Recombinant Human E3 Ubiquitin-Protein Ligase Trim63 (TRIM63) Protein (His&Myc)

Name: Recombinant Human E3 Ubiquitin-Protein Ligase Trim63 (TRIM63) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-01669P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human E3 Ubiquitin-Protein Ligase Trim63 (TRIM63) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q969Q1
Target Symbol	TRIM63
Synonyms	Iris RING finger protein;Muscle-specific RING finger protein 1;MuRF-1;MuRF1;RING finger protein 28;RING-type E3 ubiquitin transferase TRIM63;Striated muscle RING zinc finger protein;Tripartite motif-containing protein 63
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MDYKSSLIQDGNPMENLEKQLICPICLEMFTKPVVILPCQHNLCRKCANDIFQAANPYWTSRGSSVSMSGGRFRCPTCRHEVIMDRHGVYGLQRNLLVENIIDIYKQECSSRPLQKGSHPMCKEHEDEKINIYCLTCEVPTCSMCKVFGIHKACEVAPLQSVFQGQKTELNNCISMLVAGNDRVQTIITQLEDSRRVTKENSHQVKEELSQKFDTLYAILDEKKSELLQRITQEQEKKLSFIEALIQQYQEQLDKSTKLVETAIQSLDEPGGATFLLTAKQLIKSIVEASKGCQLGKTEQGFENMDFFTLDLEHIADALRAIDFGTDEEEEEFIEEEDQEEEESTEGKEEGHQ
Expression Range	1-353aa
Protein Length	Full Length
Mol. Weight	47.7 kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 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.

