Recombinant Glutathione Peroxidase 4 Monoclonal Antibody (AN301875L)
For research use only.
| Verified Samples | Verified Samples in WB: HeLa, LNCaP, Mouse liver, Rat liver |
| Dilution | WB 1:500-1:1000 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, Rat, Mouse |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant human Glutathione Peroxidase 4 fragment |
| Abbre | Glutathione Peroxidase 4 |
| Synonyms | glutathione peroxidase, GSHPx, GPx, GPX4, GPx-4, GSHPx-4, MCSP, PHGPx, SMDS, snGPx, snPHGPx, glutathione peroxidase 4, glutathione peroxidase 4, GPx-4, GSHPx-4, MCSP, PHGPx, SMDS, snGPx, snPHGPx |
| Swissprot | |
| Calculated MW | 22 kDa |
| Observed MW |
22 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 | Cytoplasm, Mitochondrion |
| 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, Cancer, Metabolism |
| Clone No. | A587 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | The selenoprotein glutathione peroxidase 4 (GPX4) is a master regulator of ferroptosis, a form of programmed cell death induced by iron-dependent lipid peroxidation. GPX4 converts lipid hydroperoxides to non-toxic lipid alcohols, therefore preventing ferroptosis. Research studies show that selenium enhances GPX4 expression and inhibits ferroptotic death to protect neurons. In addition, some therapy-resistant cancer cells depend on GPX4 to survive. Loss of GPX4 leads to ferroptosis and thus prevents tumor relapse in mice. Furthermore, redox homeostasis mediated by GPX4 is essential for activation of the cytosolic DNA-sensing cGAS-STING pathway and initiation of the subsequent innate immune response. |
Other Clones
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Unconjugated
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