Recombinant Human Muscleblind-Like Protein 1 (MBNL1) Protein (His-SUMO)

Name: Recombinant Human Muscleblind-Like Protein 1 (MBNL1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-08661P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Muscleblind-Like Protein 1 (MBNL1) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9NR56
Target Symbol	MBNL1
Synonyms	EXP; EXP35; EXP40; EXP42; KIAA0428; MBNL; MBNL protein; MBNL1; MBNL1_HUMAN; Muscleblind 41kD isoform; Muscleblind like; Muscleblind like protein 1; Muscleblind like splicing regulator 1; Muscleblind-like protein 1; Triplet expansion RNA binding protein; Triplet-expansion RNA-binding protein
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MAVSVTPIRDTKWLTLEVCREFQRGTCSRPDTECKFAHPSKSCQVENGRVIACFDSLKGRCSRENCKYLHPPPHLKTQLEINGRNNLIQQKNMAMLAQQMQLANAMMPGAPLQPVPMFSVAPSLATNASAAAFNPYLGPVSPSLVPAEILPTAPMLVTGNPGVPVPAAAAAAAQKLMRTDRLEVCREYQRGNCNRGENDCRFAHPADSTMIDTNDNTVTVCMDYIKGRCSREKCKYFHPPAHLQAKIKAAQYQVNQAAAAQAAATAAAMGIPQAVLPPLPKRPALEKTNGATAVFNTGIFQYQQALANMQLQQHTAFLPPGSILCMTPATSVVPMVHGATPATVSAATTSATSVPFAATATANQIPIISAEHLTSHKYVTQM
Expression Range	1-382aa
Protein Length	Full Length of Isoform 5
Mol. Weight	53.9 kDa
Research Area	Transcription
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	Mediates pre-mRNA alternative splicing regulation. Acts either as activator or repressor of splicing on specific pre-mRNA targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonizes the alternative splicing activity pattern of CELF proteins. Regulates the TNNT2 exon 5 skipping through competition with U2AF2. Inhibits the formation of the spliceosome A complex on intron 4 of TNNT2 pre-mRNA. Binds to the stem-loop structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Binds to the 5'-YGCU(U/G)Y-3'consensus sequence. Binds to the IR RNA. Binds to expanded CUG repeat RNA, which folds into a hairpin structure containing GC base pairs and bulged, unpaired U residues.
Subcellular Location	Nucleus. Cytoplasm. Cytoplasmic granule. Note=Localized with DDX1, TIAL1 and YBX1 in stress granules upon stress (PubMed:18335541). Localized in the cytoplasm of multinucleated myotubes (PubMed:18335541). Colocalizes with nuclear foci of retained expanded-repeat transcripts in myotubes from patients affected by myotonic dystrophy (PubMed:10970838, PubMed:11590133, PubMed:11929853).
Protein Families	Muscleblind family
Database References	HGNC: 6923 OMIM: 160900 KEGG: hsa:4154 STRING: 9606.ENSP00000282486 UniGene: PMID: 29789616 Functional depletion of the alternative splicing factors Muscleblind-like (MBNL 1 and 2) is at the basis of the neuromuscular disease myotonic dystrophy type 1 (DM1). Here, we screen for miRNAs that regulate MBNL1 and MBNL2 in HeLa cells. We thus identify miR-23b and miR-218, and confirm that they downregulate MBNL proteins in this cell line. PMID: 29946070 For exogenous activation of MBNL transcription, MBNL1 transcription start site T2 seems to be the most suitable target, as the ensuing pre-mRNA is susceptible to both major loops, e1 and e5, and hence, theoretically, following induction each cell in the body could reach the optimal MBNL content. PMID: 28949831 RAN Translation Regulated by Muscleblind Proteins in Myotonic Dystrophy Type 2 PMID: 28910618 Our work suggests that DM1 patients are at risk for Fuchs' endothelial corneal dystrophy (FECD). DMPK mutations contribute to the genetic burden of FECD but are uncommon. We establish a connection between two repeat expansion disorders converging upon RNA-MBNL1 foci and FECD. PMID: 28886202 Binding of the MBNL zinc fingers to cardiac troponin T pre-mRNA is specific and relatively simple, unlike the complex multiple dimer-trimer stoichiometries postulated in some previous studies. PMID: 28718627 Heterozygous missense mutations and one in-frame deletion in MBNL1 were identified in 3 myotonic dystrophy patients. PMID: 27222292 Nuclear retention of full-length HTT RNA is mediated by splicing factors MBNL1 and U2AF65 PMID: 26218986 muscleblind-like 1 (MBNL1) is a robust suppressor of multiorgan breast cancer metastasis. It binds the 3' untranslated regions of DBNL and TACC1 -two genes that are implicated as metastasis suppressors. PMID: 26883358 Sense DMPK RNA foci clearly co-localize with MBNL1 and MBNL2 proteins and accumulate in myotonic dystrophy 1 tissues during development. PMID: 26339785 abnormal splicing of DMD exon 78 found in dystrophic muscles of DM1 patients is due to the functional loss of MBNL1 and leads to the re-expression of an embryonic dystrophin in place of the adult isoform. PMID: 26018658 Reduced RBFOX1 activity in myotonic dystrophy type 1 tissues may amplify several of the splicing alterations caused by the deficiency in MBNL1. PMID: 25211016 MBNL1 binds with C allelic pre-miR-1307 leading to low expression of miR-1307-3p in colorectal cancer. PMID: 25977444 The result is consistent with the hypothesis that MBNL proteins are trapped by expanded CUG repeats and inactivated in myotonic dystrophy type 1 (DM1) and that CELF1 is activated in DM1. PMID: 25403273 Results show that nuclear localization is a major determinant of MBNL1 function. It promotes the nuclear retention of repeat-containing transcripts, which results in repression of aberrant protein expression from the expanded repeats. PMID: 25274774 Results highlight the importance of RNA binding by MBNL Zinc Finger domains 1 and 2 for splicing regulatory activity, even when the protein is artificially recruited to its regulatory location on target RNAs. PMID: 24373687 both MBNL1 and MBNL2 are involved in the regulation of Tau exon 2 splicing and the