Recombinant Mouse F-Box Only Protein 32 (FBXO32) Protein (His&Myc)

Name: Recombinant Mouse F-Box Only Protein 32 (FBXO32) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-04926P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse F-Box Only Protein 32 (FBXO32) 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	Q9CPU7
Target Symbol	FBXO32
Synonyms	Fbxo32F-box only protein 32; Atrogin-1; Muscle atrophy F-box protein; MAFbx
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MPFLGQDWRSPGQSWVKTADGWKRFLDEKSGSFVSDLSSYCNKEVYSKENLFSSLNYDVAAKKRKKDIQNSKTKTQYFHQEKWIYVHKGSTKERHGYCTLGEAFNRLDFSTAILDSRRFNYVVRLLELIAKSQLTSLSGIAQKNFMNILEKVVLKVLEDQQNIRLIRELLQTLYTSLCTLVQRVGKSVLVGNINMWVYRMETILHWQQQLNSIQISRPAFKGLTITDLPVCLQLNIMQRLSDGRDLVSLGQAAPDLHVLSEDRLLWKRLCQYHFSERQIRKRLILSDKGQLDWKKMYFKLVRCYPRREQYGVTLQLCKHCHILSWKGTDHPCTANNPESCSVSLSPQDFINLFKF
Expression Range	1-355aa
Protein Length	Full Length
Mol. Weight	48.9 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.
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	Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins during skeletal muscle atrophy. Recognizes TERF1.
Subcellular Location	Cytoplasm. Nucleus.
Database References	KEGG: mmu:67731 STRING: 10090.ENSMUSP00000022986 UniGene: PMID: 28930190 Indoxyl sulfate enhanced the production of atrogin-1 by enhancing oxidative stress in skeletal muscle, leading to muscle atrophy. PMID: 27549031 Valproic acid attenuated muscle wasting and myotube atrophy and reduced C/EBPbeta binding to atrogin1 promoter locus in the myotubes. PMID: 27122162 These results have revealed the roles for atrogin-1 in the regulation of smooth muscle contractility through enhancement of myocardin ubiquitylation/degradation and its transcriptional activity. PMID: 27403897 MAFbx mRNA expression was decreased in old mice relative to adult mice, whereas MuRF1 mRNA expression was less affected by ageing PMID: 26590085 Suggest role for atrogin-1 up-regulation in simvastatin-induced heart mitochondria dysfunction. PMID: 25300705 Atrogin1 was upregulated in cancer cachexia mice. Atrogin1 knockdown protected skeletal muscle cells from TNF-alpha induced atrophy. PMID: 25760630 Expression of USP19 correlates with that of MuRF1 and MAFbx/atrogin-1 in skeletal muscles PMID: 26048142 MAFbx not only regulates protein degradation, but also reduces protein synthesis, exerting a dual role in regulating cardiac mass and preventing from cardiac hypertrophy. PMID: 24650875 mechanical vibration strongly down-regulates atrophy genes myostatin and atrogin-1 both in vivo and in vitro. PMID: 22711460 mTORC1 promotes denervation-induced muscle atrophy through a mechanism involving the activation of FoxO and E3 ubiquitin ligases. PMID: 24570486 atrogin-1 promotes cardiomyocyte health through mediating the interplay between the ubiquitin/proteasome system and autophagy/lysosome system and its alteration promotes development of cardiomyopathies PMID: 24789905 Smad3 expression is sufficient to stimulate atrogin-1 promoter activity, inhibit Akt/mTOR signaling and protein synthesis, and induce muscle fiber atrophy. PMID: 24002653 The muscle wasting effects of the myostatin-atrogin-1 axis are not only limited to the degradation of MyoD and eukaryotic translation initiation factor 3 subunit f, but also encompass several other muscle proteins. PMID: 22673621 Expression of MAFbx/Atrogin-1 and MuRF1 was significantly greater in the plantaris muscle than in the soleus muscle during the early stage of atrophy. PMID: 21901639 C/EBPbeta-/- mice were resistant to Lewis lung cancer-induced atrogin1 upregulation and muscle wasting. Activation of the p38beta MAPK-C/EBPbeta signalling pathway appears to be a key component of cachexia. PMID: 21847090 Downregulation of MAFbx inhibits cardiac hypertrophy in part through stabilization of IkappaB-alpha and inactivation of nuclear factor-kappaB PMID: 21617130 Expression of MAFbx and Bnip3 was increased in hearts of mice in bearing colonic tumors. PMID: 21167183 Myogenin is upregulated in skeletal muscle following denervation and regulates expression of the E3 ubiquitin ligases MuRF1 and atrogin-1, which promote muscle proteolysis and atrophy. PMID: 20887891 Berberine impairs mitochonidrial function stimulating the expression of atrogin-1 without affecting phosphorylation of forkhead transcription factors. PMID: 20522589 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 Data show that slow in vivo release of GHRP-2 through minipump for 24h attenuated the thermal injury-induced increase in mRNA expression of IL-6 and of the E3 ubiquitin ligases, MuRF-1 and MAFbx, in rat skeletal muscle. PMID: 19577604 Data indicate that the SCF(atrogin-1) ubiquitin ligase complex represses calcineurin by targeting it for ubiquitin-mediated proteolysis, leading to inhibition of cardiac hypertrophy in response to pathologic stimuli. PMID: 15489953 MAFbx may play an important role in the course of muscle differentiation by determining the abundance of MyoD PMID: 15531760 activation of atrogin-1 may be a common general adaptation in cells undergoing a rapid reduction in size. PMID: 17008454 Results indicate that atrogin-1 does not affect the activity of Akt itself, but serves as a coactivator for members of the Forkhead family of transcription factors that function downstream of Akt. PMID: 17965779 atrogin-1 may be a critical mediator of the muscle damage induced by statins. PMID: 17992259 Targets the eukaryotic initiation factor 3 subunit 5 (eIF3-f) for ubiquitination and degradation by the proteasome. PMID: 18354498 Although further study is required to establish the causal relationships, downregulation of MAFbx may have reduced MyoD degradation in favor of muscle regeneration. PMID: 18785187 MAFbx targets MyoD for degradation in several models of skeletal muscle atrophy PMID: 19319192 This study demenostrated that the astrogin1 protein is reduced in skeletal muscle of chronic spinal cord-injured patients. PMID: 19533653 Results suggest that MAFbx functions as an F-box protein in the SCF complex for ubiquitination of myogenin. PMID: 19631210

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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.