Recombinant human KMT5A / SETD8 / Pr-SET7 protein (GST tag N-Terminus)
Recombinant human KMT5A / SETD8 / Pr-SET7 protein (GST tag N-Terminus)
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Recombinant human KMT5A / SETD8 / Pr-SET7 protein (GST tag N-Terminus) is a Human Fragment protein, in the 195 to 352 aa range, expressed in Escherichia coli, with >84%, suitable for SDS-PAGE, FuncS.
別名を表示する
PRSET7, SET07, SET8, SETD8, KMT5A, N-lysine methyltransferase KMT5A, H4-K20-HMTase KMT5A, Histone-lysine N-methyltransferase KMT5A, Lysine N-methyltransferase 5A, Lysine-specific methylase 5A, PR/SET domain-containing protein 07, SET domain-containing protein 8, PR-Set7, PR/SET07
- FuncS
Supplier Data
Functional Studies - Recombinant human KMT5A / SETD8 / Pr-SET7 protein (GST tag N-Terminus) (AB196432)
Specific activity of ab196432.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human KMT5A / SETD8 / Pr-SET7 protein (GST tag N-Terminus) (AB196432)
SDS-PAGE analysis of 7.5 μg of ab196432 on a 4-20% SDS-PAGE gel stained with Coomassie.
Reactivity data
配列情報
出荷温度及び保存条件
出荷温度
短期保存温度
長期保存温度
保管に関する情報
補足情報
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
KMT5A's activity influences several essential cellular processes such as cell cycle progression and DNA repair. As part of a larger chromatin-modulating framework it often functions alongside other chromatin-associated proteins including those from the Polycomb group. It plays a significant role in maintaining genomic stability by marking specific regions of chromatin for certain functions thereby affecting transcription regulation and cellular growth.
Pathways
KMT5A integrates into critical biological mechanisms like the DNA damage response and cell cycle regulation. It links closely with pathways involving p53 and cyclin-dependent kinase (CDK) inhibitors. KMT5A’s histone modification activity influences proteins such as p21 and p16 within the DNA damage signaling network. Its regulatory role here is essential as it facilitates an environment conducive to the DNA repair machinery following genotoxic stress.
製品の性状
製品の状態
Liquid
一般的な情報
機能
Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins (PubMed : 12086618, PubMed : 12121615, PubMed : 15964846, PubMed : 17707234, PubMed : 27338793). Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1) (PubMed : 12086618, PubMed : 12121615, PubMed : 15200950, PubMed : 15933069, PubMed : 15933070, PubMed : 15964846, PubMed : 16517599, PubMed : 27338793). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression (PubMed : 12086618, PubMed : 12121615, PubMed : 15200950, PubMed : 15933069, PubMed : 15933070, PubMed : 15964846, PubMed : 16517599). Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes (PubMed : 12086618, PubMed : 12121615, PubMed : 15200950, PubMed : 15933069, PubMed : 15933070, PubMed : 15964846, PubMed : 16517599). Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis (PubMed : 12086618, PubMed : 12121615, PubMed : 15200950, PubMed : 15933069, PubMed : 15933070, PubMed : 15964846, PubMed : 16517599). Involved in chromosome condensation and proper cytokinesis (PubMed : 12086618, PubMed : 12121615, PubMed : 15200950, PubMed : 15933069, PubMed : 15933070, PubMed : 15964846, PubMed : 16517599). Nucleosomes are preferred as substrate compared to free histones (PubMed : 12086618, PubMed : 12121615, PubMed : 15200950, PubMed : 15933069, PubMed : 15933070, PubMed : 15964846, PubMed : 16517599). Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes (PubMed : 17707234). Plays a negative role in TGF-beta response regulation and a positive role in cell migration (PubMed : 23478445).
配列の類似性
Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. PR/SET subfamily.
翻訳後修飾
Acetylated at Lys-162; does not affect methyltransferase activity. Deacetylated at Lys-162 possibly by SIRT2; does not change methyltransferase activity.. Ubiquitinated and degraded by the DCX(DTL) complex.
細胞内局在性
Nucleus
ターゲットの情報
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