Recombinant Human SMYD3 Protein (His & FLAG Tag)

Beta LifeScience SKU/CAT #: BLPSN-4302

Recombinant Human SMYD3 Protein (His & FLAG Tag)

Beta LifeScience SKU/CAT #: BLPSN-4302
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Product Overview

Tag His&FLAG
Host Species Human
Accession NP_001161212.1
Synonym bA74P14.1, KMT3E, ZMYND1, ZNFN3A1
Background SET and MYND domain-containing protein 3, also known as Zinc finger MYND domain-containing protein 1, SMYD3, and ZMYND, is a member of the histone-lysine methyltransferase family. SMYD3 contains oneMYND-type zinc finger and oneSET domain. SMYD3 is a histone H3 lysine-4-specific methyltransferase. It is expressed in skeletal muscles and testis. It is overexpressed in a majority of colorectal carcinoma (CRC) and hepatocellular carcinoma (HCC). SMYD3 plays an important role in transcriptional regulation in human carcinogenesis. It activates the transcription of a set of downstream genes. Of these downstream genes, there are several oncogenes and genes associated with cell adhesion (including those of N-Myc, CrkL, Wnt1b, L-selectin, CD31 and galectin-4), which have been shown to have effects on cell viability, adhesion, migration and metastasis. Increased SMYD3 expression is essential for the proliferation of breast cancer cells. SMYD3 may be a promising new target of therapeutic intervention for the treatment of cancers or other pathological processes associated with cell adhesion and migration.
Description A DNA sequence encoding the human SMYD3 isoform 1 (NP_001161212.1) (Met 1-Ser 428) was fused with the flag tag at the N-terminus. and the Histidine tag at the C-terminus.
Source HEK293
Predicted N Terminal Met
AA Sequence Met 1-Ser 428
Molecular Weight The recombinant human SMYD3 consists of 447 a.a. and predicts a molecular mass of 51.5 kDa. It migrates as an approxiamtely 49 kDa band in SDS-PAGE under reducing conditions.
Purity >70% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile 25mM Tris-HCl, 100mM NaCl, 20% glycerol, 3mM DTT, pH 8.0.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Histone methyltransferase. Specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. Also methylates 'Lys-5' of histone H4. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences.
Subcellular Location Cytoplasm. Nucleus.
Protein Families Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family
Database References
Tissue Specificity Expressed in skeletal muscles and testis. Overexpressed in a majority of colorectal and hepatocellular carcinomas.

