Anti-HSP90-2 | heat shock protein 90-2

(Cat#: AS11 1629)
AS11_1629
AS11_1629_1
Description
  • Immunogen: Full length recombinant HSP90-2 of Arabidopsis thaliana, UniProt: F4K6B6-1, TAIR: AT5G56030
  • 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: Western blot (WB)
  • Recommended dilutions: 1 : 3000 (WB)
  • Expected | apparent MW: 80.6 | 95 kDa (Arabidopsis thaliana)
  • Confirmed reactivity: Arabidopsis thaliana, Sorghum bicolor
  • Not reactive in: No confirmed exceptions from predicted reactivity are currently known
  • HSP90-2 (heat shock protein 90-2) is a constitutive isoform of HSP90, expressed in all tissues and abundant in root apical meristem, pollen and tapetum. Alternative names: ATHSP90.2, EARLY-RESPONSIVE TO DEHYDRATION 8, ERD8, HEAT SHOCK PROTEIN 90.2, HEAT SHOCK PROTEIN 81-2, HEAT SHOCK PROTEIN 81.2, HEAT SHOCK PROTEIN 90.2, HSP81-2, HSP81.2, HSP90.2.
  • Gao et al. (2021) Identification of a bacterial-type ATP-binding cassette transporter implicated in aluminum tolerance in sweet sorghum (Sorghum bicolor L.). Plant Signal Behav. 2021 Jul 3;16(7):1916211. doi: 10.1080/15592324.2021.1916211. Epub 2021 May 26. PMID: 34034635; PMCID: PMC8205057.Barghetti et al. (2017). Heat-shock protein 40 is the key farnesylation target in meristem size control, abscisic acid signaling, and drought resistance. Genes Dev. 2017 Nov 15;31(22):2282-2295. doi: 10.1101/gad.301242.117.He et a. (2012).SpecificMissenseAlleles of theArabidopsisJasmonicAcidCo-ReceptorCOI1RegulateInnateImmuneReceptorAccumulation andFunction. PloS Genetics, Open Access.
  • This product can be sold containing ProClin if requested

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