Recombinant Human SETD7 Protein

Beta LifeScience SKU/CAT #: BL-0215SG

Recombinant Human SETD7 Protein

Beta LifeScience SKU/CAT #: BL-0215SG
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Product Overview

Tag GST
Host Species Human
Accession NM_030648
Synonym FLJ21193; KIAA1717; KMT7; SET7; SET7/9; SET9
Background SETD7 or SET domain containing lysine methyltransferase 7 is a lysine methyltransferase which can methylates lysine-4 (K4) in histone H3 in vitro and in vivo. Methylation of K4 in histone H3 by SETD7 and methylation of K9 in histone H3 by SUV39H1 were found to have differential effects on subsequent histone acetylation by p300 (1). SETD7 can also methylate p53 at lys372 within the C-terminal regulatory region (2). Methylated p53 is restricted to the nucleus and the modification positively affects its stability. SETD7 regulates the expression of p53 target genes in a manner dependent on the p53 methylation site.
Description Recombinant full-length human SETD7 was produced by baculovirus in Sf9 insect cells, fused with a GST tag at N-terminus. This protein is purified with our unique purification methods.
Source Sf9 insect cells
AA Sequence Full Length
Molecular Weight ~75 kDa
Purity For specific purity information on a given lot, see related COA.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Active
Formulation Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability The recombinant protein is stable for up to 12 months at -70°C
Usage For Research Use Only
Storage Recombinant Human SETD7 Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation.
Subcellular Location Nucleus. Chromosome.
Protein Families Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, SET7 subfamily
Database References
Tissue Specificity Widely expressed. Expressed in pancreatic islets.

