HSP70B | Stromal alfa-HSP70 (algal)
AS06 175 | Clonality: Polyclonal | Host: Rabbit | Reactivity: Ch. reinhardtii, D. subspicatus, P. patens
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Product Information
Immunogen
mature HSP70B protein UniProt: A8HYV3, expressed with N- and C-terminal hexahistidine tags in E. coli, purified with Ni-NTA
Host
Rabbit
Clonality
Polyclonal
Purity
Serum
Format
Lyophilized
Quantity
100 µl
Reconstitution
For reconstitution add 100 ĩl of sterile water
Storage
Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles, Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes
Tested applications
Immunoprecipitation (IP), Western blot (WB)
Recommended dilution
1 : 10 000 (WB)
Expected | apparent MW
71,9 kDa
Reactivity
Confirmed reactivity
Chlamydomonas reinhardtii, Desmodesmus subspicatus, Physcomitrella patens
Predicted reactivity
Dunaliella salina, Cyanobacteria
Species of your interest not listed? Contact us
Species of your interest not listed? Contact us
Not reactive in
No confirmed exceptions from predicted reactivity are currently known
Application examples
Additional information
Background
Background
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.
Product citations
Selected references
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.
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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