Recombinant Calponin-1 Monoclonal Antibody (AN301341L)
For research use only.
| Verified Samples | Verified Samples in WB: Rat lung |
| Dilution | WB 1:2000-1:10000 |
| Isotype | IgG,κ |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant Human Calponin-1 protein |
| Abbre | Calponin-1 |
| Synonyms | CNN, Calponin H, HEL-S, Calponin, CNN1, HEL-S-14, SMCC, Sm-Calp, Calponin H1, Calponin-1, smooth muscle, CNN1, HEL-S-14, SMCC, Sm-Calp |
| Swissprot | |
| Calculated MW | 33 kDa |
| Observed MW |
33 kDa
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Cytoplasm |
| Concentration | 0.2 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A |
| Research Areas | Signal Transduction, Stem Cells, Cardiovascular |
| Clone No. | 8A6 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| 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. |
Other Clones
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Unconjugated
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