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{{/_source.additionalInfo}}Anti-PAG1 | 20S Proteasome alpha subunit G1
(Cat#: AS19 4259)
Description
- Immunogen: Recombinant, full-length PAG1 of Arabidopsis thaliana, UniProt: O23715-1, TAIR: At2g27020 overexpressed in E.coli, purified from a gel piece
- Host: Rabbit
- Clonality: Polyclonal
- Purity: Serum
- Format: Lyophilized
- Quantity: 50 µl
- Reconstitution: For reconstitution add 50 µl, of sterile water
- Storage: Store lyophilized/reconstituted at -20°C (short tem, months) or at -80°C (long term, years) ; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
- Tested applications: Western blot (WB)
- Recommended dilutions: 1 : 5000 (WB)
- Expected | apparent MW: 27.4 | 26 kDa
- Confirmed reactivity: Arabidopsis thaliana
- Not reactive in: No confirmed exceptions from predicted reactivity are currently known
- PAG1 (20S Proteasome alpha subunit G1) is a component of the 20S core complex of the 26S proteasome. The 26S proteasome is composed of a core protease (CP), known as the 20S proteasome, capped at one or both ends by the 19S regulatory particle (RP/PA700). The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. Alternative name: 20S proteasome alpha subunit G-1, DiDi 17A-2a, Proteasome component 8, Proteasome subunit alpha type-7.
- Xie et al. (2024). Proteasome resides in and dismantles plant heat stress granules constitutively. Mol Cell. 2024 Sep 5;84(17):3320-3335.e7. doi: 10.1016/j.molcel.2024.07.033.Book et al. (2010). Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse array of plant proteolytic complexes. J Biol Chem. 2010 Aug 13;285(33):25554-69. doi: 10.1074/jbc.M110.136622.
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