Mouse Anti-CAV2 Recombinant Antibody (CBT2081) (V2LY-0625-LY161)

Name: Mouse Anti-CAV2 Recombinant Antibody (CBT2081)
SKU: V2LY-0625-LY161
Rating: 5 (1 reviews)

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Tested Data

Mouse Anti-CAV2 Recombinant Antibody (CBT2081) (V2LY-0625-LY161) in WB

Mouse Anti-CAV2 Recombinant Antibody (CBT2081) (V2LY-0625-LY161) in FC

Mouse Anti-CAV2 Recombinant Antibody (CBT2081) (V2LY-0625-LY161) in IHC

Mouse Anti-CAV2 Recombinant Antibody (CBT2081) (V2LY-0625-LY161) in ELISA

Datasheet

SDS

Request for COA

Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

CBT2081

Application

WB, IHC, FC

Immunogen

Purified recombinant fragment of human CAV2 (AA: 1-86) expressed in E. Coli.

Host Species

Mouse

Specificity

Human

Antibody Isotype

IgG1

Clonality

Monoclonal Antibody

Application Notes

Application	Note
WB	1:500-1:2,000
IHC-P	1:200-1:1,000
FC	1:200-1:400
ELISA	1:10,000

Formulations & Storage [For reference only, actual COA shall prevail!]

Format

Liquid

Buffer

PBS

Preservative

Sodium azide

Concentration

Batch dependent

Purity

> 95% Purity determined by SDS-PAGE.

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

More Infomation

Target

Full Name

Caveolin 2

Entrez Gene ID

858

UniProt ID

P51636

Function

May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity).

Biological Process

Basement membrane organization Source: Ensembl
Caveola assembly Source: BHF-UCL
Cell differentiation Source: GO_Central
Endoplasmic reticulum organization Source: UniProtKB
Insulin receptor signaling pathway Source: BHF-UCL
Mitochondrion organization Source: UniProtKB
Negative regulation of endothelial cell proliferation Source: UniProtKB
Negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
Positive regulation by host of viral process Source: AgBase
Positive regulation by host of viral release from host cell Source: AgBase
Positive regulation of dopamine receptor signaling pathway Source: BHF-UCL
Positive regulation of endothelial cell proliferation Source: Ensembl
Positive regulation of GTPase activity Source: BHF-UCL
Positive regulation of MAPK cascade Source: BHF-UCL
Receptor-mediated endocytosis of virus by host cell Source: CACAO
Regulation of cytosolic calcium ion concentration Source: GO_Central
Regulation of mitotic nuclear division Source: BHF-UCL
Skeletal muscle fiber development Source: UniProtKB
Vesicle docking Source: BHF-UCL
Vesicle fusion Source: BHF-UCL
Vesicle organization Source: BHF-UCL

Cellular Location

Cell membrane; Golgi apparatus membrane; Cytoplasm; Nucleus; Caveola. Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and is translocated to the nucleus in complex with MAPK1 in response to insulin (By similarity). Tyr-27-phosphorylated form is located both in the cytoplasm and plasma membrane. CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. Ser-36-phosphorylated form resides in intracellular compartments.

Topology

Cytoplasmic: 1-86
Helical: 87-107
Cytoplasmic: 108-162

PTM

Phosphorylated on serine and tyrosine residues. CAV1 promotes phosphorylation on Ser-23 which then targets the complex to the plasma membrane, lipid rafts and caveolae. Phosphorylation on Ser-36 appears to modulate mitosis in endothelial cells (By similarity). Phosphorylation on both Tyr-19 and Tyr-27 is required for insulin-induced 'Ser-727' phosphorylation of STAT3 and its activation. Phosphorylation on Tyr-19 is required for insulin-induced phosphorylation of MAPK1 and DNA binding of STAT3. Tyrosine phosphorylation is induced by both EGF and insulin (By similarity).

Liu, Y., Wang, M., Wang, D., Fay, W. P., Korthuis, R. J., & Sowa, G. (2021). Elevated post-ischemic tissue injury and leukocyte-endothelial adhesive interactions in mice with global deficiency in caveolin-2: role of PAI-1. American Journal of Physiology-Heart and Circulatory Physiology.

Mamoor, S. (2021). Differential expression of caveolin 2 in cancers of the breast.

Kwon, H., Choi, M., Ahn, Y., & Pak, Y. (2020). N-myristoylation regulates insulin-induced phosphorylation and ubiquitination of Caveolin-2 for insulin signaling. Biochemical and Biophysical Research Communications, 532(4), 535-540.

Yang, X., Ma, L., Wei, R., Ye, T., Zhou, J., Wen, M., ... & Yang, L. (2020). Twist1-induced miR-199a-3p promotes liver fibrosis by suppressing caveolin-2 and activating TGF-β pathway. Signal transduction and targeted therapy, 5(1), 1-12.

Bulacio, R. P., Nosetto, E. C., Brandoni, A., & Torres, A. M. (2019). Novel finding of caveolin‐2 in apical membranes of proximal tubule and first detection of caveolin‐2 in urine: A promising biomarker of renal disease. Journal of cellular biochemistry, 120(4), 4966-4974.

Bulacio, R. P., & Torres, A. M. (2019). Caveolin-2 in urine as a novel biomarker of renal recovery after cisplatin induced nephrotoxicity in rats. Toxicology letters, 313, 169-177.

Gerstenberger, W., Wrage, M., Kettunen, E., Pantel, K., Anttila, S., Steurer, S., & Wikman, H. (2018). Stromal caveolin-1 and caveolin-2 expression in primary tumors and lymph node metastases. Analytical cellular pathology, 2018.

Liu, F., Shangli, Z., & Hu, Z. (2018). CAV2 promotes the growth of renal cell carcinoma through the EGFR/PI3K/Akt pathway. OncoTargets and therapy, 11, 6209.

Liang, C., Shi, S., Meng, Q., Liang, D., Hua, J., Qin, Y., ... & Yu, X. (2018). MiR‐29a, targeting caveolin 2 expression, is responsible for limitation of pancreatic cancer metastasis in patients with normal level of serum CA125. International journal of cancer, 143(11), 2919-2931.

de Almeida, C. J. G. (2017). Caveolin-1 and caveolin-2 can be antagonistic partners in inflammation and beyond. Frontiers in immunology, 8, 1530.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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Isotype control

For research use only. Not intended for any clinical use.

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