Recombinant Human SETD7/SET7/9 Protein (His Tag) (PKSH031208)

For research use only.
Synonyms | KMT7, SET7, SET7/9, SET9 |
Species | Human |
Expression Host | E.coli |
Sequence | Asp 2-Lys 366 |
Accession | NP_085151.1 |
Calculated Molecular Weight | 41.5 kDa |
Observed Molecular Weight | 48 kDa |
Tag | N-His |
Bio-activity | Not validated for activity |
Purity | > 94 % as determined by reducing SDS-PAGE. |
Endotoxin | Please contact us for more information. |
Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
Formulation |
Lyophilized from sterile PBS, pH 7.4 Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
Reconstitution | Please refer to the printed manual for detailed information. |
Background | Histone-lysine N-methyltransferase SETD7, also known as SET domain containing (lysine methyltransferase) 7, SET7/9, Histone H3-K4 methyltransferase SETD7, H3-K4-HMTase SETD7, and SETD7, is a member of thehistone-lysine methyltransferase family and SET7 subfamily. SETD7 is widely expressed and expressed in pancreatic islets. SETD7 contains three MORN repeats and one SET domain. SETD7 plays a central role in the transcriptional activation of genes such as collagenase or insulin. As a protein lysine methyltransferase (PKMT), SETD7 also has methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding in substrate proteins. The mono-methyltransferase activity of SETD7 is achieved by disrupting the formation at near-attack conformations for the dimethylation reaction. SETD7 is also a novel coactivator of NF-kappaB and plays a role in inflammation and diabetes. |
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