Myosin IIb Antibody [F18M11] | Primary Antibodies

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:1000 IP1:30 IHC1:2000 IF1:100 FCM1:600

Application
WB, IP, IHC, IF, FCM

Reactivity
Mouse, Rat, Human

Source
Rabbit 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 Observed MW
229 kDa 230 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
Myosin IIb Antibody [F18M11] detects endogenous levels of total Myosin IIb protein.

Clone
F18M11

Synonym(s)
Myosin-10, Myosin heavy chain 10, Non-muscle myosin heavy chain B, Non-muscle myosin heavy chain IIb, NMMHC-B, NMMHC II-b, NMMHC-IIB, MYH10

Background
Myosin IIb, encoded by MYH10, is a non‑muscle class II myosin heavy chain that functions as a central actomyosin motor in vertebrate cells and contributes to cell shape control, migration, cytokinesis, and specialized neuronal functions through ATP‑dependent interaction with filamentous actin. The heavy chain contains an N‑terminal motor domain with actin‑ and ATP‑binding sites, a neck region that associates with essential and regulatory light chains, and a long coiled‑coil tail that supports bipolar filament assembly and isoform‑specific subcellular localization, forming hexameric complexes that generate contractile force along actin bundles. Myosin IIb localizes to the cell rear, perinuclear region, junctional belts, and dendritic spines, where it cooperates with myosin IIa and IIc to organize cortical and stress‑fiber actin networks, couple protrusion at the leading edge to retraction of the cell body, and maintain tension at adherens junctions and intercalated disc–like structures. Motor activity and filament assembly of myosin IIb are regulated by phosphorylation of its regulatory light chain through Ca²⁺/calmodulin‑dependent myosin light‑chain kinase and Rho‑GTP–dependent ROCK, which link Rho‑family signaling to graded activation of actomyosin contractility and determine the spatial distribution of IIa‑ versus IIb‑rich contractile zones during polarized migration and matrix engagement. In migrating endothelial and fibroblast‑like cells, myosin IIb accumulates preferentially at the trailing edge and central region, where its motor‑dependent forward movement on F‑actin and its ability to form and remodel bipolar filaments align crossed actin bundles into antiparallel arrays that transmit traction forces from the lamellipodium to the cell body and coordinate protrusive activity with whole‑cell translocation. In the nervous system, myosin IIb is enriched in dendritic spines and postsynaptic compartments and regulates actin dynamics during synaptic plasticity; activation downstream of long‑term potentiation–inducing stimulation drives reorganization of spine actin into specialized structures that stabilize potentiated synapses and support memory consolidation, while myosin II motor inhibition disrupts these actin rearrangements and impairs maintenance of plasticity. Myosin IIb function integrates with signaling pathways that control spine remodeling and gene expression, including Ca²⁺‑dependent and Rho‑family effectors, and contributes to the mechanical coupling between glutamatergic receptor activation, actin network remodeling, and long‑lasting changes in synaptic efficacy.

Background

Myosin IIb, encoded by MYH10, is a non‑muscle class II myosin heavy chain that functions as a central actomyosin motor in vertebrate cells and contributes to cell shape control, migration, cytokinesis, and specialized neuronal functions through ATP‑dependent interaction with filamentous actin. The heavy chain contains an N‑terminal motor domain with actin‑ and ATP‑binding sites, a neck region that associates with essential and regulatory light chains, and a long coiled‑coil tail that supports bipolar filament assembly and isoform‑specific subcellular localization, forming hexameric complexes that generate contractile force along actin bundles. Myosin IIb localizes to the cell rear, perinuclear region, junctional belts, and dendritic spines, where it cooperates with myosin IIa and IIc to organize cortical and stress‑fiber actin networks, couple protrusion at the leading edge to retraction of the cell body, and maintain tension at adherens junctions and intercalated disc–like structures. Motor activity and filament assembly of myosin IIb are regulated by phosphorylation of its regulatory light chain through Ca²⁺/calmodulin‑dependent myosin light‑chain kinase and Rho‑GTP–dependent ROCK, which link Rho‑family signaling to graded activation of actomyosin contractility and determine the spatial distribution of IIa‑ versus IIb‑rich contractile zones during polarized migration and matrix engagement. In migrating endothelial and fibroblast‑like cells, myosin IIb accumulates preferentially at the trailing edge and central region, where its motor‑dependent forward movement on F‑actin and its ability to form and remodel bipolar filaments align crossed actin bundles into antiparallel arrays that transmit traction forces from the lamellipodium to the cell body and coordinate protrusive activity with whole‑cell translocation. In the nervous system, myosin IIb is enriched in dendritic spines and postsynaptic compartments and regulates actin dynamics during synaptic plasticity; activation downstream of long‑term potentiation–inducing stimulation drives reorganization of spine actin into specialized structures that stabilize potentiated synapses and support memory consolidation, while myosin II motor inhibition disrupts these actin rearrangements and impairs maintenance of plasticity. Myosin IIb function integrates with signaling pathways that control spine remodeling and gene expression, including Ca²⁺‑dependent and Rho‑family effectors, and contributes to the mechanical coupling between glutamatergic receptor activation, actin network remodeling, and long‑lasting changes in synaptic efficacy.

References
https://pubmed.ncbi.nlm.nih.gov/20797537/ https://pubmed.ncbi.nlm.nih.gov/14617807/

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%