Recombinant Insulin Monoclonal Antibody (AN301325L)
For research use only.
| Verified Samples | Verified Samples in WB: MIN6 |
| Dilution | WB 1:1000-1:5000 |
| Isotype | IgG,κ |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant Human Insulin protein |
| Abbre | Insulin |
| Synonyms | MODY, IDDM, IDDM1, IDDM2, ILPR, IRDN, MODY10, INS, Insulin, Connecting Peptide, Insulin A chain, Insulin B chain, Preproinsulin, Proinsulin, Proinsulin precursor, IDDM, IDDM1, IDDM2, ILPR, ins, INS, Insulin A chain, Insulin B chain, IRDN, MODY10, Preproinsulin, Proinsulin, Proinsulin precursor, Pro-Insulin |
| Swissprot | |
| Calculated MW | 12 kDa |
| Observed MW |
12 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 | Cytoplasmic |
| 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, Neuroscience, Cardiovascular, Metabolism |
| Clone No. | 9C4 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | After removal of the precursor signal peptide, proinsulin is post-translationally cleaved into three peptides: the B chain and A chain peptides, which are covalently linked via two disulfide bonds to form insulin, and C-peptide. Binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. A multitude of mutant alleles with phenotypic effects have been identified. There is a read-through gene, INS-IGF2, which overlaps with this gene at the 5' region and with the IGF2 gene at the 3' region. Alternative splicing results in multiple transcript variants. |
Other Clones
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Unconjugated
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