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

Name: Recombinant Rat E3 Ubiquitin-Protein Ligase Trim63 (TRIM63) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-01881P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Rat 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 90% as determined by SDS-PAGE.
Uniprotkb	Q91Z63
Target Symbol	TRIM63
Synonyms	Muscle-specific RING finger protein 1 RING-type E3 ubiquitin transferase TRIM63 Tripartite motif-containing protein 63
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MDYKSGLIPDGNAMENLEKQLICPICLEMFTKPVVILPCQHNLCRKCANDIFQAANPYWTNRGGSVSMSGGRFRCPSCRHEVIMDRHGVYGLQRNLLVENIIDIYKQECSSRPLQKGSHPMCKEHEDEKINIYCLTCEVPTCSLCKVFGAHQACEVAPLQSIFQGQKTELSNCISMLVAGNDRVQTIISQLEDSCRVTKENSHQVKEELSHKFDALYAILDEKKSELLQRITQEQEEKLDFIEALILQYREQLEKSTKLVETAIQSLDEPGGATFLLSAKPLIKSIVEASKGCQLGKTEQGFENMDYFTLNLEHIAEALRAIDFGTDEEEEFTEEEEEEDQEEGVSTEGHQ
Expression Range	1-351aa
Protein Length	Full Length
Mol. Weight	47.2 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	KEGG: rno:140939 STRING: 10116.ENSRNOP00000058869 UniGene: Rn.40636
Tissue Specificity	Muscle specific. Selectively expressed in heart and skeletal muscle.

Gene Functions References

Exercise down-regulated the mRNA levels of murf1 and atrogin-1, decreased reactive oxygen species level, increased antioxidant capacity, regulated the expression of insulin-like growth factor 1 (IGF1), mechano growth factor (MGF), Neuregulin1 (NRG1) and Myostatin (MSTN), and activated Akt and Erk1/2 signalings in soleus muscle. PMID: 30312703
UBE2D2 is not the cognate ubiquitinating enzyme for MuRF1 PMID: 27378730
Data suggest that FOXO3a plays a role in muscle atrophy through regulation of expression of MuRF1 and atrogin-1 in skeletal muscle in Cushing's syndrome. (FOXO3a = forkhead box protein O3a; MuRF1 = muscle-specific RING finger protein 1) PMID: 28246104
Independent of the metabolic condition, after muscle contraction, both TRIM63 and FBXO32 proteins correlated significantly with miR-1-3p, miR-29a/b-3p, and miR-133a/b-3p. PMID: 28000044
The muscles also showed significantly contrasting transcriptional regulation of the microRNAs miR-1 and miR-206. MuRF1 and Atrogin-1 showed the highest levels of expression in the denervated gastrocnemius muscle PMID: 26691660
MuRF1 and MuRF2 translocate to the nuclei in the soleus muscle during gravitational unloading. PMID: 25868327
Data from model of hypertensive heart disease suggest expression of E3 ubiquitin ligases (muscle RING-finger protein-1; atrogin-1) are upregulated in cardiomyocytes as left ventricle hypertrophy develops and down-regulated if hypertrophy prevented. PMID: 24084216
Suppression of atrogin-1 resulted in increased expression of MuRF1. PMID: 23866982
miR-19a/b family regulates phenotypes of cardiomyocytes via suppression of multiple direct target genes such as murf-1. PMID: 24117217
Branched-chain amino acids attenuated atrogin-1 and MuRF1 protein levels induced by hindlimb suspension. PMID: 23084640
Ligustrazine may postpone denervated skeletal muscle atrophy by reducing mRNA and protein expressions of FoXO3a, MAFbx, and MuRF1. PMID: 22702057
Diabetes modulated the expression of MuRF1 leading to muscle wasting, and the mechanism might be involved with oxidative stress. PMID: 21826997
recombinant GST-MuRF1 physically interacted and polyubiquitinylated actin in vitro and that MuRF1 is a critical component for actin breakdown, since MuRF1 siRNA stabilized flag-actin PMID: 21764995
AMPK regulates the transcription of Atrogin-1 and MuRF1 and enhances UPS-mediated protein degradation in heart. PMID: 21921267
Exercise training diminished the skeletal muscle wasting in diabetic rats by decreasing oxidative stress and inhibiting MuRF1 expression at both the mRNA and protein levels. PMID: 21620866
Heart failure induces fiber type IIB specific atrophy, up-regulating atrogin-1 and MuRF1 mRNA expression in extensor digitorum longus muscle of monocrotaline treated rats. PMID: 20349269
Dietary fish oil prior to and during immobilization may alleviate the immobilization-induced soleus muscle atrophy, at least in part, via the Akt pathway through E3 ubiquitin ligases and p70s6k. PMID: 20555375
Persistent over-expression of MAFbx and MuRF1 mRNA after muscle transfer has a close relationship with muscle atrophy and muscle dysfunction. PMID: 19803207
atrogin-1 and MuRF1 are upregulated in experimental hyperthyroidism in rats PMID: 19777444
MafBx and Murf mRNA are up-regulated in response to LPS and might play a role in the muscle proteolysis observed PMID: 12782319
IGF-1/Akt and TNFalpha represent potential mediators implicated in the regulation of MuRF1 and atrogin-1 genes during aging PMID: 16949134
Murf1 in muscle atrophy caused by blocked neuromuscular transmission and muscle unloading is described. PMID: 17622304
The antioxidant Trolox attenuates mechanical ventilation-induced diaphragmatic atrophy independent of alterations in Akt regulation of FoxO transcription factors and expression of MAFbx or MuRF-1. PMID: 17916612
the regulation by glucocorticoids of MuRF1 and the role of the GR may be different in L6 (a rat cell line) and C2C12 (a mouse cell line) myotubes PMID: 18615595
the transcriptional activities of Foxo3a and NF-kappaB, which are implicated in the regulation of atrogin-1 and MuRF1, were abolished by Hsp70 PMID: 18644837
Ghrelin inhibits skeletal muscle protein breakdown in rats with thermal injury through normalizing elevated expression of E3 ubiquitin ligases MuRF1 and MAFbx. PMID: 19211729

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.