Caveolin 3 Antibody (Mouse mAb) [L5G2]

Application: Reactivity: Rat

Usage Information

Dilution
WB1:1000

Application
WB, IHC

Reactivity
Rat

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
17 kDa

Positive Control	Rat muscle
Negative Control

Datasheet & SDS

Biological Description

Specificity
Caveolin 3 Antibody (Mouse mAb) [L5G2] detects endogenous levels of total Caveolin 3 protein.

Clone
L5G2

Synonym(s)
Caveolin-3, M-caveolin, CAV3

Background
Caveolin-3 belongs to the caveolin family of membrane scaffolding proteins alongside caveolin-1 and caveolin-2, but unlike its paralogs, it shows striated muscle-restricted expression across cardiac and skeletal tissue, where it serves as the defining structural component of caveolae, flask-shaped plasma membrane invaginations. The protein has both its N- and C-termini exposed to the cytoplasm, while a central hydrophobic segment forms a membrane-embedded loop that does not fully cross the bilayer, and a caveolin scaffolding domain within the cytoplasmic region mediates direct protein-protein interactions that recruit signaling partners into the caveolar membrane microdomain. Through this scaffolding domain, caveolin-3 binds directly to the intracellular I-II loop of Cav1.1, the pore-forming alpha subunit of the skeletal muscle L-type calcium channel, with the two proteins co-immunoprecipitating from triadic membrane preparations and colocalizing within the T-tubular membrane, and loss of this direct physical interaction reduces maximal L-type calcium channel conductance by half in cultured myotubes and fetal skeletal muscle fibers. Caveolin-3 additionally engages nitric oxide synthase isoforms and components of G-protein-coupled receptor signaling through the same scaffolding mechanism, positioning caveolae as organizing platforms that concentrate excitation-coupling and beta-adrenergic signaling machinery at defined membrane sites rather than allowing these components to diffuse freely across the sarcolemma. Caveolin-3 also co-purifies with dystrophin and represents a fraction of the dystrophin-associated protein pool, and its cytoplasmic WW-like domain binds the same PPXY sequence on beta-dystroglycan that is recognized by the WW domain of dystrophin, meaning caveolin-3 and dystrophin compete for an overlapping binding site on the dystrophin-glycoprotein complex, so that caveolin-3 overexpression can displace dystrophin from the plasma membrane and promote its degradation. Point mutations disrupt these interactions in distinct ways depending on their location: the P104L substitution within the membrane-spanning domain and a nine-base-pair microdeletion within the scaffolding domain each produce a marked reduction in sarcolemmal caveolin-3 protein and cause autosomal dominant limb-girdle muscular dystrophy type 1C, while other CAV3 mutations cluster in the flexible N-terminus and scaffolding domain and underlie rippling muscle disease, distal myopathy, and hyperCKemia. Because caveolin-3 loss directly destabilizes calcium channel conductance and disrupts the competitive balance with dystrophin at the membrane, the protein functions as a defined structural and signaling hub whose disruption connects mechanistically to both muscular dystrophy and cardiac arrhythmia phenotypes associated with CAV3 mutation.

Background

Caveolin-3 belongs to the caveolin family of membrane scaffolding proteins alongside caveolin-1 and caveolin-2, but unlike its paralogs, it shows striated muscle-restricted expression across cardiac and skeletal tissue, where it serves as the defining structural component of caveolae, flask-shaped plasma membrane invaginations. The protein has both its N- and C-termini exposed to the cytoplasm, while a central hydrophobic segment forms a membrane-embedded loop that does not fully cross the bilayer, and a caveolin scaffolding domain within the cytoplasmic region mediates direct protein-protein interactions that recruit signaling partners into the caveolar membrane microdomain. Through this scaffolding domain, caveolin-3 binds directly to the intracellular I-II loop of Cav1.1, the pore-forming alpha subunit of the skeletal muscle L-type calcium channel, with the two proteins co-immunoprecipitating from triadic membrane preparations and colocalizing within the T-tubular membrane, and loss of this direct physical interaction reduces maximal L-type calcium channel conductance by half in cultured myotubes and fetal skeletal muscle fibers. Caveolin-3 additionally engages nitric oxide synthase isoforms and components of G-protein-coupled receptor signaling through the same scaffolding mechanism, positioning caveolae as organizing platforms that concentrate excitation-coupling and beta-adrenergic signaling machinery at defined membrane sites rather than allowing these components to diffuse freely across the sarcolemma. Caveolin-3 also co-purifies with dystrophin and represents a fraction of the dystrophin-associated protein pool, and its cytoplasmic WW-like domain binds the same PPXY sequence on beta-dystroglycan that is recognized by the WW domain of dystrophin, meaning caveolin-3 and dystrophin compete for an overlapping binding site on the dystrophin-glycoprotein complex, so that caveolin-3 overexpression can displace dystrophin from the plasma membrane and promote its degradation. Point mutations disrupt these interactions in distinct ways depending on their location: the P104L substitution within the membrane-spanning domain and a nine-base-pair microdeletion within the scaffolding domain each produce a marked reduction in sarcolemmal caveolin-3 protein and cause autosomal dominant limb-girdle muscular dystrophy type 1C, while other CAV3 mutations cluster in the flexible N-terminus and scaffolding domain and underlie rippling muscle disease, distal myopathy, and hyperCKemia. Because caveolin-3 loss directly destabilizes calcium channel conductance and disrupts the competitive balance with dystrophin at the membrane, the protein functions as a defined structural and signaling hub whose disruption connects mechanistically to both muscular dystrophy and cardiac arrhythmia phenotypes associated with CAV3 mutation.

References
https://pubmed.ncbi.nlm.nih.gov/21262376/ https://pubmed.ncbi.nlm.nih.gov/33228026/

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%