Recombinant Mouse Myelin Basic Protein (MBP) Protein (His)

Name: Recombinant Mouse Myelin Basic Protein (MBP) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00419P
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 Myelin Basic Protein (MBP) 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	P04370
Target Symbol	MBP
Species	Mus musculus (Mouse)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	MGNHSGKRELSAEKASKDGEIHRGEAGKKRSVGKLSQTASEDSDVFGEADAIQNNGTSAEDTAVTDSKHTADPKNNWQGAHPADPGNRPHLIRLFSRDAPGREDNTFKDRPSESDELQTIQEDPTAASGGLDVMASQKRPSQRSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFSGDRGAPKRGSGKDSHTRTTHYGSLPQKSQHGRTQDENPVVHFFKNIVTPRTPPPSQGKGGRDSRSGSPMARR
Expression Range	1-250aa
Protein Length	Full Length
Mol. Weight	29.2 kDa
Research Area	Others
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	The classic group of MBP isoforms (isoform 4-isoform 13) are with PLP the most abundant protein components of the myelin membrane in the CNS. They have a role in both its formation and stabilization. The non-classic group of MBP isoforms (isoform 1-isoform 3/Golli-MBPs) may preferentially have a role in the early developing brain long before myelination, maybe as components of transcriptional complexes, and may also be involved in signaling pathways in T-cells and neural cells. Differential splicing events combined to optional post-translational modifications give a wide spectrum of isomers, with each of them potentially having a specialized function.
Subcellular Location	[Isoform 13]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; [Isoform 12]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; [Isoform 11]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; [Isoform 10]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; [Isoform 9]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; [Isoform 8]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; [Isoform 7]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; [Isoform 6]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; [Isoform 5]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; [Isoform 4]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; [Isoform 3]: Cytoplasm. Nucleus.; [Isoform 2]: Cytoplasm. Nucleus.; [Isoform 1]: Cytoplasm. Nucleus.
Protein Families	Myelin basic protein family
Database References	KEGG: mmu:17196 STRING: 10090.ENSMUSP00000046185 UniGene: PMID: 29111742 golli-KO mice display abnormal behavior including deficits in episodic memory and reduced anxiety. PMID: 26497031 The Mbp(+/-) mice exhibited defects of sensorimotor gating, as evidenced by reduced prepulse-inhibition, and a late-onset catatonia phenotype. PMID: 27470661 myelin basic protein (MBP) is inhibitory to both primitive neural stem cells and definitive neural stem cells derived colony formation. PMID: 27573615 CNP directly associates with and organizes the actin cytoskeleton, thereby providing an intracellular strut that counteracts membrane compaction by myelin basic protein (MBP). PMID: 28076777 to further characterize the mechanism regulating mbp transcription, study defined M3 structure/function relationships; multiple M3 regulatory element combinations were found to drive expression in oligodendrocytes and Schwann cells with a minimal 129 bp sequence conferring expression in oligodendrocytes throughout myelin elaboration, maintenance and repair PMID: 26507463 Results show the expression of sncRNA715 in Schwann cells and its inverse correlation with Mbp mRNA in cultured cells and the sciatic nerve. Its inhibitory effect on MBP was confirmed in differentiating primary Schwann cells. PMID: 26317513 Results suggest that GAL is a regulator of myelination, as demonstrated by MBP synthesis, and may be one of the myelination promoters PMID: 25450959 Data indicate that 18.5 kDa myelin basic protein (MBP) segment upstream of the primary SH3-ligand is involved in interaction. PMID: 25343306 Data suggest that prenatal alterations in expression of various fetal brain proteins (including up-regulation of Mbp) are associated with aberrant behavioral characteristics of transgenic mice that model autism-like behavior. PMID: 25849768 Data suggest that hybrid protein composed of two different Myelin basic protein (MBP) isoforms (TandeMBP) might become a tool for in vitro assays to analyse various protein kinase activities. PMID: 24713852 Data indicate a role for myelin basic protein (MBP) isoforms in protein-protein interactions during membrane and cytoskeletal extension and remodeling in oligodendrocytes (OLGs). PMID: 24956930 Disappearance of 21.5 pMBP corresponded to demyelination and its reappearance corresponded to prevention of demyelination. PMID: 24459152 Golli-BG21 enhanced SCP1/GIP phosphatase activity, whereas PKCalpha-phosphorylated BG21 inhibited its activity, suggesting a potential role of BG21 as a molecular switch ("quick-brake mechanism") on SCP1/GIP. PMID: 24751520 MBP expression in cultured Fmr1 KO oligodendrocytes is similar to wild type, and expression of MBP in brain homogenates of the Fmr1 KO mouse to be similar to wild type. PMID: 23891804 myelin basic protein drives myelin biogenesis using weak forces arising from its inherent capacity to phase separate. PMID: 23762018 Myelin basic protein-21.5 kDa in the nucleus promotes oligodendrocyte proliferation, while melin basic protein-18.5-kDa in plasma membrane does not. PMID: 23184356 21.5-kDa MBP contains two non-traditional PY-nuclear-localization signals, and arginine and lysine