Recombinant Calmodulin 1/2/3 Monoclonal Antibody (AN301731L)
For research use only.
| Verified Samples | Verified Samples in WB: HeLa, NIH/3T3, Mouse brain, Rat brain |
| Dilution | WB 1:1000-1:5000 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, Rat, Mouse |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant human Calmodulin 1/2/3 fragment |
| Abbre | Calmodulin 1/2/3 |
| Synonyms | CALM1, CALM2, CALM3 |
| Swissprot | |
| Calculated MW | 17 kDa |
| Observed MW |
17 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 | Cytoskeleton |
| Concentration | 1 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A purified |
| Clone No. | A439 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calmodulin (CaM) is a ubiquitously expressed Ca2+ binding protein best known for its ability to activate CaM-dependent kinases in a variety of cells. It was initially identified in its role as an activator of cAMP PDE. In fact, calmodulin was first known as the calcium-dependent regulator protein of PDE. Calmodulin is involved, directly and indirectly, in modulation of several ion channels, including Na+, K+, L-type Ca2+, and RYR2 channels. The main binding partner of calmodulin in cardiac cells is RyR2, which regulates Ca2+ release from the sarcoplasmic reticulum. Acting as an intracellular Ca2+ sensor, Ca2+-saturated calmodulin binds RYR2 to inhibit Ca2+ release by stabilizing the RyR2 channel closed state. |
Other Clones
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Unconjugated
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