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{{/_source.additionalInfo}}Anti-HSP70B | Stromal alfa-HSP70 (algal)
(Cat#: AS06 175)
Description
- 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 µl of sterile water
- Storage: 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.
- Tested applications: Immunoprecipitation (IP), Western blot (WB)
- Recommended dilutions: 1 : 10 000 (WB)
- Expected | apparent MW: 71.9 kDa
- Confirmed reactivity: Chlamydomonas reinhardtii, Desmodesmus subspicatus, Physcomitrium patens, Chlorococcum dorsiventrale
- Not reactive in: No confirmed exceptions from predicted reactivity are currently known
- 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.
- Cvetkovska et 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.14203Gonzaga 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.Lang et 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.
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