Anti-HSP70B | Stromal alfa-HSP70 (algal)
Product Specifications
Background
HSP70Bis 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.
Host
Rabbit
Reactivity
Chlamydomonas reinhardtii, Desmodesmus subspicatus, Physcomitrium patens, Chlorococcum dorsiventrale
Not reactive in
No confirmed exceptions from predicted reactivity are currently known
Immunogen
Mature HSP70B protein UniProt:A8HYV3,expressed with N- and C-terminal hexahistidine tags inE. coli, purified with Ni-NTA
Clonality
Polyclonal
Applications
Immunoprecipitation (IP), Western blot (WB)
Dilution
1 : 10 000 (WB)
Purity
Serum
Format
Lyophilized
Reconstitution
For reconstitution add 100 µl of sterile water
Molecular Weight
71.9 kDa
References & Citations
Cvetkovskaet al. (2022) A constitutive stress response is a result of low temperature growth in the Antarctic green alga Chlamydomonas sp. UWO241. Plant, Cell & Environment, 45, 156– 177. https://doi.org/10.1111/pce.14203GonzagaHeredia-Martinez et al. (2018). Chloroplast damage induced by the inhibition of fatty acid synthesis triggers autophagy in Chlamydomonas. Plant Physiol, Sept. 2018.Diaz-Troyaet al. (2011). Inhibition of protein synthesis by TOR inactivation revealed a conserved regulatory mechanism of the BiP chaperone in Chlamydomonas. Plant Physiol.Langet al. (2011).Simultaneous isolation of pure and intact chloroplasts and mitochondria from moss as the basis for sub-cellular proteomics. Plant Cell Rep. 2011 Feb;30(2):205-15.doi: 10.1007/s00299-010-0935-4.
Storage Conditions
Store lyophilized/reconstituted at -20°C; 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.
Product Datasheet
https://cdn.gentaur.com/products/451/6867f70b994c49e6dc670261/datasheet/as06 175.pdf
CAS Number
9007-83-4
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