Recombinant Mouse Tripartite Motif-Containing Protein 72 (TRIM72) Protein (His)

Name: Recombinant Mouse Tripartite Motif-Containing Protein 72 (TRIM72) Protein (His)
Brand: Beta LifeScience
SKU: BLC-01443P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Tripartite Motif-Containing Protein 72 (TRIM72) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q1XH17
Target Symbol	TRIM72
Synonyms	Mitsugumin-53;Mg53
Species	Mus musculus (Mouse)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	MSAAPGLLRQELSCPLCLQLFDAPVTAECGHSFCRACLIRVAGEPAADGTVACPCCQAPTRPQALSTNLQLSRLVEGLAQVPQGHCEEHLDPLSIYCEQDRTLVCGVCASLGSHRGHRLLPAAEAQARLKTQLPQQKMQLQEACMRKEKTVAVLEHQLVEVEETVRQFRGAVGEQLGKMRMFLAALESSLDREAERVRGDAGVALRRELSSLNSYLEQLRQMEKVLEEVADKPQTEFLMKFCLVTSRLQKILSESPPPARLDIQLPVISDDFKFQVWKKMFRALMPALEELTFDPSSAHPSLVVSSSGRRVECSDQKAPPAGEDTRQFDKAVAVVAQQLLSQGEHYWEVEVGDKPRWALGVMAADASRRGRLHAVPSQGLWLLGLRDGKILEAHVEAKEPRALRTPERPPARIGLYLSFADGVLAFYDASNPDVLTPIFSFHERLPGPVYPIFDVCWHDKGKNAQPLLLVGPEQEQA
Expression Range	1-477aa
Protein Length	Full Length
Mol. Weight	53.9 kDa
Research Area	Cell Biology
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	Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)-dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles.
Subcellular Location	Cell membrane, sarcolemma. Cytoplasmic vesicle membrane. Note=Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine.
Protein Families	TRIM/RBCC family
Database References	KEGG: mmu:434246 STRING: 10090.ENSMUSP00000079832 UniGene: PMID: 27841305 MG53 is essential to preserve T-tubule integrity and thereby Ca(2+) handling properties and cardiac function under pathological cardiac stress. PMID: 28822805 MG53 is an effective biomarker of myocardial injury and dysfunction in murine hearts. However, MG53 is not expressed in human heart and therefore does not hold utility as a clinical biomarker of myocardial injury PMID: 26790476 TRIM72 directly and indirectly modulates caveolar endocytosis PMID: 26637632 MG53 protein is expressed in lung tissue. PMID: 25034454 Findings indicate that the manifestation of metabolic syndrome alters MG53 activity by reducing its extracellular expression in the serum and causing it to aggregate around mitochondria within striated muscle cells. PMID: 25950605 MG53 is a facilitator of rapid injury repair, a mediator of cell migration, and a modulator of myofibroblast differentiation during wound healing PMID: 26306047 MG53 is a vital component of reno-protection, and targeting MG53-mediated repair of renal proximal tubular epithelium cells represents a potential approach to prevention and treatment of acute kidney injury PMID: 25787762 Zn(2+) interacts with MG53 in protection against injury to the cell membrane PMID: 25869134 MG53-deficient hearts downregulated PPARalpha target genes. MG53 plays a novel role in transcriptional upregulation of PPARalpha and its target genes, resulting in lipid accumulation and lipid toxicity, thereby contributing to diabetic cardiomyopathy. PMID: 25637627 These data suggest an essential role for TRIM72 in repair of alveolar epithelial cells under plasma membrane stress failure. PMID: 25106429 MG53 is an ubiquitin E3 ligase that induces IRS-1 ubiquitination with the help of an E2-conjugating enzyme, UBE2H. PMID: 23965929 MG53 induces FAK ubiquitination with the aid of UBE2H during skeletal myogenesis. PMID: 24344130 TRIM72 regulates cardiac muscle size. PMID: 23567182 MG53 binds to sarcoplasmic reticulum Ca(2+)-ATPase 1a (SERCA1a) via its tripartite motif (TRIM) and PRY domains. PMID: 23103543 muscle-specific mitsugumin 53 mediates the degradation of the insulin receptor and insulin receptor substrate 1 (IRS1), and when upregulated, causes metabolic syndrome featuring insulin resistance, obesity, hypertension and dyslipidaemia PMID: 23354051 MG53 participates in ischemic postconditioning-mediated cardioprotection largely through tethering CaV3 and PI3K and subsequent activation of the RISK pathway. PMID: 21285295 data show that oxidation of the thiol group of Cys242 and leucine zipper-mediated interaction among the MG53 molecules both contribute to the nucleation process for MG53-mediated cell membrane repair PMID: 21525429 membrane-delimited interaction between MG53 and PTRF contributes to initiation of cell membrane repair PMID: 21343302 TRIM72 is a novel antagonist of IRS-1, and is essential as a negative regulator of IGF-induced muscle differentiation. PMID: 20139895 Cholesterol-dependent MG53-mediated membrane repair is a vital, heretofore unappreciated cardioprotective mechanism against a multitude of insults. PMID: 20466981 the synergism of MyoD (or myogenin) and MEF2 is necessary for TRIM72 expression during myogenesis. PMID: 20399744 Co-expression studies indicated that MG53 activity is regulated by a functional interaction with caveolin-3 PMID: 19029292 Intracellular vesicle translocation and Ca(2+)-dependent membrane fusion are distinct steps involved in the repair of membrane damage; MG53 may initiate the assembly of the membrane repair machinery in an oxidation-dependent manner. PMID: 19043407 Suggest MG53 is involved in a constitutive cycle of cell-surface proteins between the plasma membrane and endosome-like vesicles in striated muscle, and also that the vesicular dynamics are essential for the quality control of KV2.1 in cardiomyocytes. PMID: 19202355 Molecular complex formed by MG53, dysferlin, and Cav3 is essential for repair of muscle membrane damage in muscular dystrophy. PMID: 19380584

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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.

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