IDE Monoclonal Antibody (E-AB-22041)
For research use only.
| Verified Samples |
Verified Samples in WB: Hela, HepG2 Verified Samples in IHC: Human liver cancer Verified Samples in IF: Human breast |
| Dilution | WB 1:500-1:2000, IHC 1:50-300, IF 1:100-1:300 |
| Isotype | IgG |
| Host | Mouse |
| Reactivity | Human |
| Applications | WB, IHC-p, IF |
| Clonality | Monoclonal |
| Immunogen | Synthetic Peptide |
| Abbre | IDE |
| Synonyms | Abeta-degrading protease, FLJ35968, IDE, Ide, Insulin protease, Insulin-degrading enzyme, Insulinase, Insulysin, OTTHUMP00000020097 |
| Swissprot | |
| Observed MW |
118 kDa
The actual band is not consistent with the expectation.
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. Cell surface. Present at the cell surface of neuron cells. The membrane-associated isoform is approximately 5 kDa larger than the known cytosolic isoform. |
| Concentration | 1 mg/mL |
| Buffer | Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer, 0.5% protein protectant and 50% glycerol. |
| Purification Method | Protein A purification |
| Research Areas | Cancer, Cell Biology, Cardiovascular, Metabolism, Neuroscience, Signal Transduction |
| Clone No. | 1H4 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | The product is shipped with ice pack,upon receipt,store it immediately at the temperature recommended. |
| background | This gene encodes a zinc metallopeptidase that degrades intracellular insulin, and thereby terminates insulins activity, as well as participating in intercellular peptide signalling by degrading diverse peptides such as glucagon, amylin, bradykinin, and kallidin. The preferential affinity of this enzyme for insulin results in insulin-mediated inhibition of the degradation of other peptides such as beta-amyloid. Deficiencies in this protein's function are associated with Alzheimer's disease and type 2 diabetes mellitus but mutations in this gene have not been shown to be causitive for these diseases. This protein localizes primarily to the cytoplasm but in some cell types localizes to the extracellular space, cell membrane, peroxisome, and mitochondrion. Alternative splicing results in multiple transcript variants encoding distinct isoforms. Additional transcript variants have been described but have not been experimentally verified. |
Other Clones
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Other Formats
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Unconjugated
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