Recombinant Human N-lysine methyltransferase SMYD2 (SMYD2)

Code CSB-YP885705HU
MSDS
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Source Yeast
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Code CSB-EP885705HU
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Source E.coli
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Code CSB-EP885705HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP885705HU
MSDS
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Source Baculovirus
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Code CSB-MP885705HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
SMYD2
Uniprot No.
Alternative Names
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
Species
Homo sapiens (Human)
Expression Region
1-433
Target Protein Sequence
MRAEGLGGLE RFCSPGKGRG LRALQPFQVG DLLFSCPAYA YVLTVNERGN HCEYCFTRKE GLSKCGRCKQ AFYCNVECQK EDWPMHKLEC SPMVVFGENW NPSETVRLTA RILAKQKIHP ERTPSEKLLA VKEFESHLDK LDNEKKDLIQ SDIAALHHFY SKHLGFPDND SLVVLFAQVN CNGFTIEDEE LSHLGSAIFP DVALMNHSCC PNVIVTYKGT LAEVRAVQEI KPGEEVFTSY IDLLYPTEDR NDRLRDSYFF TCECQECTTK DKDKAKVEIR KLSDPPKAEA IRDMVRYARN VIEEFRRAKH YKSPSELLEI CELSQEKMSS VFEDSNVYML HMMYQAMGVC LYMQDWEGAL QYGQKIIKPY SKHYPLYSLN VASMWLKLGR LYMGLEHKAA GEKALKKAIA IMEVAHGKDH PYISEIKQEI ESH
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.
Gene References into Functions
  1. We show that tool compounds as well as CRISPR/Cas9 fail to reproduce many of the cell proliferation findings associated with SMYD2 and SMYD3 inhibition previously obtained with RNAi based approaches and with early stage chemical probes. PMID: 29856759
  2. Lysine methylation represses p53 activity in teratocarcinoma cancer cells via up-regulation of SMYD2 and PR-Set7 and perpetuation of cancer cells proliferation. PMID: 27535933
  3. SMYD2-H4K20me1-L3MBTL1 axis contributes to HIV-1 latency and can be targeted with small-molecule SMYD2 inhibitors. PMID: 28494238
  4. identifie novel cellular substrates of the lysine methyltransferase SMYD2. Of the 14 novel putative SMYD2 substrates identified, six were confirmed in cells by immunoprecipitation: MAPT, CCAR2, EEF2, NCOA3, STUB1, and UTP14A. Treatment with the selective SMYD2 inhibitor BAY-598 abrogated the methylation signal, indicating that methylation of these novel substrates was dependent on the catalytic activity of SMYD2 PMID: 27163177
  5. The SMYD2 may promote BMP signaling by directly methylating BMPR2, which, in turn, stimulates BMPR2 kinase activity and activation of the BMP pathway. PMID: 28588028
  6. Knockdown of SMYD2 as well as treatment with a SMYD2 inhibitor in two NSCLC cell lines with an EML4-ALK gene significantly attenuated the phosphorylation levels of the EML4-ALK protein. PMID: 28370702
  7. SMYD2 knockdown confers relative resistance to human AML cells against multiple classes of DNA damaging agents. PMID: 28187429
  8. Substrate crevices of Smyd2 and Smyd3 show distinct features in terms of spatial, hydration, and electrostatic properties that emphasize their characteristic modes of substrates interaction and entry pathways for inhibitor binding. PMID: 27959541
  9. High expression of SMYD2 is associated with chronic lymphocytic leukemia. PMID: 26790435
  10. Study reveals a collection of 10 enriched sequence motifs in Kme1 sites that were identified upon SMYD2 overexpression which were also downregulated in response to SMYD2 knockdown. These findings suggest that these motifs reflect the substrate specificity of SMYD2 in esophageal squamous cell carcinoma cell line. PMID: 26750096
  11. Results show that high expression levels of SMYD2, SETD3, and NO66 in renal cell tumors. Their low expression levels were significantly associated with shorter disease-specific and disease-free survival. PMID: 26488939
