SET7 (SET9) Antibody (Center)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application ![]()
| WB, IHC-P, E |
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Primary Accession | Q8WTS6 |
Reactivity | Human, Mouse |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 40721 Da |
Antigen Region | 159-189 aa |
Gene ID | 80854 |
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Other Names | Histone-lysine N-methyltransferase SETD7, Histone H3-K4 methyltransferase SETD7, H3-K4-HMTase SETD7, Lysine N-methyltransferase 7, SET domain-containing protein 7, SET7/9, SETD7, KIAA1717, KMT7, SET7, SET9 |
Target/Specificity | This SET7 (SET9) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 159-189 amino acids from the Central region of human SET7 (SET9). |
Dilution | WB~~1:1000 IHC-P~~1:50~100 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | SET7 (SET9) Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | SETD7 |
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Function | Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3 (PubMed:11779497, PubMed:11850410, PubMed:12540855, PubMed:12588998, PubMed:16141209). H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation (PubMed:12540855, PubMed:12588998, PubMed:16141209). Plays a central role in the transcriptional activation of genes such as collagenase or insulin (PubMed:12588998, PubMed:16141209). Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription (PubMed:16141209). Also has methyltransferase activity toward non- histone proteins such as CGAS, p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins (PubMed:15099517, PubMed:15525938, PubMed:16415881, PubMed:35210392). Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II (PubMed:15099517, PubMed:16415881). Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation (PubMed:15525938, PubMed:16415881, PubMed:17108971). Monomethylates 'Lys-491' of CGAS, promoting interaction between SGF29 and CGAS (By similarity). |
Cellular Location | Nucleus. Chromosome |
Tissue Location | Widely expressed. Expressed in pancreatic islets. |

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Background
Similar to acetylation and phosphorylation, histone methylation at the N-terminal tail has emerged as an important role in regulating chromatin dynamics and gene activity. Histone methylation occurs on arginine and lysine residues and is catalyzed by two families of proteins, the protein arginine methyltransferase family and the SET-domain-containing methyltransferase family. Five members have been identified in the arginine methyltransferase family. About 27 are grouped into the SET-domain family, and another 17 make up the PR domain family that is related to the SET domain family. The retinoblastoma protein-interacting zinc finger geneRIZ1 is a tumor suppressor gene and a FOUNDING member of the PR domain family. RIZ1 inactivation is commonly found in many types of human cancers and occurs through loss of mRNA expression, frame shift mutation, chromosomal deletion, and missense mutation. RIZ1 is also a tumor susceptibility gene in mice. The loss of RIZ1 mRNA in human cancers was shown to associate with DNA methylation of its promoter CpG island. Methylation of the RIZ1 promoter strongly correlated with lost or decreased RIZ1 mRNA expression in breast, liver, colon, and lung cancer cell lines as well as in liver cancer tissues.
References
Wysocka, J., et al., Genes Dev. 17(7):896-911 (2003). Xiao, B., et al., Nature 421(6923):652-656 (2003). Kwon, T., et al., EMBO J. 22(2):292-303 (2003). Nishioka, K., et al., Genes Dev. 16(4):479-489 (2002). Wilson, J.R., et al., Cell 111(1):105-115 (2002).

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