Rabbit anti-Human CAVIN1 Polyclonal Antibody

Uniprot Id

Q6NZI2

Target Species

Human

Target Name

CAVIN1

Target Full Name

Caveolae-associated protein 1

Target Function

Plays an important role in caveolae formation and organization. Essential for the formation of caveolae in all tissues. 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. The caveolae biogenesis pathway is required for the secretion of proteins such as GASK1A.

Target Involvement

Congenital generalized lipodystrophy 4 (CGL4)

Target Subcellular Location

Membrane, caveola. Cell membrane. Microsome. Endoplasmic reticulum. Cytoplasm, cytosol. Mitochondrion. Nucleus.

Target Protein Families

CAVIN family

Target Synonyms

2310075E07Rik; AW546441; Cavin 1; Cavin; Cavin-1; CAVIN1; CGL4; FKSG13; FLJ90031; MGC118550; OTTMUSP00000002049; Polymerase I and transcript release factor; Ptrf; PTRF_HUMAN; RNA polymerase I and transcript release factor; RP23-279L23.6; TTF I interacting peptide 12

Target Background

This gene encodes 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.