Phospho-MBP (Thr98) Antibody [A3B1]

Application: Reactivity: vertebrates

Lane 1: Mouse brain, Lane 2: Rat brain

Usage Information

Dilution
WB1:1000

Application
WB

Reactivity
vertebrates

Source
Mouse Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
33 kDa

Datasheet & SDS

Biological Description

Specificity
Phospho-MBP (Thr98) Antibody [A3B1] detects endogenous levels of total MBP protein only when it is phosphorylated at Thr98.

Clone
A3B1

Synonym(s)
Myelin basic protein; MBP; Myelin A1 protein; Myelin membrane encephalitogenic protein; MBP

Background
Phospho-MBP designates post-translationally modified myelin basic protein isoforms within the central nervous system myelin sheath, where MAPK-mediated phosphorylation at conserved threonine residues like Thr95 and Thr125 dynamically modulates compact multilayer stability and cytoskeletal interactions. MBP organizes intrinsically disordered regions flanking amphipathic alpha-helical segments and proline-rich polyproline II helices that compact apposed cytoplasmic leaflets through multivalent cationic interactions with phospholipid headgroups and actin microfilaments. Phosphorylation introduces negative charge that electrostatically disrupts MBP-lipid adhesion, loosening sheath compaction while altering the central molecular switch region where Thr92/Thr95 phosphorylation impedes alpha-helical folding stability and reduces reversibility upon thermal perturbation through altered electrostatics that propagate globally via repulsions in the proline-rich domain. This modification attenuates MBP-actin polymerization and bundling capacity alongside a dramatic reduction in actin-MBP-lipid ternary complex formation at negatively charged bilayers, with sequential MAPK action at both sites compounding inhibition beyond net charge reduction alone. High-frequency neuronal stimulation triggers alveus MBP hyperphosphorylation via MAPK activation that propagates action potentials, while tetrodotoxin blockade prevents this regulated loosening essential for myelin plasticity during synaptic remodeling. All four major MBP charge isomers exhibit coordinated dephosphorylation responses, reflecting isoform-nonspecific pathway control. Phospho-MBP calibrates conduction velocity adaptation and oligodendroglial process dynamics during CNS development and activity-dependent myelination.

Background

Phospho-MBP designates post-translationally modified myelin basic protein isoforms within the central nervous system myelin sheath, where MAPK-mediated phosphorylation at conserved threonine residues like Thr95 and Thr125 dynamically modulates compact multilayer stability and cytoskeletal interactions. MBP organizes intrinsically disordered regions flanking amphipathic alpha-helical segments and proline-rich polyproline II helices that compact apposed cytoplasmic leaflets through multivalent cationic interactions with phospholipid headgroups and actin microfilaments. Phosphorylation introduces negative charge that electrostatically disrupts MBP-lipid adhesion, loosening sheath compaction while altering the central molecular switch region where Thr92/Thr95 phosphorylation impedes alpha-helical folding stability and reduces reversibility upon thermal perturbation through altered electrostatics that propagate globally via repulsions in the proline-rich domain. This modification attenuates MBP-actin polymerization and bundling capacity alongside a dramatic reduction in actin-MBP-lipid ternary complex formation at negatively charged bilayers, with sequential MAPK action at both sites compounding inhibition beyond net charge reduction alone. High-frequency neuronal stimulation triggers alveus MBP hyperphosphorylation via MAPK activation that propagates action potentials, while tetrodotoxin blockade prevents this regulated loosening essential for myelin plasticity during synaptic remodeling. All four major MBP charge isomers exhibit coordinated dephosphorylation responses, reflecting isoform-nonspecific pathway control. Phospho-MBP calibrates conduction velocity adaptation and oligodendroglial process dynamics during CNS development and activity-dependent myelination.

References
https://pubmed.ncbi.nlm.nih.gov/23861868/ https://pubmed.ncbi.nlm.nih.gov/10461899/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%