residues within these motifs were involved in subcellular trafficking of this protein to the nucleus, where it may have functional roles during myelinogenesis. PMID: 22609403 Loss of MBP is associated with aging and hearing loss. PMID: 22496821 Myelin basic protein (MBP) performs distinct actions on the formation, maturation, degeneration and regeneration of sciatic nerve myelin sheath. PMID: 21824506 Regulation of the Mbp gene, along with the relative amount of expressed Mbp protein, suggests that the immortalized cell lines containing them are representative of immature oligodendrocytes. PMID: 21472765 The results of this study suggested that MBP's SH3 ligand domain plays a key role in intracellular protein interactions in vivo and may be required for proper membrane elaboration of developing oligodendrocytes. PMID: 21887699 Molecular dynamics simulations were conducted to investigate the conformation of the immunodominant epitope of acetylated myelin basic protein residues 1-11 and its altered peptide ligands, mutated at position 4 to an alanine or a tyrosine residue. PMID: 22042377 define hnRNP F as a regulatory element of MBP expression in oligodendrocytes and imply an important function of hnRNP F in the control of myelin synthesis. PMID: 22128153 there is an N-terminal binding domain in MBP for Ca(2+)-CaM PMID: 21889463 Human umbilical cord blood-derived mesenchymal stem cells upregulate myelin basic protein in shiverer mice. PMID: 20925478 our data indicate a key role for golli proteins in the regulation of TRPC-mediated Ca(2+) influx PMID: 21389218 The density of high-voltage-activated currents is reduced in oligodendroglial precursor cells recorded in golli-deficient tissue, while low-voltage-activated currents remain unaltered in these cells. PMID: 20607717 The QKI-6 RNA binding protein localizes with the MBP mRNAs in stress granules of glial cells. PMID: 20862255 These results are the first to provide atomic-level detail of a membrane-anchoring segment of MBP. PMID: 20713009 Secondary structure and solvent accessibility of a calmodulin-binding C-terminal segment of membrane-associated myelin basic protein. PMID: 20831157 When MBP was reconstituted with myelin-mimetic membranes, there was a rearrangement of secondary structure components upon addition of zinc. PMID: 20169373 results provide a detailed picture of the MBP-CaM interaction, including a 3D model of the complex between full-length proteins PMID: 19855925 the divalent cations copper and zinc induce a compaction of the extended myelin basic protein in vitro, suggestive of a tertiary conformation that may reflect its arrangement in myelin. PMID: 19903451 helical tubular vesicles were formed by binary monolayers containing a nickel-chelating lipid and phosphoinositides in the presence of myelin basic protein PMID: 11841829 Myelin basic protein has a role in contact-mediated expression of inducible Nitric Oxide Synthase in microglial cells PMID: 12176974 calmodulin-binding properties of N- and C-terminal deletion mutants of MBP PMID: 12901870 MBP has an alpha-helix tilted 9 degrees, and the central lysine is positioned for side-chain interaction with the negatively charged phospholipid head groups PMID: 14630913 role in expression of insulin-like growth factor 1 PMID: 15139287 electron paramagnetic resonance of MBP-CaM interactions PMID: 15522783 An enhancer 9.0 kb upstream of Mbp (MbpSCE1) activates Mpz specifically in Schwann cells in transgenic mice. MbpSCE1 is active in both Schwann cells and oligodendrocytes, but by diverse mechanisms. PMID: 15525335 Fyn plays critical roles in promoting accelerated MBP expression during myelinogenesis in a MBP isoform-preferential manner, and QKI may act in the same pathway downstream of Fyn for MBP mRNA homeostasis PMID: 15528192 Taken together, these results demonstrate that microglia and/or microglia secreted factors, are necessary for the LPS-promoted proliferation of OPCs and suggest possible involvement of Golli proteins as one of mediators in this process. PMID: 15546149 Deimination of MBP, a posttranslational modification which occurs early in life, attenuates the ability of MBP to polymerize and bundle actin, and to bind it to a negatively charged membrane. PMID: 15736962 microglial activation of C/EBPbeta but not NF-kappaB by T cell:microglial contact is a gender-specific event, resulting in the inability of male MBP-primed T cells to induce microglial expression of proinflammatory molecules PMID: 16046404 role for golli proteins in oligodendrocyte differentiation, migration, and/or myelin elaboration in the brain PMID: 16049176 Transient transfections with a luciferase reporter gene driven by the myelin basic protein promoter define how changes in the molecular composition of these transcriptional complexes modulate myelin gene expression. PMID: 16148239 discovered epitope-specific antibody-mediated degradation of MBP suggests a mechanistic explanation of the slow development of neurodegeneration associated with multiple sclerosis PMID: 16387849 These results demonstrate that both STOP and MBP function as microtubule-stabilizing proteins in differentiating oligodendrocytes and could be important for the PMID: 16773649 Golli-deficient T cells were hyperproliferative and showed enhanced calcium entry upon T cell receptor stimulation. PMID: 16782028

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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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