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Recombinant Human CNN1 protein (His tag)
Recombinant Human CNN1 protein (His tag)
Artikelnummer
ELSPDEH100414-20
Verpackungseinheit
20 µg
Hersteller
Elabscience Biotechnology
Verfügbarkeit:
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Abbreviation: CNN1
Target Synonym: Calponin-1;CNN1;Calponin H1;smooth muscle
Target Species: Human
Expression Host: E.coli
Fusion Tag: N-His
UNIProt ID: P51911
Background: CNN-1 (Calponin 1 [calcium and calmodulin-binding troponin T-like protein]; also Calponin basic, CaP and Calponin H1) is a 32-36 kDa cytoplasmic member of the calponin family of proteins. Although reportedly expressed in fibroblasts and endothelial cells, it actually appears to be restricted to smooth muscle and smooth muscle-like cells such as myoepithelium and myofibroblasts in the adult. CNN-1 interacts with F-actin in a phosphorylation-dependent manner. When nonphosphorylated, CNN-1 blocks actomyosin ATPase activity, contributing to the stabilization of actin stress fiber bundles. Thus, CNN-1 expression inhibits cell motility and the formation of podosomes. Human CNN-1 is 297 amino acids (aa) in length. It contains one CH/calponin homology domain (aa 30-127), and three consecutive calponin-like repeats (aa 164-268). The repeats are suggested to mediate actin binding. There are five potential Ser/Thr phosphorylation sites. Full-length human CNN-1 shares 97% aa sequence identity with mouse CNN-1.
Sequence: Met 1-Ala 297
Purity: > 95 % as determined by reducing SDS-PAGE.
Formulation: Lyophilized from sterile PBS, pH 7.4.
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
Endotoxin: Please contact us for more information.
Target Synonym: Calponin-1;CNN1;Calponin H1;smooth muscle
Target Species: Human
Expression Host: E.coli
Fusion Tag: N-His
UNIProt ID: P51911
Background: CNN-1 (Calponin 1 [calcium and calmodulin-binding troponin T-like protein]; also Calponin basic, CaP and Calponin H1) is a 32-36 kDa cytoplasmic member of the calponin family of proteins. Although reportedly expressed in fibroblasts and endothelial cells, it actually appears to be restricted to smooth muscle and smooth muscle-like cells such as myoepithelium and myofibroblasts in the adult. CNN-1 interacts with F-actin in a phosphorylation-dependent manner. When nonphosphorylated, CNN-1 blocks actomyosin ATPase activity, contributing to the stabilization of actin stress fiber bundles. Thus, CNN-1 expression inhibits cell motility and the formation of podosomes. Human CNN-1 is 297 amino acids (aa) in length. It contains one CH/calponin homology domain (aa 30-127), and three consecutive calponin-like repeats (aa 164-268). The repeats are suggested to mediate actin binding. There are five potential Ser/Thr phosphorylation sites. Full-length human CNN-1 shares 97% aa sequence identity with mouse CNN-1.
Sequence: Met 1-Ala 297
Purity: > 95 % as determined by reducing SDS-PAGE.
Formulation: Lyophilized from sterile PBS, pH 7.4.
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
Endotoxin: Please contact us for more information.
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