mis-splicing of Tau in DM1 is due to the combined inactivation of both. PMID: 24440524 MBNL1 and RBFOX2 cooperate to establish a splicing programme involved in pluripotent stem cell differentiation. PMID: 24048253 MBNL1 is highly mobile and changes localization in response to altered transcription and splicing activity, providing an insight into the sensitivity of the lens to changes in MBNL1 distribution. PMID: 24354850 in both dystrophic and sarcopenic muscles MBNL1 undergoes intranuclear relocation, accumulating in its usual functional sites but also ectopically moving to domains which are usually devoid of this protein in healthy adults PMID: 23807294 This report demonistrated that the association of several genetic variants of the MBNL1 gene with DM1 or with the severity of the disease. PMID: 23161457 consistent with a central and negative regulatory role for MBNL proteins in pluripotency, their knockdown significantly enhances the expression of key pluripotency genes and the formation of induced pluripotent stem cells during somatic cell reprogramming PMID: 23739326 MBNL1 loss shows a graded effect on the number and severity of the ensuing RNA splice defects. PMID: 23166594 study suggests that regulation of CUGBP1 and MBNL1 is essential for accurate control of destabilization of a broad spectrum of mRNAs as well as of alternative splicing events PMID: 22355723 It was demonstrated that functionally distinct classes of MBNL1-mediated splicing events exist as defined by requirements for zinc finger-RNA interactions. PMID: 22890842 The present results show that the MBNL1 protein is expressed and more or less sequestered into the CCUGexp nuclear foci also in analyzed non-muscle tissues of DM2 patients. PMID: 22520280 congenital myotonic dystrophy muscle has nuclear foci that contain muscleblind-like 1 (MBNL1) protein. PMID: 22113158 The removal of one pair of zinc fingers greatly impairs the binding affinity of MBNL1, which indicates that the two pairs of zinc fingers might possibly interact with RNA targets cooperatively. PMID: 22106026 Common variants near MBNL1 and NKX2-5 are associated with infantile hypertrophic pyloric stenosis. PMID: 22306654 Expanded CUG repeats Dysregulate RNA splicing by altering the stoichiometry of the muscleblind 1 complex PMID: 21900255 Deletion of the MBNL1 response element eliminated MBNL1 splicing regulation and led to complete inclusion of exon 5, which is consistent with the suppressive effect of MBNL1 on splicing. PMID: 21832083 Although MBNL1 contains four Zn fingers, it appears that only two Zn fingers binding GC motifs are necessary for high affinity RNA binding. PMID: 21548961 MBNL1 regulates pre-miR-1 biogenesis. PMID: 21685920 results indicate the occurrence of a mis-splicing event in myotonic dystrophy type 1 that is induced neither by a loss of muscleblind-like 1 (MBNL1) function nor by a gain of CUGBP1 PMID: 21439371 the abnormally high inclusion of the exon 5 and 7 regions in DM1 is expected to enhance the potential of MBNL1 of being sequestered with nuclear CUG expansions, which provides new insight into DM1 pathophysiology. PMID: 21454535 Findings demonstrate a role for Mbnl1 in controlling insulin receptor exon 11 inclusion via binding to a downstream intronic enhancer element. PMID: 20519504 MBNL proteins promote opposite splicing patterns for cardiac troponin T and insulin receptor alternative exons PMID: 15257297 small interfering RNA-mediated down-regulation of MBNL1 in normal myoblasts results in abnormal insulin receptor splicing PMID: 15546872 The GFP-MBNL1 in CUG and CAG foci have similar half-times of recovery and fractions of immobile molecules, suggesting GFP-MBNL1 is bound by both CUG and CAG repeats and formation of RNA foci and disruption of MBNL1-regulated splicing are separable events. PMID: 15961406 The fact that a human protein works in a Drosophila cellular context illustrates the use of an in vivo test to prove functional conservation. PMID: 16394256 findings show that MBNL1 nuclear sequestration in protein foci is a molecular pathology marker of DM1 and DM2 patients where ribonuclear inclusions of transcripts with expanded CUG/CCUG repeats are also present PMID: 16920640 Elevated levels of MBNL1 show RNA-independent interaction with hnRNP H and dampen the inhibitory activity of increased hnRNP H levels on IR splicing in normal myoblasts. PMID: 16946708 MBNL1 (muscleblind-like protein 1) is an alternative splicing factor that becomes highly concentrated with mutant RNA foci. PMID: 17846170 MBNL may bind all of its RNA substrates, both normal and pathogenic, as structured stem-loops containing pyrimidine mismatches. PMID: 17942744 Examination of dynamics of MBNL1 in response to stress, and suggestion of a role for MBNL1 in mRNA metabolism in the cytoplasm. PMID: 18335541 Both the ZnF3 and the ZnF4 zinc-finger domains target GC steps, with site-specific recognition mediated by a network of hydrogen bonds formed primarily with main chain groups of the protein. PMID: 19043415 MBNL1 and MBNL2 always co-distributed. Functional differences between MBNL1 and MBNL2 have not yet been found PMID: 19095965 Our data seem indicate that the presence of ribonuclear inclusions and MBNL1 nuclear foci are involved in alteration of alternative splicing but do not impair DM2 myogenic differentiation. PMID: 19345584 Data show that ligand 1 selectively destabilizes the MBNL1N-poly(CUG) complex. PMID: 19805260

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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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