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Mouse Anti-CAVIN1 Recombinant Antibody (P0141) (CBMAB-P0141-YC)


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Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
P0141
Antibody Isotype
IgG1, κ
Application
WB, IP, IF

Basic Information

Immunogen
Amino acids 157-272 of PTRF of mouse origin.
Host Species
Mouse
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)1:50-1:500

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

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.2 mg/ml
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at-20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Caveolae Associated Protein 1
Introduction
CAVIN1 is a protein that enables the dissociation of paused ternary polymerase I transcription complexes from the 3' end of pre-rRNA transcripts. This protein regulates rRNA transcription by promoting the dissociation of transcription complexes and the reinitiation of polymerase I on nascent rRNA transcripts. This protein also localizes to caveolae at the plasma membrane and is thought to play a critical role in the formation of caveolae and the stabilization of caveolins. This protein translocates from caveolae to the cytoplasm after insulin stimulation. Caveolae contain truncated forms of this protein and may be the site of phosphorylation-dependent proteolysis. This protein is also thought to modify lipid metabolism and insulin-regulated gene expression. Mutations in this gene result in a disorder characterized by generalized lipodystrophy and muscular dystrophy.
Entrez Gene ID
284119
UniProt ID
Q6NZI2
Alternative Names
FKSG13; CGL4; cavin-1; CAVIN; CAVIN1
Function
Plays an important role in caveolae formation and organization. Essential for the formation of caveolae in all tissues (PubMed:18056712, PubMed:18191225, PubMed:19726876).
Core component of the CAVIN complex which is essential for recruitment of the complex to the caveolae in presence of calveolin-1 (CAV1). Essential for normal oligomerization of CAV1. Promotes ribosomal transcriptional activity in response to metabolic challenges in the adipocytes and plays an important role in the formation of the ribosomal transcriptional loop. Dissociates transcription complexes paused by DNA-bound TTF1, thereby releasing both RNA polymerase I and pre-RNA from the template (By similarity) (PubMed:18056712, PubMed:18191225, PubMed:19726876).
The caveolae biogenesis pathway is required for the secretion of proteins such as GASK1A (By similarity).
Biological Process
Positive regulation of cell motility Source: UniProtKB
Protein secretion Source: Ensembl
rRNA transcription Source: UniProtKB
Termination of RNA polymerase I transcription Source: UniProtKB
Transcription initiation from RNA polymerase I promoter Source: UniProtKB
Cellular Location
Mitochondrion; Microsome; Endoplasmic reticulum; Cytosol; Cell membrane; Nucleus; Caveola. Translocates to the cytoplasm from the caveolae upon insulin stimulation (PubMed:17026959). Colocalizes with CAV1 in lipid rafts in adipocytes. Localizes in the caveolae in a caveolin-dependent manner (By similarity).
Involvement in disease
Congenital generalized lipodystrophy 4 (CGL4): A disorder characterized by the association of congenital generalized lipodystrophy with muscular dystrophy and cardiac anomalies. Congenital generalized lipodystrophy is characterized by a near complete absence of adipose tissue, extreme insulin resistance, hypertriglyceridemia, hepatic steatosis and early onset of diabetes.
PTM
Phosphorylated. Present in active and inactive forms. Changes in phosphorylation pattern may alter activity. Phosphorylation at Tyr-156 is essential for its functionin the regulation of ribosomal transcriptional activity.
Five truncated forms are found in the caveolae. These are thought to be the result of proteolysis and may be phosphorylation-dependent.1 Publication
Monoubiquitinated.
More Infomation

Zhou, Y., Ariotti, N., Rae, J., Liang, H., Tillu, V., Tee, S., ... & Parton, R. G. (2021). Caveolin-1 and cavin1 act synergistically to generate a unique lipid environment in caveolae. Journal of Cell Biology, 220(3).

Liu, L. (2020). Lessons from cavin-1 deficiency. Biochemical Society Transactions, 48(1), 147-154.

Pu, W., Qiu, J., Nassar, Z. D., Shaw, P. N., McMahon, K. A., Ferguson, C., ... & Parat, M. O. (2020). A role for caveola‐forming proteins caveolin‐1 and CAVIN1 in the pro‐invasive response of glioblastoma to osmotic and hydrostatic pressure. Journal of cellular and molecular medicine, 24(6), 3724-3738.

Guo, Q., Guan, G. F., Cheng, W., Zou, C. Y., Zhu, C., Cheng, P., & Wu, A. H. (2019). Integrated profiling identifies caveolae‐associated protein 1 as a prognostic biomarker of malignancy in glioblastoma patients. CNS neuroscience & therapeutics, 25(3), 343-354.

Pu, W., Nassar, Z. D., Khabbazi, S., Xie, N., McMahon, K. A., Parton, R. G., ... & Parat, M. O. (2019). Correlation of the invasive potential of glioblastoma and expression of caveola-forming proteins caveolin-1 and CAVIN1. Journal of neuro-oncology, 143(2), 207-220.

Patni, N., Vuitch, F., & Garg, A. (2019). Postmortem findings in a young man with congenital generalized lipodystrophy, type 4 due to CAVIN1 mutations. The Journal of Clinical Endocrinology & Metabolism, 104(3), 957-960.

Bai, X. L., Yang, X. Y., & Li, J. Y. (2017). Cavin-1 regulates caveolae-mediated LDL transcytosis: Crosstalk in an AMPK/eNOS/NF-κB/Sp1 loop. Oncotarget, 8(61), 103985.

Zhou, L. J., Chen, X. Y., Liu, S. P., Zhang, L. L., Xu, Y. N., Mu, P. W., ... & Tan, Z. (2017). Downregulation of Cavin‐1 Expression via Increasing Caveolin‐1 Degradation Prompts the Proliferation and Migration of Vascular Smooth Muscle Cells in Balloon Injury–Induced Neointimal Hyperplasia. Journal of the American Heart Association, 6(8), e005754.

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

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