CNN1 Protein (AA 1-297) (His tag)
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- Target See all CNN1 Proteins
- CNN1 (Calponin 1 (CNN1))
- Protein Type
- Recombinant
- Protein Characteristics
- AA 1-297
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Origin
- Human
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Source
- Escherichia coli (E. coli)
- Purification tag / Conjugate
- This CNN1 protein is labelled with His tag.
- Sequence
- Met 1-Ala 297
- Characteristics
- A DNA sequence encoding the Human CNN1 protein (P51911) (Met 1-Ala 297) was expressed with a N-His tag.
- Purity
- > 95 % as determined by reducing SDS-PAGE.
- Top Product
- Discover our top product CNN1 Protein
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- Restrictions
- For Research Use only
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- Format
- Lyophilized
- Buffer
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Lyophilized from sterile PBS, pH 7.4.
Normally 5 % - 8 % trehalose, mannitol and 0.01 % Tween80 are added as protectants before lyophilization. - Storage
- 4 °C,-20 °C,-80 °C
- Storage Comment
- Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
- Expiry Date
- 12 months
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- Target
- CNN1 (Calponin 1 (CNN1))
- Alternative Name
- CNN1 (CNN1 Products)
- Synonyms
- CN Protein, CnnI Protein, SMCC Protein, Sm-Calp Protein, XclpH3 Protein, clpH3 Protein, cnn2 Protein, calponin 1 Protein, calponin 1, basic, smooth muscle L homeolog Protein, cnn1 Protein, Cnn1 Protein, CNN1 Protein, cnn1.L Protein
- Background
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Abbreviation: CNN1
Target Synonym: Calponin-1,CNN1,Calponin H1,smooth muscle
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.
- Molecular Weight
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Calculated MW: 32.56 kDa
Observed MW: 35 kDa
- UniProt
- P51911
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