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AGO set
Tag Antibody Set 

HSP70B | Stromal alfa-HSP70 (algal)

AS06 175  Clonality: Polyclonal  |  Host: Rabbit  |  Reactivity: Ch. reinhardtii, D. subspicatus, P. patens

HSP70B | Stromal alfa-HSP70 (algal) in the group Antibodies for Plant/Algal  / Environmental Stress / Heat shock at Agrisera AB (Antibodies for research) (AS06 175)

PRODUCT INFORMATION IN PDF

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355 €

Datasheet Product citations Protocols Add review

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 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 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
Not reactive in No confirmed exceptions from predicted reactivity are currently known.

Application examples

Additional information

Related products

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.

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