WD repeat domain 5 (WDR5, BIG3, BIG-3, BMP2-induced 3-kb gene protein, SWD3, WD repeat-containing protein 5), Goat

Artikelnummer: USB-W1006-12
Artikelname: WD repeat domain 5 (WDR5, BIG3, BIG-3, BMP2-induced 3-kb gene protein, SWD3, WD repeat-containing protein 5), Goat
Artikelnummer: USB-W1006-12
Hersteller Artikelnummer: W1006-12
Alternativnummer: USB-W1006-12-100
Hersteller: US Biological
Wirt: Goat
Kategorie: Antikörper
Applikation: WB
Immunogen: Recombinant human WDR5, aa1-120.
WDR5 (WD repeat-containing protein 5, also BMP2-induced 3 kb gene protein/BIG3) is a nuclear, 36-40kD monomeric member of the WD family of repeat proteins. It is known to be expressed in osteoblasts, osteocytes and chrondrocytes, among other cells, and appears to serve as a structural organizer for the histone methyltransferase MLL1 complex. This complex methylates histone H3, and within this complex, WDR5 binds to mono- or dimethylated histone H3 and serves as an anchor for complex subunits RbBP5, Ash2L and MLL1. Human WDR5 is 334 amino acids in length. It contains seven WD domains (aa43-333) that likely participate in protein-protein interactions, plus a phosphorylation site at Ser267. There are three isoform variants for WDR5. Human and mouse WDR5 are absolutely identical in aa sequence. Applications: Suitable for use in Western Blot. Other applications not tested. Recommended Dilution: Western Blot: 1ug/ml Optimal dilutions to be determined by the researcher. Storage and Stability: Lyophilized powder may be stored at -20C. Stable for 12 months at -20C. Reconstitute with sterile ddH2O, sterile 40-50% glycerol, 0.02% sodium azide, aliquot and store at -20C. Reconstituted product is stable for 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
UniProt: P61964
Reinheit: Purified by immunoaffinity chromatography.
Formulierung: Supplied as a lyophilized powder in PBS, 5% trehalose. Reconstitute with 500ul sterile PBS.