BAIAP2L1 Polyclonal Antibody (E-AB-52462)
For research use only.
| Verified Samples |
Verified Samples in WB: HepG2, Hela, A172, A549, A431 Verified Samples in IHC: Human esophagus cancer, Human thyroid cancer |
| Dilution | WB 1:500-1:2000, IHC 1:25-1:100 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB, IHC |
| Clonality | Polyclonal |
| Immunogen | Fusion protein of human BAIAP2L1 |
| Abbre | BAIAP2L1 |
| Synonyms | BAI1 associated protein 2 like 1, BAI1 associated protein 2 like protein 1, BAI1-associated protein 2-like protein 1, BI2L1, Baiap2l1, Brain specific angiogenesis inhibitor 1 associated protein 2 like protein 1, Brain-specific angiogenesis inhibitor 1-associate |
| Swissprot | |
| Calculated MW | 57 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, cytoskeleton. Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites. |
| Concentration | 0.5 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 | This gene encodes a member of the IMD (IRSp53/MIM homology domain) family. Members of this family can be subdivided in two groups, the IRSp53-like and MIM-like, based on the presence or absence of the SH3 (Src homology 3) domain. The protein encoded by this gene contains a conserved IMD, also known as F-actin bundling domain, at the N-terminus, and a canonical SH3 domain near the C-terminus, so it belongs to the IRSp53-like group. This protein is the substrate for insulin receptor tyrosine kinase and binds to the small GTPase Rac. It is involved in signal transduction pathways that link deformation of the plasma membrane and remodeling of the actin cytoskeleton. It also promotes actin assembly and membrane protrusions when overexpressed in mammalian cells, and is essential to the formation of a potent actin assembly complex during EHEC (Enterohemorrhagic Escherichia coli) pedestal formation. |
Other Clones
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Unconjugated
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