E3 ubiquitin-protein ligase TRIM63 (Trim63), rat, recombinant

Organism: Rattus norvegicus (Rat). Source: E.coli. Expression Region: 1-351aa. Protein Length: Full Length. Tag Info: N-terminal 10xHis-tagged and C-terminal Myc-tagged. Target Protein Sequence: MDYKSGLIPD GNAMENLEKQ LICPICLEMF TKPVVILPCQ HNLCRKCAND IFQAANPYWT NRGGSVSMSG GRFRCPSCRH EVIMDRHGVY GLQRNLLVEN IIDIYKQECS SRPLQKGSHP MCKEHEDEKI NIYCLTCEVP TCSLCKVFGA HQACEVAPLQ SIFQGQKTEL SNCISMLVAG NDRVQTIISQ LEDSCRVTKE NSHQVKEELS HKFDALYAIL DEKKSELLQR ITQEQEEKLD FIEALILQYR EQLEKSTKLV ETAIQSLDEP GGATFLLSAK PLIKSIVEAS KGCQLGKTEQ GFENMDYFTL NLEHIAEALR AIDFGTDEEE EFTEEEEEED QEEGVSTEGH Q. 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 ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells. Catalytic activity S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. EC:2.3.2.27 Pathway: protein ubiquitination This protein is involved in the pathway protein ubiquitination, which is part of Protein modification. Reference: "Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I." Kedar V., McDonough H., Arya R., Li H.-H., Rockman H.A., Patterson C. Proc. Natl. Acad. Sci. U.S.A. 101:18135-18140(2004). Function: nan