Target Details

Target Function	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.
Subcellular Location	Cytoplasm. Nucleus. Cytoplasm, myofibril, sarcomere, M line. Cytoplasm, myofibril, sarcomere, Z line.
Database References	HGNC: 16007 OMIM: 606131 KEGG: hsa:84676 STRING: 9606.ENSP00000363390 UniGene: PMID: 26738803 the involvement of oxidative stress in the atrophy of COPD peripheral muscle cells in vitro, via the FoxO1/MuRF1/atrogin-1 signaling pathway of the ubiquitin/proteasome system PMID: 27526027 The mitochondrial damage-cGAS-STING-IRF3 pathway is critically involved in metabolic stress-induced endothelial inflammation. PMID: 28302626 Altogether, these results suggest a novel function for p63 as a contributor to muscular atrophic processes via the regulation of multiple genes, including the muscle atrophy gene Trim63. PMID: 26919175 Vitamin D3 might have an inhibitory effect on the expression of MAFbx and MuRF1 in skeletal muscle. PMID: 25876656 MURF1 expression intended to be increased in the skeletal muscle of patients with malignant disease even before cancer related cachexia weight loss. PMID: 25760630 TRIM63 gene expression involved in skin hyperpigmentation. PMID: 25950827 Expression of USP19 correlates with that of MuRF1 and MAFbx/atrogin-1 in skeletal muscles PMID: 26048142 Skeletal muscle atrophy induced by Angiotensin II involves activation of MuRF1 expression. PMID: 26137861 These data strongly supported that rare variants in MuRF1 and MuRF2 are associated with higher penetrance and more severe clinical manifestations of hypertrophic cardiomyopathy. PMID: 24865491 In conclusion, atrogin-1, MuRF1, FOXO1/3A, and eIF3-f mRNA, and protein levels, are differentially regulated by exercise contraction mode but not WPH supplementation combined with hypertrophy-inducing training. PMID: 24458747 Data reveal that Titin protein is a pseudokinase with non-detectable catalytic output but is a high-affinity binding locus for MuRF1. PMID: 24850911 both MuRF1 and MAFbx are enriched in skeletal, cardiac, and smooth muscle--REVIEW PMID: 25096180 SMAD3 regulates transcription of MuRF-1 by increasing FoxO3 binding at a conserved FRE-SBE motif within the proximal promoter region, and by increasing FoxO3 protein content and transcriptional activity. PMID: 24920680 In MuRF1 the COS-box mediates the in vivo targeting of sarcoskeletal structures and points to the pharmacological relevance of the COS domain for treating MuRF1-mediated muscle atrophy. PMID: 24671946 MURF-1 protein gene expression is increased in patients with severe burn injury. PMID: 23816995 Quadriceps muscle MuRF-1 levels did not differ between patients with COPD (with normal or low fat-free mass index) and controls. MURF1 levels were not associated with quadriceps fiber cross-sectional area or strength in patients. PMID: 23844868 Regular exercise training leads to a decrease in Rnf28 expression in skeletal muscle in patients with advanced chronic heart failure. PMID: 22445192 relationship was found between IL-6 and MuRF-1 expression after incubation with PGE2 PMID: 23490068 MuRF-1 RNA expression was significantly increased in malnourished cirrhotic patients vs. well-nourished patients. PMID: 23432902 Data suggest that expression of atrogin-1 and MuRF-1 likely play role in aging-related decrease in muscle mass (i.e., development of sarcopenia); up-regulation of atrogin-1 and MuRF-1 has potential to prevent or reverse sarcopenia. [REVIEW] PMID: 22815045 Human molecular genetic and functional studies identify TRIM63, encoding Muscle RING Finger Protein 1, as a novel gene for human hypertrophic cardiomyopathy. PMID: 22821932 investigation of factors regulating expression of two ubiquitin ligases (MURF1 and MAFbx) in skeletal muscle (i.e., vastus lateralis): effects of resistance exercise and anabolic dietary supplement (i.e., branched-chain amino acids) PMID: 22127230 Data suggest that the inhibition of MuRF1 could be a novel mechanism to prevent or reverse muscle wasting associated with various pathologies. PMID: 21448668 MuRF1 regulates cardiomyocyte cell size and energy metabolism to inhibit cardiac hypertrophy and reverse experimental cardiac hypertrophy. PMID: 21686210 11beta-HSD1 controls glucocorticoid-induced protein degradation in human and murine skeletal muscle via regulation of the E3 ubiquitin ligases Atrogin-1 and MuRF-1. PMID: 21304964 Reduced expression of MuRF1 and MAFbx in the myocardium might permit hypertrophy characteristic of the early post-infarction remodeling phase. PMID: 19859778 atrogin-1 specifically targets truncated M7t-cMyBP-C, but not WT-cMyBP-C, for proteasomal degradation and that MuRF1 indirectly reduces cMyBP-C levels by regulating the transcription of myosin heavy chain. PMID: 19850579 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1. PMID: 11927605 MURF2 associates transiently with microtubules, myosin and titin during sarcomere assembly. PMID: 12414993 MuRF1 functions as a ubiquitin ligase to catalyze ubiquitylation of troponin I through a RING finger-dependent mechanism PMID: 15601779 MuRF1 mRNA expression was significantly increased in quadriceps of patients with COPD; transcriptional regulation of atrogin-1 and MuRF1 may occur via FoxO-1, but independently of AKT PMID: 17478621 Expression of mRNA for MuRF-1 increased approximately 3-fold at 10 days without changes in MAFbx or tripeptidyl peptidase II mRNA, but all decreased between 10 and 21 days of muscle disuse. PMID: 17901116 MuRF-1 and MAFbx, are differently affected by the exercise as well as by repeated exercise PMID: 17971512 Results showed upregulation of MuRf1 and MAFbx in atrophied muscle and support their role as regulatory peptides in various conditions which lead to muscle atrophy. PMID: 17977773 MuRF1 expression in skeletal muscle re-directs glycogen synthesis to the liver and stimulates pancreatic insulin secretion, providing a feedback loop that connects skeletal muscle metabolism with the liver and the pancreas during metabolic stress. PMID: 18468620 These findings present new insights into the role of the glucocorticoid receptor and FOXO family of transcription factors in the transcriptional regulation of the MuRF1 gene PMID: 18612045 Findings aid the future exploration of the cellular function and therapeutic potential of MuRF1. PMID: 18795805 This study demenostrated that the muscle RING finger 1 protein, human is reduced in skeletal muscle of chronic spinal cord-injured patients. PMID: 19533653

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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