Gene Functions References

  1. Setd7 KD impacted a larger set of genes and caused a higher fold change compared to PEITC treatment. This study offers new insights into the mechanisms of action of the epigenetic modifier Setd7 and the effects of PEITC treatment in PCa cells and enhances our understanding of the potential cancer preventive/treatment effects of isothiocyanate compounds such as PEITC in PCa. PMID: 30396921
  2. High SET7 expression is associated with hepatocellular carcinoma progression. PMID: 30106440
  3. SET7/9 expression in nonadherent cells isolated from the effluent of peritoneal dialysis (PD) patients. SET7/9 expression was elevated in nonadherent cells isolated from the effluent of PD patients. SET7/9 expression was positively correlated with dialysate/plasma ratio of creatinine in PD patients. PMID: 29723250
  4. Methylation at K436 and K595 respectively by Set7 increases the stability and DNA binding ability of Gli3, resulting in an enhancement of Shh signaling activation. PMID: 27146893
  5. the methyltransferase Set9 potentiates TGF-beta signaling by targeting Smad7, an inhibitory downstream effector. PMID: 27292644
  6. SET9 expression levels were significantly higher in samples from patients with pathological complete remission than in samples from patients with disease recurrence, which indicates that SET9 acts as a tumor suppressor in breast cancer and that its expression may serve as a prognostic marker for malignancy. PMID: 27132511
  7. SETD7 plays a critical role in HCC, and its immunohistochemistry signature provides potential clinical significance for personalized prediction of HCC prognosis. PMID: 27183310
  8. These findings underscore the role of KMT7 as an important monomethyltransferase regulating HIV transcription through Tat. PMID: 27235396
  9. High SET7 expression is associated with breast cancer. PMID: 26779630
  10. SET7 was required for GATA1-induced breast tumor angiogenesis and growth in nude mice. GATA1 and SET7 are independent poor prognostic factors in breast cancer. PMID: 26848522
  11. SET7/SET9-mediated YY1 methylation was shown to be involved in YY1-regulated gene transcription and cell proliferation. PMID: 26902152
  12. These results demonstrate that S...O chalcogen bonds contribute to AdoMet recognition and can enable methyltransferases to distinguish between substrate and product. PMID: 26713889
  13. Reduced expression of SET7 is associated with gastric cancer progression. PMID: 26701885
  14. study identified a novel locus associated with serum lycopene concentrations and results raise a number of possibilities regarding the nature of the relationship between SETD7 and lycopene, both independently associated with prostate cancer. PMID: 26861389
  15. Lysine methylation by SETD7 is important for the fine-tuning of reactive oxygen species signaling through its regulation on pro-inflammatory responses. PMID: 26435321
  16. Knock-down of SETD7 causes differentiation defects in human embryonic stem cell including delay in both the silencing of pluripotency-related genes and the induction of differentiation genes. PMID: 26890252
  17. Unleashed expression of Mdm2 in cancer patients with diminished expression of Set7/9 is associated with poor survival outcome. PMID: 26317544
  18. Based on our results miR-153 inhibits proliferation and suppresses EMT and the invasive potential of ovarian cancer cells through downregulation of SET7 and ZEB2, supporting the pursuit of miR-153 as a potential target for ovarian cancer intervention. PMID: 25954928
  19. Findings indicate the regulation of Wnt/beta-catenin signaling and the role of SET domain-containing protein 7/9 (SET7/9) in cancer cells. PMID: 26116705
  20. Set7-induced epigenetic changes contribute to vascular dysfunction in patients with T2DM. PMID: 25472959
  21. SET9 enriches at hypoxia response elements sites of HIF-1 responsive glycolytic genes and stabilizes HIF-1alpha at these sites in hypoxia. PMID: 25637186
  22. Set7/9 is a potential biomarker in tumour cells and is associated with overexpressed E2F1 activity. PMID: 25124555
  23. Results show that histone-lysine N-methyltransferase Set7 facilitates hepatitis C virus (HCV) replication through the attenuation of interferon-alpha (IFN-alpha) signaling pathways and IFN-related effectors. PMID: 25681344
  24. Set7-dependent gene expression changes that occurred independent of H3K4m1 may involve transcription factor lysine methylation events. PMID: 24875254
  25. Results show Set7 efficiently monomethylates Sox2 at K119 residue controling its stability. PMID: 25042802
  26. study indicates that Set7/9 prevents the histone deacetylase activity of SirT1, potentiating euchromatin formation on the promoter site of COL2A1 and resulting in morphology-dependent COL2A1 gene transactivation. PMID: 23873758
  27. Vesicular stomatitis virus and influenza A virus increased IFITM3-K88me1 levels by promoting the interaction between IFITM3 and SET7, suggesting that this pathway could be hijacked to support infection; conversely, IFN-alpha reduced IFITM3-K88me1 levels. PMID: 24129573
  28. The crystal structures presented here provide information about the binding of both AdoMet-analogue inhibitors and peptides by the SET domain of SET7/9. PMID: 23519668
  29. Methylation of SUV39H1 by SET7/9 results in heterochromatin relaxation and genome instability. PMID: 23509280
  30. The methyltransferase Set9 directly methylates FoxO3 in vitro and in cells. The modulation of FoxO3 stability and activity by methylation may be critical for fine-tuning cellular responses to stress stimuli. PMID: 22820736
  31. H3K4me3 level defines unrecognized subsets of heptaocellular carcinoma patients with distinct epigenetic phenotype and clinical outcome and can thus be a novel predictor for poor prognosis of heptaocellular carcinoma patients PMID: 22406368
  32. simulations show that while the wild-type SET7/9 is a monomethylase, the Y245-->A mutation increases the ability of the enzyme to add more methyl groups on the target lysine PMID: 22242964
  33. The response to hyperglycemia in vascular endothelial cells involves Set7 mediated changes in chromatin remodeling and gene expression. PMID: 22403242
  34. genetic association studies in a Finnish population with type I diabetes: No associations were found between SNPs in SETD7 and the diabetic complications studied. PMID: 21896933
  35. Direct evidence for methyl group coordination by carbon-oxygen hydrogen bonds in the lysine methyltransferase SET7/9. PMID: 21454678
  36. Set9 directly acts on AR at the amino acid level. Chromatin recruitment of Set9 to AREs is suggestive of its additional role as a transcriptional coactivator. PMID: 21273441
  37. Data show that STAT3 binds to the SOCS3 promoter, and S727 is then phosphorylated, followed by the coincident binding of SET9 and dimethylation of K140, and lastly by the binding of LSD1. PMID: 21098664
  38. results reveal that Set7/9 is a critical regulator of the SIRT1-p53 interaction and suggest that Set7/9 can modulate p53 function indirectly in addition to acting through a methylation-dependent mechanism PMID: 21245319
  39. SET7/9 catalytic mutants reveal the role of active site water molecules in lysine multiple methylation PMID: 20675860
  40. Set7/9-KMT7 associates with the HIV promoter in vivo and monomethylates lysine 51, a highly conserved residue located in the RNA-binding domain of Tat. PMID: 20227666
  41. the binding of two SET domain-containing proteins, ALL1 and SET7, to chromatin substrates was studied. PMID: 19752191
  42. purification and functional characterization of a histone H3-lysine 4-specific methyltransferase PMID: 11779497
  43. crystal structure of human SET7/9 shows residues essential for catalytic activity with histone H3 PMID: 12372304
  44. Crystal structure and catalytic mechanism of the human histone methyltransferase SET7/9 PMID: 12540855
  45. This enzyme and human Sin3 deacetylase are tethered together selectively by the cell-proliferation factor HCF-1. PMID: 12670868
  46. SET7/9 recognizes a conserved K/R-S/T/A motif preceding the lysine substrate and has a propensity to bind aspartates and asparagines on the C-terminal side of the lysine target PMID: 16415881
  47. RBP2 associates with MRG15 complex to maintain reduced H3K4 methylation at transcribed regions, which may ensure the transcriptional elongation state PMID: 17573780
  48. Results suggest that the cross talk between lysine methylation and acetylation is critical for p53 activation in response to DNA damage and that Set7/9 may play an important role in tumor suppression. PMID: 17646389
  49. Results show that estrogen receptor alpha is directly methylated at lysine 302 (K302) by the SET7 methyltransferase. PMID: 18471979
  50. This report shows that H3K9 monomethylation is dependent upon the PR-Set7 H4K20 monomethyltransferase but independent of its catalytic function, indicating that PR-Set7 recruits an H3K9 monomethyltransferase to establish the trans-tail histone code. PMID: 18474616

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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