  12. Suggest that SMYD2 plays a role in tumor progression and might be a useful prognosticator in HPV-unrelated, nonmultiple head and neck squamous cell carcinomas. PMID: 26826421
  13. SMYD2-mediated methylation negatively regulates PTEN tumor suppressor activity and results in activation of the phosphatidylinositol 3-kinase-AKT pathway. PMID: 25925379
  14. Comprehensive motif-based searches and mutational analysis further established four additional substrates of SMYD2. PMID: 25533488
  15. in addition to esophageal squamous cell carcinoma, SMYD2 is also amplified and/or overexpressed in breast and liver primary tumors PMID: 25825497
  16. a novel mechanism of PARP1 in human cancer through its methylation by SMYD2 PMID: 24726141
  17. SMYD2 has a crucial role in tumor cell proliferation by its overexpression and highlight its usefulness as a prognostic factor and potential therapeutic target in gastric cancer. PMID: 25321194
  18. Data indicate that irect estrogen receptor alpha (ERalpha) methylation by histone methyltransferase SMYD2 regulates estrogen signaling. PMID: 24594358
  19. A novel mechanism for human carcinogenesis via methylation of HSP90AB1 by SMYD2. PMID: 24880080
  20. SMYD2 expression is altered in acute lymphoblastic leukemia bone marrow samples and its high expression was correlated with a bad prognosis. Moreover, SMYD2 expression level significantly decreases in patients that respond to chemotherapy treatment. PMID: 24631370
  21. Findings suggest that SMYD2 (SET and MYND domain containing protein 2), a histone lysine methyltransferase, in embryonic stem (ES) cell differentiation. PMID: 23873367
  22. Data suggest that SMYD2-mediated estrogen receptor alpha (ERalpha) protein methylation and p300/cAMP response element-binding protein-binding protein-dependent ERalpha acetylation play an important role in the estrogen-induced gene expression profiles. PMID: 24101509
  23. -dependent RB1 methylation at lysine 810 promotes cell cycle progression of cancer cells. Further study may explore SMYD2-dependent RB1 methylation as a potential therapeutic target in human cancer. PMID: 22787429
  24. Data report the crystal structure of the full-length human Smyd2 in complex with S-adenosyl-L-homocysteine (AdoHcy). PMID: 21724641
  25. Data highlights the ability of SMYD proteins to form unique protein complexes that may underlie their various biological functions and the SMYD2-mediated methylation of the key molecular chaperone HSP90. PMID: 22028380
  26. SMYD2 has a role in specifically recognizing and regulating functions of p53 tumor suppressor through Lys-370 monomethylation PMID: 21880715
  27. Structural basis of substrate methylation and inhibition of SMYD2 PMID: 21782458
  28. Substrate specificity and product analysis studies established SMYD2 as a monomethyltransferase that prefers nonmethylated p53 peptide substrate. PMID: 21678921
  29. SMYD2 gene expression is decreased in both classic and follicular variants of papillary thyroid carcinoma. PMID: 21509594
  30. RB monomethylation at lysine 860 by SMYD2 provides a direct binding site for L3MBTL1. PMID: 20870719
  31. The combination of the SMYD2 interactome with the gene expression data suggests that some of the genes regulated by SMYD2 are closely associated with SMYD2-interacting proteins. PMID: 18065756
  32. SMYD2 plays an important role in tumor cell proliferation through its activation/overexpression and highlight its usefulness as a prognosticator and potential therapeutic target in ESCC. PMID: 19423649

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Subcellular Location
Cytoplasm, cytosol. Nucleus.
Protein Families
Class V-like SAM-binding methyltransferase superfamily
Database Links

HGNC: 20982

OMIM: 610663

KEGG: hsa:56950

STRING: 9606.ENSP00000355924

UniGene: Hs.66170

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