RuvB-like 2 (RUVBL2), human, recombinant

Organism: Homo sapiens (Human). Source: E.coli. Expression Region: 2-463aa. Protein Length: Full Length of Mature Protein. Tag Info: N-terminal 6xHis-SUMO-tagged. Target Protein Sequence: ATVTATTKVP EIRDVTRIER IGAHSHIRGL GLDDALEPRQ ASQGMVGQLA ARRAAGVVLE MIREGKIAGR AVLIAGQPGT GKTAIAMGMA QALGPDTPFT AIAGSEIFSL EMSKTEALTQ AFRRSIGVRI KEETEIIEGE VVEIQIDRPA TGTGSKVGKL TLKTTEMETI YDLGTKMIES LTKDKVQAGD VITIDKATGK ISKLGRSFTR ARDYDAMGSQ TKFVQCPDGE LQKRKEVVHT VSLHEIDVIN SRTQGFLALF SGDTGEIKSE VREQINAKVA EWREEGKAEI IPGVLFIDEV HMLDIESFSF LNRALESDMA PVLIMATNRG ITRIRGTSYQ SPHGIPIDLL DRLLIVSTTP YSEKDTKQIL RIRCEEEDVE MSEDAYTVLT RIGLETSLRY AIQLITAASL VCRKRKGTEV QVDDIKRVYS LFLDESRSTQ YMKEYQDAFL FNELKGETMD TS. Purity: Greater than 90% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 °C/-80 °C. The shelf life of lyophilized form is 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. Relevance: Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (5' to 3') activity, hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. May also inhibit the transcriptional activity of ATF2. Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway where it negatively regulates expression of ER stress response genes. Reference: "Genome-wide screen identifies a novel p97/CDC-48-dependent pathway regulating ER-stress-induced gene transcription."Marza E., Taouji S., Barroso K., Raymond A.A., Guignard L., Bonneu M., Pallares-Lupon N., Dupuy J.W., Fernandez-Zapico M.E., Rosenbaum J., Palladino F., Dupuy D., Chevet E.EMBO Rep. 16:332-340(2015). Function: Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (5' to 3') activity, hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity., FUNCTION