HSP70B | Stromal alfa-HSP70 (algal)
AS06 175 | Clonality: Polyclonal | Host: Rabbit | Reactivity: Ch. reinhardtii, D. subspicatus, P. patens
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mature HSP70B protein UniProt: A8HYV3, expressed with N- and C-terminal hexahistidine tags in E. coli, purified with Ni-NTA
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Reactant: Chlamydomonas reinhardtii (Green Alga)
Application: Western Blotting
Pudmed ID: 23118617
Journal: PLoS Biol
Figure Number: 5A
Published Date: 2012-11-03
First Author: Teng, Y. S., Chan, P. T., et al.
Impact Factor: 7.279Open Publication
Protein import into Chlamydomonas chloroplasts is not differentially regulated.[35S]Met-labeled precursors of Cr-prRBCS, Cr-prL11, prOE23, prTic40, and prL11 were imported into chloroplasts isolated from synchronized cultures of Chlamydomonas 1, 6, and 11 h after the start of the third light cycle and used for import experiments. Samples were analyzed by SDS-PAGE and autoradiography. An equal number of chloroplasts were loaded in each lane of the same gel. The amount of Chlamydomonas chloroplast Hsp70B was analyzed by immunoblotting and used for normalization of quantifications in the bar graph shown below each gel. The amount of mature protein imported at hour 1 was set as 100%. Data shown are mean ą SD, n?=?3. m, mature form; p, precursor form; TR, in vitro–translated precursor proteins before import.
HSP70B is a nuclear-encoded, chloroplast-targeted chaperone of the HSP70 family. It is the major HSP70 in the stroma of Chlamydomonas reinhardtii chloroplasts. It interacts with HSP90C, CGE1, CDJ2, and VIPP1.
Gonzaga Heredia-Martinez et al. (2018). Chloroplast damage induced by the inhibition of fatty acid synthesis triggers autophagy in Chlamydomonas. Plant Physiol, Sept. 2018.
Diaz-Troya et al. (2011). Inhibition of protein synthesis by TOR inactivation revealed a conserved regulatory mechanism of the BiP chaperone in Chlamydomonas. Plant Physiol, in press.
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