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Home > Products > 380 003

HSP90 alpha antibody - 380 003 K.O.

Heat shock proteins 90 (HSP90) are molecular chaperones
Rabbit polyclonal purified antibody
Cat. No.: 380 003
Amount: 50 µg
Price: $375.00
Cat. No. 380 003 50 µg specific antibody, lyophilized. Affinity purified with the immunogen. Albumin was added for stabilization. For reconstitution add 50 µl H2O to get a 1mg/ml solution in PBS. Then aliquot and store at -20°C to -80°C until use.
Antibodies should be stored at +4°C when still lyophilized. Do not freeze!
Applications
 
WB: 1 : 1000 (AP staining) gallery  
IP: not tested yet
ICC: 1 : 500 gallery  
IHC: not tested yet
IHC-P: 1 : 500 gallery  
Immunogen Synthetic peptide corresponding to AA 701 to 717 from human HSP90 α (UniProt Id: P07900)
Reactivity Reacts with: human (P07900), rat (P82995), mouse (P07901).
Other species not tested yet.
Specificity K.O. validated PubMed: 31849607
Matching control protein/peptide 380-0P
Data sheet 380_003.pdf

References for HSP90 alpha - 380 003

The Alpha Isoform of Heat Shock Protein 90 and the Co-chaperones p23 and Cdc37 Promote Opioid Anti-nociception in the Brain.
Lei W, Duron DI, Stine C, Mishra S, Blagg BSJ, Streicher JM
Frontiers in molecular neuroscience (2019) 12: 294. 380 003 IHC; KO verified; tested species: mouse
Cat. No.: 380 003
Amount: 50 µg
Price: $375.00
The Alpha Isoform of Heat Shock Protein 90 and the Co-chaperones p23 and Cdc37 Promote Opioid Anti-nociception in the Brain.
Lei W, Duron DI, Stine C, Mishra S, Blagg BSJ, Streicher JM
Frontiers in molecular neuroscience (2019) 12: 294. 380 003 IHC; KO verified; tested species: mouse
WB
ICC
IHC-P
Background
Heat shock proteins 90 (HSP 90) are molecular chaperones. Two isoforms (α and β) have been described so far. They promote the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. They undergo a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation.
HSP 90s interact dynamically with various co-chaperones that modulate their substrate recognition, ATPase cycle and chaperone function.
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