Recombinant Phospho-Caveolin-1 (Tyr14) Monoclonal Antibody (AN302089L)
For research use only.
| Verified Samples | Verified Samples in WB: A431 |
| Dilution | WB 1:500-1:1000 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | phosphorylated human Caveolin-1 (Tyr14) peptide |
| Abbre | Phospho-Caveolin-1 (Tyr14) |
| Synonyms | PPH, CGL, BSCL, MSTP, cell growth-inhibiting protein, OTTHUMP, VIP, BSCL3, CGL3, LCCNS, MSTP085, PPH3, VIP21, CAV1, 22 kD, caveolae protein, caveolin 1 alpha isoform, caveolin 1 beta isoform, Caveolin 1 caveolae protein 22kDa, Caveolin1, Caveolin-1, cell growth-inhibiting protein 32, OTTHUMP00000025031, VIP 21, CAV |
| Swissprot | |
| Calculated MW | 20 kDa |
| Observed MW |
22 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 | Golgi apparatus, Cell membrane |
| Concentration | 1 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A purified |
| Research Areas | Cardiovascular, Signal Transduction, Tags & Cell Markers, Cancer, Metabolism |
| Clone No. | A813 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Caveolins are the principal structural components of the cholesterol/sphingolipid-enriched plasma membrane microdomain caveolae. Three members of the caveolin family (caveolin-1, -2, and -3) have been identified with different tissue distributions. Caveolins form hetero- and homo-oligomers that interact with cholesterol and other lipids. Caveolins are involved in diverse biological functions, including vesicular trafficking, cholesterol homeostasis, cell adhesion, and apoptosis, and are also implicated in neurodegenerative disease. Caveolins interact with multiple signaling molecules, such as Gα subunit, tyrosine kinase receptors, PKCs, Src family tyrosine kinases, and eNOS. It is believed that caveolins serve as scaffolding proteins for the integration of signal transduction. Phosphorylation at Tyr14 is essential for caveolin association with SH2 or PTB domain-containing adaptor proteins, such as GRB7. Phosphorylation at Ser80 regulates caveolin binding to the ER membrane and entry into the secretory pathway. |
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