ACTα2 Polyclonal Antibody (D-AB-10442L)
For research use only.
| Verified Samples |
Verified Samples in WB: Human Hela |
| Dilution | WB 1:500-1:1000 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human |
| Applications | WB |
| Clonality | Polyclonal |
| Immunogen | Recombinant Mouse ACTα2 protein expressed by E.coli |
| Abbre | ACTα2 |
| Synonyms | Acta2, Actin, Actsa, Actvs, Alpha-actin-2, aortic smooth muscle, intermediate form |
| Swissprot | |
| Calculated MW | 42 kDa |
| Observed MW |
42 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 | Secreted |
| Tissue Specificity | Expressed in the liver |
| Concentration | 1 mg/mL |
| Buffer | PBS with 0.05% proclin 300, 1% protective protein and 50% glycerol,pH7.4 |
| Purification Method | Antigen Affinity Purification |
| Research Areas | Immunology, Neuroscience, Stem Cells |
| 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 | alpha-2-macroglobulin,also known as α2-macroglobulin(α2M and A2M),is an abundant protein of the plasma of vertebrates and members of several invertebrate phyla and functions as a broad-spectrum protease-binding protein. alpha-2-macroglobulin is produced by the liver,and is a major component of the alpha-2 band in protein electrophoresis. alpha-2-macroglobulin is a large plasma glycoprotein that has long been known as an irreversible inhibitor of a variety of proteinases. More recently,it has been reported that numerous growth factors,cytokines and hormones bind to alpha 2M through diverse mechanisms. A2M is also produced in the brain where it binds multiple extracellular ligands and is internalized by neurons and astrocytes. In the brain of Alzheimer's disease (AD) patients,A2M has been localized to diffuse amyloid plaques. A2M also binds soluble beta-amyloid,of which it mediates degradation. Protease-conjugated alpha2-macroglobulin is selectively bound by cells contacting the body fluids and alpha2-macroglobulin and its protease cargo are then internalized and degraded in secondary lysosomes of those cells. In addition to this function as an agent for protease clearance,alpha2-macroglobulin binds a variety of other ligands,including several peptide growth factors and modulates the activity of a lectin-dependent cytolytic pathway in arthropods. |
Other Clones
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Other Formats
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Unconjugated
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