SORBS2 Polyclonal Antibody (E-AB-19081)
For research use only.
| Verified Samples |
Verified Samples in WB: L-O2, 231 Verified Samples in IHC: Human liver cancer |
| Dilution | WB 1:1000-1:5000, IHC 1:150-1:300 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB, IHC |
| Clonality | Polyclonal |
| Immunogen | Fusion protein of human SORBS2 |
| Abbre | SORBS2 |
| Synonyms | Arg binding protein 2, Arg-binding protein 2, Arg/Abl interacting protein, Arg/Abl interacting protein 2, Arg/Abl-interacting protein 2, ArgBP2, KIAA0777, PRO0618, SRBS2, Sorbin, Sorbin and SH3 domain-containing protein 2, Sorbs2, sorbin and SH3 domain containing 2 |
| Swissprot | |
| Calculated MW | 124 kDa |
| Observed MW |
Refer to figures
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, perinuclear region. Apical cell membrane. Cell junction, focal adhesion. Cell projection, lamellipodium. Found at the Z-disk sarcomeres, stress fibers, dense bodies and focal adhesion. In pancreatic acinar cells, localized preferentially to the apical membrane. Colocalized with vinculin and filamentous actin at focal adhesions and lamellipodia of pancreatic cells. |
| Concentration | 1.02 mg/mL |
| Buffer | Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer and 50% glycerol. |
| Purification Method | Antigen affinity purification |
| Research Areas | Signal transduction |
| 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 | Arg and c-Abl represent the mammalian members of the Abelson family of non-receptor protein-tyrosine kinases.They interact with the Arg/Abl binding proteins via the SH3 domains present in the carboxy end of the latter group of proteins.This gene encodes the sorbin and SH3 domain containing 2 protein.It has three C-terminal SH3 domains and an N-terminal sorbin homology (SoHo) domain that interacts with lipid raft proteins.The subcellular localization of this protein in epithelial and cardiac muscle cells suggests that it functions as an adapter protein to assemble signaling complexes in stress fibers, and that it is a potential link between Abl family kinases and the actin cytoskeleton.Alternative splicing results in multiple transcript variants encoding different isoforms. |
Other Clones
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Unconjugated
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