [Content Brief]
[7]. Li LX, et al. Lysine methyltransferase SMYD2 promotes triple negative breast cancer progression. Cell Death Dis. 2018 Feb 27;9(3):326. [Content Brief]
[8]. Xia K, et al. Role of SMYD2 in gastrointestinal cancer progression (Review). Oncol Lett. 2025 Apr 8;29(6):282. [Content Brief]
[9]. Wang R, et al. Effects of SMYD2-mediated EML4-ALK methylation on the signaling pathway and growth in non-small-cell lung cancer cells. Cancer Sci. 2017 Jun;108(6):1203-1209. [Content Brief]
[10]. Zhong X, et al. The lysine methyltransferase SMYD2 facilitates neointimal hyperplasia by regulating the HDAC3-SRF axis. Acta Pharm Sin B. 2024 Feb;14(2):712-728. [Content Brief]
[11]. Tracy C, et al. The Smyd Family of Methyltransferases: Role in Cardiac and Skeletal Muscle Physiology and Pathology. Curr Opin Physiol. 2018 Feb;1:140-152. [Content Brief]
[12]. Eggert E, et al. Discovery and Characterization of a Highly Potent and Selective Aminopyrazoline-Based in Vivo Probe (BAY-598) for the Protein Lysine Methyltransferase SMYD2. J Med Chem. 2016 May 26;59(10):4578-600. [Content Brief]
[13]. Nguyen H, et al. LLY-507, a Cell-active, Potent, and Selective Inhibitor of Protein-lysine Methyltransferase SMYD2. J Biol Chem. 2015 May 29;290(22):13641-53. [Content Brief]
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