Recombinant Human Histone-Lysine N-Methyltransferase Setd7 (SETD7) Protein (His-SUMO&Myc)

Name: Recombinant Human Histone-Lysine N-Methyltransferase Setd7 (SETD7) Protein (His-SUMO&Myc)
Brand: Beta LifeScience
SKU: BLC-02226P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Histone-Lysine N-Methyltransferase Setd7 (SETD7) Protein (His-SUMO&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q8WTS6
Target Symbol	SETD7
Synonyms	FLJ21193; H3 K4 HMTase; H3-K4-HMTase SETD7; H4 lysine 4 specific; Histone H3 K4 methyltransferase; Histone H3 lysine 4 specific methyltransferase; Histone H3-K4 methyltransferase SETD7; Histone H4 K4 methyltransferase; Histone lysine N methyltransferase; Histone lysine N methyltransferase H3 lysine 4 specific SET7; Histone-lysine N-methyltransferase SETD7; KIAA1717; KMT7; Lysine methyltransferase; Lysine N-methyltransferase 7; OTTHUMP00000164543; OTTHUMP00000220049; SET 7; SET 7/9; SET 9; SET D7; SET domain containing (lysine methyltransferase) 7; SET domain containing protein 7; SET domain containing protein 8; SET domain-containing protein 7; SET7; SET7/9; SET9; Setd7; SETD7_HUMAN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His-SUMO&C-Myc
Target Protein Sequence	YKDNIRHGVCWIYYPDGGSLVGEVNEDGEMTGEKIAYVYPDERTALYGKFIDGEMIEGKLATLMSTEEGRPHFELMPGNSVYHFDKSTSSCISTNALLPDPYESERVYVAESLISSAGEGLFSKVAVGPNTVMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFTPNCIYDMFVHPRFGPIKCIRTLRAVEADEELTVAYGYDHSPPGKSGPEAPEWYQVELKAFQATQQK
Expression Range	110--366aa
Protein Length	Partial
Mol. Weight	48.7kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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	HGNC: 30412 OMIM: 606594 KEGG: hsa:80854 STRING: 9606.ENSP00000274031 UniGene: PMID: 30396921 High SET7 expression is associated with hepatocellular carcinoma progression. PMID: 30106440 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 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 the methyltransferase Set9 potentiates TGF-beta signaling by targeting Smad7, an inhibitory downstream effector. PMID: 27292644 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 SETD7 plays a critical role in HCC, and its immunohistochemistry signature provides potential clinical significance for personalized prediction of HCC prognosis. PMID: 27183310 These findings underscore the role of KMT7 as an important monomethyltransferase regulating HIV transcription through Tat. PMID: 27235396 High SET7 expression is associated with breast cancer. PMID: 26779630 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 SET7/SET9-mediated YY1 methylation was shown to be involved in YY1-regulated gene transcription and cell proliferation. PMID: 26902152 These results demonstrate that S...O chalcogen bonds contribute to AdoMet recognition and can enable methyltransferases to distinguish between substrate and product. PMID: 26713889 Reduced expression of SET7 is associated with gastric cancer progression. PMID: 26701885 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 Lysine methylation by SETD7 is important for the fine-tuning of reactive oxygen species signaling through its regulation on pro-inflammatory responses. PMID: 26435321 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 Unleashed expression of Mdm2 in cancer patients with diminished expression of Set7/9 is associated with poor survival outcome. PMID: 26317544 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 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 Set7-induced epigenetic changes contribute to vascular dysfunction in patients with T2DM. PMID: 25472959 SET9 enriches at hypoxia response elements sites of HIF-1 responsive glycolytic genes and stabilizes HIF-1alpha at these sites in hypoxia. PMID: 25637186 Set7/9 is a potential biomarker in tumour cells and is associated with overexpressed E2F1 activity. PMID: 25124555 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 Set7-dependent gene expression changes that occurred independent of H3K4m1 may involve transcription factor lysine methylation events. PMID: 24875254 Results show Set7 efficiently monomethylates Sox2 at K119 residue controling its stability. PMID: 25042802 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 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 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 Methylation of SUV39H1 by SET7/9 results in heterochromatin relaxation and genome instability. PMID: 23509280 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 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 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 The response to hyperglycemia in vascular endothelial cells involves Set7 mediated changes in chromatin remodeling and gene expression. PMID: 22403242 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 Direct evidence for methyl group coordination by carbon-oxygen hydrogen bonds in the lysine methyltransferase SET7/9. PMID: 21454678 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 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 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 SET7/9 catalytic mutants reveal the role of active site water molecules in lysine multiple methylation PMID: 20675860 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 the binding of two SET domain-containing proteins, ALL1 and SET7, to chromatin substrates was studied. PMID: 19752191 purification and functional characterization of a histone H3-lysine 4-specific methyltransferase PMID: 11779497 crystal structure of human SET7/9 shows residues essential for catalytic activity with histone H3 PMID: 12372304 Crystal structure and catalytic mechanism of the human histone methyltransferase SET7/9 PMID: 12540855 This enzyme and human Sin3 deacetylase are tethered together selectively by the cell-proliferation factor HCF-1. PMID: 12670868 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 RBP2 associates with MRG15 complex to maintain reduced H3K4 methylation at transcribed regions, which may ensure the transcriptional elongation state PMID: 17573780 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 Results show that estrogen receptor alpha is directly methylated at lysine 302 (K302) by the SET7 methyltransferase. PMID: 18471979 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.

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