protein

ANO1/Anoctamin-1 Protein, Human (N-His, C-Myc)

HY-P700616

20 μg;50 μg

230;505 USD

ANO1/Anoctamin-1 Protein, Human (N-His, C-Myc)

proteins

E. coli

20 μg;50 μg

230;505 USD

ANO1/Anoctamin-1 protein, a calcium-activated chloride channel (CaCC), is involved in ion transport, smooth muscle contraction, and mucus secretion. ANO1/Anoctamin-1 Protein, Human (N-His, C-Myc) is the recombinant human-derived ANO1/Anoctamin-1 protein, expressed by E. coli , with C-Myc, N-10*His labeled tag.

Human

ANO1/Anoctamin-1 protein, a calcium-activated chloride channel (CaCC), plays diverse roles in cellular functions. It serves as a major contributor to basal and stimulated chloride conductance in airway epithelial cells, impacting tracheal cartilage development and contributing to airway mucus expression induced by interleukins IL3 and IL8, as well as by the asthma-associated protein CLCA1. ANO1 is indispensable for normal functioning of the interstitial cells of Cajal (ICCs), crucial for electrical pacemaker activity in gastrointestinal smooth muscles, and is involved in transepithelial anion transport and smooth muscle contraction. It is also required for CFTR activation and membrane expression, modulating endoplasmic reticulum Ca(2+) store release. Additionally, ANO1 participates in calcium-activated chloride secretion in human sweat gland epithelial cells, showing increased basal chloride permeability and decreased Ca(2+)-induced chloride permeability. In sensory neurons, ANO1 acts as a heat sensor and modulates spontaneous firing patterns, contributing to calcium-activated chloride channel activity in taste cells and mediating non-histaminergic Mas-related G-protein coupled receptor (MRGPR)-dependent itching in dorsal root ganglion neurons. In the developing brain, ANO1 is essential for the Ca(2+)-dependent process extension of radial glial cells.

anoctamin 1, calcium activated chloride channel; oral cancer overexpressed 2, ORAOV2, TMEM16A, transmembrane protein 16A; anoctamin-1; DOG1; FLJ10261; TAOS2; oral cancer overexpressed 2; tumor-amplified and overexpressed sequence 2; discovered on gastrointestinal stromal tumors protein 1; transmembrane protein 16A (eight membrane-spanning domains); ORAOV2; TMEM16A

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of PBS, 6% Trehalose, pH 7.4.

Room temperature in continental US; may vary elsewhere.