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HSP90C | alfa-HSP90C, heat shock protein (algal)

AS06 174  |  Clonality: Polyclonal  |  Host: Rabbit  | Reactivity: Chlamydomonas reinhardtii

HSP90C | alfa-HSP90C, heat shock protein (algal) in the group Antibodies Plant/Algal  / Environmental Stress / Heat shock at Agrisera AB (Antibodies for research) (AS06 174)
HSP90C | alfa-HSP90C, heat shock protein (algal)



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Product Information

Immunogen

C-terminal 238 amino acids of HSP90C, Q66T67, 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 ĩl
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 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 dilution 1 : 3000 (WB)
Expected | apparent MW

89 kDa

Reactivity

Confirmed reactivity Chlamydomonas reinhardtii
Predicted reactivity

Ostreococcus sp.


Species of your interest not listed? Contact us
Not reactive in No confirmed exceptions from predicted reactivity are currently known

Application examples

Additional information

HSP90C protein is easily degraded and degradation products are detected by this antibody

Related products

Background

Background

HSP90C is a nuclear-encoded, chloroplast-targeted chaperone of the HSP90 family. It forms dimers that interact with HSP70B. HSP90C displays a weak ATPase activity that is inhibited by radicicol.

Product citations

Selected references 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.14203
Perlaza et al. (2019). The Mars1 kinase confers photoprotection through signaling in the chloroplast unfolded protein response. Elife. 2019 Oct 15;8. pii: e49577. doi: 10.7554/eLife.49577.
Willmund & Schroda (2005). HSP90C is a bona-fide Hsp90 that interacts with plastidic HSP70B in Chlamydomonas reinhardtii. Plant Phys. 138, 2310–2322.
immunogen:

C-terminal 238 amino acids of HSP90C, Q66T67, expressed with N- and C-terminal hexahistidine tags in E. coli, purified with Ni-NTA

Reconstitution: For reconstitution add 100 ĩl of sterile water
Host: Rabbit
Clonality: Polyclonal
Purity: Serum
Format: Lyophilized
Quantity: 100 ĩl
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 dilution: 1 : 3000 (WB)
calculated | apparent molecular mass [kDa]:

89 kDa

Confirmed reactivity: Chlamydomonas reinhardtii
predicted reactivity:

Ostreococcus sp.


Species of your interest not listed? Contact us
not reactive in: No confirmed exceptions from predicted reactivity are currently known
additional information (application): HSP90C protein is easily degraded and degradation products are detected by this antibody
background:

HSP90C is a nuclear-encoded, chloroplast-targeted chaperone of the HSP90 family. It forms dimers that interact with HSP70B. HSP90C displays a weak ATPase activity that is inhibited by radicicol.

All references: 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.14203
Perlaza et al. (2019). The Mars1 kinase confers photoprotection through signaling in the chloroplast unfolded protein response. Elife. 2019 Oct 15;8. pii: e49577. doi: 10.7554/eLife.49577.
Willmund & Schroda (2005). HSP90C is a bona-fide Hsp90 that interacts with plastidic HSP70B in Chlamydomonas reinhardtii. Plant Phys. 138, 2310–2322.

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