ClpC | Chloroplastic form of HSP100
AS01 001 | Clonality: Polyclonal | Host: Rabbit | Reactivity: A.thaliana, C.reinhardtii, cyanobacteria, Plectonema sp., Streptomyces sp.
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Recombinant ClpC (C-terminal domain overexpressed as fusion with maltose-binding protein), UniProt: Q55023
92 | 87 kDa
Algae (red), Catalpa bungei, Hordeum vulgare, Nicotiana tabacum, Ostreococcus sp., Oryza sativa, Populus trichocarpa, Physcomitrella patens, Pisum sativum, Solanum tuberosum, Zea mays
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ClpC is a chloroplastic protein of the Hsp100 family. It is believed to function as a housekeeping enzyme, both in its capacity as an independent molecular chaperone and as the regulatory component of the Clp protease.
Lee et al. (2018). Prolines in Transit Peptides Are Crucial for Efficient Preprotein Translocation into Chloroplasts. Plant Physiol. 2018 Jan;176(1):663-677. doi: 10.1104/pp.17.01553. Epub 2017 Nov 20.
Hu et al. (2015). Site-specific Nitrosoproteomic Identification of Endogenously S-Nitrosylated Proteins in Arabidopsis. Plant Physiol. 2015 Feb 19. pii: pp.00026.2015.
Rosano et al. (2011). Insights into the Clp/HSP100 chaperone system from chloroplasts of Arabidopsis thaliana. J Biol Chem. Aug 26;286(34):29671-80. (Western blot, Arabidopsis thaliana)
Karradt et al. (2008) NblA, a Key Protein of Phycobilisome Degradation, Interacts with ClpC, a HSP100 Chaperone Partner of a Cyanobacterial Clp Protease. J Biol Chem 283: 32394-32403.
Porankiewicz & Clarke (1997) Induction of the heat shock protein ClpB affects cold acclimation in the cyanobacterium Synechococcs sp. strain PCC7942. J Bacteriol 179:5111-5117.
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