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{{/_source.additionalInfo}}Anti-RPN1a 26S proteasome regulatory subunit RPN1a
(Cat#: AS19 4264)
Description
- Immunogen: Recombinant, full-length Arabidopsis thaliana RPN1a protein sequence UniProt: Q9SIV2-1, TAIR: At2g20580 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 : 1000 (WB)
- Expected | apparent MW: 98.1 | 100 kDa
- Confirmed reactivity: Arabidopsis thaliana
- Not reactive in: No confirmed exceptions from predicted reactivity are currently known
- RPN1a (26S proteasome regulatory subunit RPN1a) Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins (By similarity). Required during embryogenesis and involved in innate immune response, proteasome-mediated ubiquitin-dependent protein catabolic process, protein catabolic process, regulation of cell cycle, regulation of protein catabolic process, response to salicylic acid, ubiquitin-dependent protein catabolic process. Alternative names: 26S proteasome non-ATPase regulatory subunit 2 homolog A, AtRPN1a, 26S proteasome regulatory subunit S2 homolog A.
- Meng, Wang, Hao, et al. (2023) RNA-binding protein MAC5A interacts with the 26S proteasome to regulate DNA damage response in Arabidopsis. Plant Physiol. 2023;191(1):446-462. doi:10.1093/plphys/kiac510Yang et al. (2004). Purification of the Arabidopsis 26 S proteasome: biochemical and molecular analyses revealed the presence of multiple isoforms. J Biol Chem. 2004 Feb 20;279(8):6401-13.
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