Gene Functions References

  1. Study reported for the first time that SMYD3 promoter hypomethylation was associated with colorectal cancer in a Chinese cohort. PMID: 29969917
  2. The property that SMYD3 is preferentially recruited to individual promoters may rely on both its binding sequences and its binding partners. Further investigation is required to clarify this specificity. PMID: 28630472
  3. High Ki67, EZH2, and SMYD3 immunoexpression, adjusted for standard clinicopathological parameters, independently predicts outcome in patients with prostate cancer, at diagnosis. PMID: 29174711
  4. SMYD3 VNTR 3/3 polymorphism confers an increased risk and poor prognosis of hepatocellular carcinoma in a Chinese population PMID: 29691085
  5. EZH2 rs12670401 and rs6464926 polymorphisms, EZH2 and SMYD3 expression, clinical staging, lymph node metastasis, human epidermal growth factor receptor-2 (HER2) status, and metastasis may be correlated with breast cancer susceptibility and prognosis. PMID: 29089464
  6. Overexpression of SMYD3 is an independent prognostic risk of unfavorable prognosis of hepatocellular carcinoma (HCC). The anti-SMYD3 therapy may be a potential approach to treat HCC. PMID: 29187705
  7. SMYD3-mediated methylation of HER2 at Lysine 175 may regulate the formation of HER2 homodimer and subsequent autophosphorylation and suggest that the SMYD3-mediated methylation pathway seems to be a good target for development of novel anti-cancer therapy. PMID: 28639750
  8. SMYD3-mediated methylation of AKT1 at lysine 14 is essential for AKT1 activation and that SMYD3-mediated AKT1 methylation appears to be a good target for development of anti-cancer therapy. PMID: 27626683
  9. However, stratification of patients according to their smoking history significantly expands the prognostic value of SMYD3 to overall survival and other features, suggesting that smoking-related effects saturate the clinical analysis and mask the function of SMYD3 as an oncogenic potentiato PMID: 27554136
  10. SMYD3 enhances tumorigenicity in esophageal squamous cell carcinoma by enhancing transcription of ezrin and LOXL2, which are involved in proliferation, migration, and invasion. PMID: 26980013
  11. SMYD3-mediated H2A.Z.1K101 dimethylation activates cyclin A1 expression and contributes to driving the proliferation of breast cancer cells. PMID: 27569210
  12. VNTR genotype 3/3 of the SMYD3 gene was associated with the risk of ovarian cancer. PMID: 28024138
  13. The present results suggest that NS5A interacts with SMYD3 and induces AP-1 activation, possibly by facilitating binding between HSP90 and SMYD3. This may be a novel mechanism of AP-1 activation in HCV-infected cells. PMID: 27080060
  14. SMYD3 physically interacts with the promoter of BCLAF1 and upregulates its expression by accumulating di- and trimethylation of H3K4 at the BCLAF1 locus. SMYD3 overexpression in bladder cancer cells promotes autophagy activation. PMID: 26676636
  15. High expression of SMYD3 is associated with chronic lymphocytic leukemia. PMID: 26790435
  16. results clearly revealed structural determinants for the substrate preference of SMYD3 and provided mechanistic insights into lysine methylation of MAP3K2. PMID: 26929412
  17. A novel HBx-interacting protein, SMYD3, was identified, leading to proposal of a novel mechanism of AP-1 activation in HBV-infected cells. PMID: 26616333
  18. Postulate that AdoMet cofactor acts like a key and locks Smyd3 in a closed conformation. PMID: 27085704
  19. Results showed that SMYD3 is overexpressed in human glioma and contributes to glioma tumorigenicity through p53. PMID: 26328527
  20. SMYD3 interacts with the human positive coactivator 4 (PC4) and that such interaction potentiates a group of genes whose expression is linked to cell proliferation and invasion. PMID: 26350217
  21. Results support a proto-oncogenic role for SMYD3 in prostate carcinogenesis, mainly due to its methyltransferase enzymatic activity. PMID: 25980436
  22. role of histone methyltransferase SMYD3 in tumors PMID: 25248712
  23. Loss of SMYD3-HSP90 interaction leads to SMYD3 mislocalization within the nucleus, thereby losing its chromatin association. This results in reduction of SMYD3-mediated cell proliferation and, potentially, impairment of SMYD3's oncogenic activity. PMID: 25738358
  24. High SMYD3 and pSTAT3 expressions may indicate poor prognosis of patients with gastric cancer PMID: 25471787
  25. Results suggest that high expression of SMYD3 is related to the occurrence of esophageal squamous cell carcinoma. Also, its suppression promoted the expression of RIZ1 suggesting a signal transduction pathway between SMYD3 and RIZ1. PMID: 24993551
  26. SMYD3 and MMP-9 may play important roles in tumor invasion, metastasis, and prognosis and could work as promising targets for prognostic prediction in gastric cancer. PMID: 25627005
  27. SET and MYND domain-containing protein 3 expression and TGF-beta1 expression in gastric cancer (GC) tissues were significantly and positively correlated. High expression levels of SMYD3 and TGF-beta1 can indicate poor prognoses for GC patients. PMID: 26077602
  28. represent the proof of principle that SMYD3 is a druggable target PMID: 25728514
  29. SMYD3-mediated methylation of MAP3K2 increases mutant K-Ras-induced activation of ERK1/2. (Review) PMID: 25382779
  30. SMYD3 performed an important function in the aggressiveness of gastric carcinoma and may act as a promising target for prognostic prediction. PMID: 25472580
  31. The expression profiling revealed in the more aggressive diseases (i.e. occurrence of metastases; persistent disease; disease-related death) a significant increase of EZH2 and SMYD3 gene expression. PMID: 24813658
  32. Mutational analyses revealed that the MYND-domain of SMYD3 and domain III of hepatitis C virus NS5A are required for the interaction. PMID: 25092459
  33. methylation of MAP3K2 by SMYD3 increases MAP kinase signalling and promotes the formation of Ras-driven carcinomas PMID: 24847881
  34. SMYD3 promotes prostate tumorigenesis and mediates epigenetic upregulation of AR expression. PMID: 24174655
  35. low miR-124 levels mediated by HCV core protein via DNMT1 promote intrahepatic cholangiocarcinoma cell migration and invasion by targeting SMYD3 PMID: 22819820
  36. Depletion of Smyd3 leads to diminished cell proliferation in HeLa cell line. PMID: 22419068
  37. Down-regulation of SMYD3 induces G1-phase cell cycle arrest, indicating the potent induction of apoptosis by SMYD3 knockdown. PMID: 20957523
  38. Results show SMYD3 as an important new regulator of MMP-9 transcription, and provide a molecular link between SMYD3 overexpression and metastatic cancer progression. PMID: 22194464
  39. The structure revealed an overall compact architecture in which the "split-SET" domain adopts a canonical SET domain fold and closely assembles with a Zn-binding MYND domain and a C-terminal superhelical 9 alpha-helical bundle. PMID: 21779408
  40. HCVc could upregulate the methylation status of the RASSF1A promoter through regulation of SMYD3, and histone methylation may affect the DNA methylation of downstream gene by an unknown mechanism PMID: 21450690
  41. Structural analysis shows that the previously uncharacterized C-terminal domain of Smyd3 contains a tetratrico-peptide repeat domain which together with the SET and post-SET domains forms a deep, narrow substrate binding pocket. PMID: 21266482
  42. SmyD3 has a two-lobed structure with the substrate binding cleft located at the bottom of a 15-A-deep crevice formed between the N- and C-terminal lobes. PMID: 21167177
  43. presence of activating KRAS mutations is significantly correlated to an upregulation of 13 genes (adjusted P-value <0.05), among them DUSP4, a MAP-kinase phosphatase, and SMYD3, a histone methyltransferase PMID: 20725992
  44. HBx may induce the expression of histone methyltransferase SMYD3, which in turn stimulates cell proliferation and blocks apoptosis in HepG2 cells. PMID: 19403031
  45. SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells. PMID: 15235609
  46. SMYD3-NY is a novel transcript variant of the SMYD3 gene, and SMYD3-NY protein may influence transcriptional regulation during spermatogenesis via HTMase activity PMID: 16081583
  47. The common variable number of tandem repeats polymorphism in SMYD3 is a susceptibility factor for some types of human cancer. PMID: 16155568
  48. Enhanced SMYD3 expression is associated with growth of breast cancer PMID: 16441421
  49. study shows that SMYD3 polymorphism is not associated with the occurrence and metastasis of hepatocellular carcinoma in Chinese population PMID: 17431393
  50. The proliferation, migration induction and apoptosis inhibition activities of SMYD3 in hepatocellular carcinoma may be mediated through RIZ1 CpG promoter hypermethylation. PMID: 17963297

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