E3 ubiquitin-protein ligase TRIM9 (TRIM9), human, recombinant

Organism: Homo sapiens (Human). Source: E.coli. Expression Region: 1-550aa. Protein Length: Full Length of isoform 5. Tag Info: N-terminal 6xHis-SUMO-tagged. Target Protein Sequence: MEEMEEELKC PVCGSFYREP IILPCSHNLC QACARNILVQ TPESESPQSH RAAGSGVSDY DYLDLDKMSL YSEADSGYGS YGGFASAPTT PCQKSPNGVR VFPPAMPPPA THLSPALAPV PRNSCITCPQ CHRSLILDDR GLRGFPKNRV LEGVIDRYQQ SKAAALKCQL CEKAPKEATV MCEQCDVFYC DPCRLRCHPP RGPLAKHRLV PPAQGRVSRR LSPRKVSTCT DHELENHSMY CVQCKMPVCY QCLEEGKHSS HEVKALGAMW KLHKSQLSQA LNGLSDRAKE AKEFLVQLRN MVQQIQENSV EFEACLVAQC DALIDALNRR KAQLLARVNK EHEHKLKVVR DQISHCTVKL RQTTGLMEYC LEVIKENDPS GFLQISDALI RRVHLTEDQW GKGTLTPRMT TDFDLSLDNS PLLQSIHQLD FVQVKASSPV PATPILQLEE CCTHNNSATL SWKQPPLSTV PADGYILELD DGNGGQFREV YVGKETMCTV DGLHFNSTYN ARVKAFNKTG VSPYSKTLVL QTSEGKALQQ YPSERELRGI. 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: E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions and may also participate in the formation or breakdown of abnormal inclusions in neurodegenerative disorders. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the SNARE complex formation. Reference: The tripartite motif family identifies cell compartments.Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L., Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S., Pelicci P.G., Ballabio A.EMBO J. 20:2140-2151(2001). Function: E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions and may also participate in the formation or breakdown of abnormal inclusions in neurodegenerative disorders. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the SNARE complex formation.