Recombinant AID Monoclonal Antibody (AN302047L)
For research use only.
| Verified Samples |
Verified Samples in WB: K562(negative control), Ramos, Daudi Verified Samples in IHC: Human tonsil, Human diffuse large B-cell lymphoma |
| Dilution | WB 1:1000, IHC 1:2000 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, |
| Applications | WB, IHC |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Peptide. This information is proprietary to PTMab. |
| Abbre | AID |
| Synonyms | AID, AICDA |
| Swissprot | |
| Calculated MW | 24 kDa |
| Observed MW |
23 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, Nucleus |
| Concentration | 1 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A purified |
| Research Areas | Immunology, Epigenetics and Nuclear Signaling |
| Clone No. | A767 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Activation-induced cytidine deaminase (AID) is thought to modify RNA due to its high homology to the RNA editing enzyme APOBEC-1. This function, however, has not been confirmed in in vitro studies, which show that AID has significant cytidine deaminase activity, and that this activity is blocked by zinc chelation.The B cell immune system must specifically recognize several infectious agents, which vastly outnumber immunoglobulin gene segments present in a given organism. Mechanisms such as somatic hypermutation, isotype switch recombination and gene conversion introduce diversity and specificity to the immune system. Analysis of mouse models and patients with AID deficiency has established a link between all three of these mechanisms and AID function. AID protein is detected in germinal center centroblast and germinal center derived lymphomas (Burkitt lymphoma), but not in pre-germinal center B cells or post-germinal center neoplasms (B cell chronic lymphocytic leukemia and multiple myeloma). |
Other Clones
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Other Formats
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Unconjugated
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