Mouse Anti-Arabidopsis PBA1 Antibody (CBMOAB-38178FYC)
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Specifications
| Host species | Mouse (Mus musculus) |
| Species Reactivity | A. thaliana (Arabidopsis thaliana) |
| Clone | MO38178FC |
| Specificity | This antibody binds to Arabidopsis PBA1. |
| Format | Liquid or Lyophilized |
| Storage | Store at 4°C: short-term (1-2weeks) Store at -20°C: long-term and future use |
| Purity | > 90% was determined by SDS-PAGE |
| Purification | Purified with Protein A or G affinity chromatography |
| Cellular Localization | Nucleus; Vacuole; Cytosol; Other locations; Plasma Membrane |
Application Information
| Application | WB, ELISA |
| Application Notes | ELISA: 1:1000-1:3000 Other applications are to be developed. The optimal dilution should be determined by the end user. |
Target
| Introduction | The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. |
| Product Overview | Mouse Anti-Arabidopsis PBA1 Antibody is a mouse antibody against PBA1. It can be used for PBA1 detection in Western Blot, Enzyme-Linked Immunosorbent Assay. |
| Alternative Names | Proteasome subunit beta type; EC 3.4.25.1; PBA1; At4g31300 |
| UniProt ID | F4JRY2 |
| Protein Refseq | The length of the protein is 234 amino acids long. The sequence is show below: MDLNLDAPHSMGTTIIGVTYNGGVVLGADSRTSTGMYVANRASDKITQLTDNVYVCRSGSAADSQVVSDYVRYFLHQHTIQHGQPATVKVSANLIRMLAYNNKQNMLQTGLIVGGWDKYEGGKIYGIPLGGTVVEQPFAIGGSGSSYLYGFFDQAWKDNMTKEEAEQLVVKAVSLAIARDGASGGVVRTVIINSEGVTRNFYPGDKLQLWHEELEPQNSLLDILNAAGPEPMAM. |
Reference
| Reference | 1. Cai, Y. M., Yu, J., Ge, Y., Mironov, A., & Gallois, P. (2018). Two proteases with caspase-3-like activity, cathepsin B and proteasome, antagonistically control ER-stress-induced programmed cell death in Arabidopsis. New Phytologist, 218(3), 1143-1155. 2. Chung, T., Phillips, A. R., & Vierstra, R. D. (2010). ATG8 lipidation and ATG8-mediated autophagy in Arabidopsis require ATG12 expressed from the differentially controlled ATG12A AND ATG12B loci. The Plant Journal, 62(3), 483-493. 3. Pogány, M., Dankó, T., Kámán-Tóth, E., Schwarczinger, I., & Bozsó, Z. (2015). Regulatory proteolysis in Arabidopsis-pathogen interactions. International journal of molecular sciences, 16(10), 23177-23194. 4. Sueldo, D. J., & van der Hoorn, R. A. (2017). Plant life needs cell death, but does plant cell death need Cys proteases?. The FEBS Journal, 284(10), 1577-1585. |
| CBMOAB-02821CR | Mouse Anti-Yeast PBA1 Antibody (CBMOAB-02821CR) |
| MOFAB-212W | Rabbit Anti-PBA1 Antibody (MOFAB-212W) |
| MO-DKB-0360RA | Rabbit Anti-PBA1 Antibody (MO-DKB-0360RA) |
| MO-DKB-00396W | Rabbit Anti-PBA1 Antibody (MO-DKB-00396W) |
Figure 1 Profile of ATG8 proteins in wild type (WT) and various atg mutants. Total protein was extracted directly into SDS-PAGE sample buffer from seedlings and subjected to SDS-PAGE in the presence of urea followed by immunoblot analysis with antibodies against ATG8a and ATG5. Equal protein loads were confirmed by immunoblot analysis with anti-PBA1 antibodies. The genotypes of the various seedlings are indicated. The dashed lines, solid lines, and asterisk locate the group of free ATG8 proteins, the possible ATG8-phosphatidylethanolamine (PE) adducts, and the ATG8 cross-reacting species, respectively. The open and close arrowheads locate ATG5 and the ATG12-ATG5 conjugate, respectively.
Reference: Chung, T., Phillips, A. R., & Vierstra, R. D. (2010). ATG8 lipidation and ATG8-mediated autophagy in Arabidopsis require ATG12 expressed from the differentially controlled ATG12A AND ATG12B loci. The Plant Journal, 62(3), 483-493.