Recombinant Activin A Receptor Type IB/ALK-4 Monoclonal Antibody (AN301427L)
For research use only.
| Verified Samples |
Verified Samples in WB: U87MG, HepG2, Mouse kidney Verified Samples in IF: SH-SY5Y |
| Dilution | WB 1:500-1:1000, IF 1:50 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, Mouse |
| Applications | WB, IF |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant human Activin A Receptor Type IB/ALK-4 fragment |
| Abbre | Activin A Receptor Type IB/ALK-4 |
| Synonyms | SKR, Activin Receptor-Like Kinase, Serine/Threonine-Protein Kinase Receptor R, ACVRLK, ALK, ACVR1B, ACTRIB, ACVRLK4, ALK4, SKR2, Activin Receptor Type IB, Activin Receptor Type-1B, Activin Receptor-Like Kinase 4, ACTR-IB, ALK-4, Serine/Threonine-Protein Kinase Receptor R2 |
| Swissprot | |
| Calculated MW | 52 kDa |
| Observed MW |
55 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 | Membrane |
| Concentration | 1 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A purified |
| Research Areas | Signal Transduction, Stem Cells |
| Clone No. | A122 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Transmembrane serine/threonine kinase activin type-1 receptor forming an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating a many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, type-2 receptors (ACVR2A and/or ACVR2B) act as a primary activin receptors whereas the type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor such as ACVR1B. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. |
Other Clones
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