Caveolin-2 Antibody (Rabbit mAb) [E6A6]

Application: Reactivity: Human

Usage Information

Dilution
WB1:5000 - 1:10000 IHC1:100 - 1:250 IF1:100 - 1:250 FCM1:2000

Application
WB, IHC, IF, FCM

Reactivity
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
18 kDa 20 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
Caveolin-2 Antibody (Rabbit mAb) [E6A6] detects endogenous levels of total Caveolin-2 protein.

Clone
E6A6

Synonym(s)
Caveolin-2, CAV2

Background
Caveolin‑2 is a member of the caveolin family of integral membrane proteins that localizes to cholesterol‑ and glycosphingolipid‑rich caveolae at the inner surface of the plasma membrane and forms stable hetero‑oligomeric complexes with caveolin‑1, acting as an accessory scaffolding component that targets caveolar assemblies to lipid rafts and modulates the activity of associated signaling proteins. The protein is expressed in adipocytes, vascular endothelial cells, type I pneumocytes and select smooth muscle populations, and alternative initiation in a single transcript generates α and β isoforms whose distinct phosphorylation patterns on serine and tyrosine residues govern subcellular distribution between plasma membrane caveolae, cytoplasm, intracellular compartments and nucleus, with Ser‑23 phosphorylation by caveolin‑1 driving recruitment to the caveolar membrane and Tyr‑19/Tyr‑27 phosphorylation by Src or growth factor signaling controlling nuclear translocation and cytoplasmic versus membrane localization. As a caveolar scaffolding protein, caveolin‑2 interacts with G‑protein α subunits and RAS p21 protein activator 1, and positively regulates mitogenesis through the MAPK pathway: Ser‑36‑phosphorylated caveolin‑2 modulates mitosis in endothelial cells, Tyr‑19 phosphorylation is required for insulin-induced ERK2 phosphorylation and STAT3 DNA binding, and dual Tyr‑19/Tyr‑27 phosphorylation is necessary for insulin-stimulated STAT3 Ser‑727 phosphorylation and nuclear activation, placing caveolin‑2 at the center of insulin‑responsive MAPK1/STAT3 signaling that controls cell-cycle progression and growth. In adipose tissue, caveolin‑2 mRNA is abundant and induced during 3T3‑L1 differentiation to adipocytes, paralleling caveolin‑1, and the hetero‑oligomeric Cav1–Cav2 complex contributes to caveolae formation and lipid metabolism, supporting roles in fatty acid uptake, cholesterol homeostasis and insulin signaling at the adipocyte surface. Caveolin‑2‑deficient mice show selective pulmonary defects, such as thickened alveolar septa and altered endothelial morphology, with little or no change in caveolin‑1 expression or caveolae abundance, indicating that caveolin‑2 has nonredundant roles in lung function that extend beyond simply supporting caveolar structure. In severe pulmonary hypertension, immunolocalization studies demonstrate absent or markedly decreased caveolin expression—including caveolin‑2—in plexiform vascular lesions and some muscularized precapillary arterioles, while total lung caveolin levels remain unchanged, suggesting that local loss of caveolin‑2 in proliferating, apoptosis‑resistant endothelial cells contributes to lesion formation and altered vascular signaling, in parallel with coordinated changes in stress‑response proteins such as heme oxygenase‑1. Biochemical characterization shows that caveolin‑2 has a lower tendency than caveolin‑1 to form very high molecular weight oligomers, making it particularly suitable for studying protein–lipid and protein–protein interactions within caveolar rafts, and reinforcing the view that caveolin‑2 fine‑tunes caveolar signaling assemblies rather than acting as the primary structural core.

Background

Caveolin‑2 is a member of the caveolin family of integral membrane proteins that localizes to cholesterol‑ and glycosphingolipid‑rich caveolae at the inner surface of the plasma membrane and forms stable hetero‑oligomeric complexes with caveolin‑1, acting as an accessory scaffolding component that targets caveolar assemblies to lipid rafts and modulates the activity of associated signaling proteins. The protein is expressed in adipocytes, vascular endothelial cells, type I pneumocytes and select smooth muscle populations, and alternative initiation in a single transcript generates α and β isoforms whose distinct phosphorylation patterns on serine and tyrosine residues govern subcellular distribution between plasma membrane caveolae, cytoplasm, intracellular compartments and nucleus, with Ser‑23 phosphorylation by caveolin‑1 driving recruitment to the caveolar membrane and Tyr‑19/Tyr‑27 phosphorylation by Src or growth factor signaling controlling nuclear translocation and cytoplasmic versus membrane localization. As a caveolar scaffolding protein, caveolin‑2 interacts with G‑protein α subunits and RAS p21 protein activator 1, and positively regulates mitogenesis through the MAPK pathway: Ser‑36‑phosphorylated caveolin‑2 modulates mitosis in endothelial cells, Tyr‑19 phosphorylation is required for insulin-induced ERK2 phosphorylation and STAT3 DNA binding, and dual Tyr‑19/Tyr‑27 phosphorylation is necessary for insulin-stimulated STAT3 Ser‑727 phosphorylation and nuclear activation, placing caveolin‑2 at the center of insulin‑responsive MAPK1/STAT3 signaling that controls cell-cycle progression and growth. In adipose tissue, caveolin‑2 mRNA is abundant and induced during 3T3‑L1 differentiation to adipocytes, paralleling caveolin‑1, and the hetero‑oligomeric Cav1–Cav2 complex contributes to caveolae formation and lipid metabolism, supporting roles in fatty acid uptake, cholesterol homeostasis and insulin signaling at the adipocyte surface. Caveolin‑2‑deficient mice show selective pulmonary defects, such as thickened alveolar septa and altered endothelial morphology, with little or no change in caveolin‑1 expression or caveolae abundance, indicating that caveolin‑2 has nonredundant roles in lung function that extend beyond simply supporting caveolar structure. In severe pulmonary hypertension, immunolocalization studies demonstrate absent or markedly decreased caveolin expression—including caveolin‑2—in plexiform vascular lesions and some muscularized precapillary arterioles, while total lung caveolin levels remain unchanged, suggesting that local loss of caveolin‑2 in proliferating, apoptosis‑resistant endothelial cells contributes to lesion formation and altered vascular signaling, in parallel with coordinated changes in stress‑response proteins such as heme oxygenase‑1. Biochemical characterization shows that caveolin‑2 has a lower tendency than caveolin‑1 to form very high molecular weight oligomers, making it particularly suitable for studying protein–lipid and protein–protein interactions within caveolar rafts, and reinforcing the view that caveolin‑2 fine‑tunes caveolar signaling assemblies rather than acting as the primary structural core.

References
https://pubmed.ncbi.nlm.nih.gov/22229094/ https://pubmed.ncbi.nlm.nih.gov/20598236/

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%