F/a 18 Non-hsp Support Parts

(Page 22) End item NSN parts page 22 of 28
Part Number
NSN
NIIN
530-12A Torque Motor
012960793
530408-101 A Fault-function Indicator Panel
013475720
530408-105 A Fault-function Indicator Panel
013475720
530408-109 A Fault-function Indicator Panel
013475720
532758-1 Electrical Receptacle Connector
011708295
53992 Ejection Seat Pin Key
011635300
55660-90008 Multimeter
012421583
57L414 Hydraulic Fluid Con Analysis Kit
001506486
58-C-1 Indicator Panel
014886467
59301 Thermal Insulation Pipe Covering
011232278
5943665-1 Maintenance Fixture
010824699
59440-14 Directional Control Linear Valve
014673557
5E1570/04-0024 Electrolytic Fixed Capacitor
013015790
5HKDH 105-263 Aft Generator Beari
014801700
5HKH 008-177 Aircra Ball Bearing
014801701
5M2370-001 Impedance Matching Network
011561160
5M2578-001 Aircraft Cockpit Light
013219903
5R9720-002-1621 Film Fixed Resistor
013174313
5R9720-002-2212 Film Fixed Resistor
013174312
5R9720-002-3523 Film Fixed Resistor
013303619
Page: 22

F/a 18 Non-hsp Support

Picture of F/a 18 Non-hsp Support

Hsp90 (heat shock protein 90) is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation. It also stabilizes a number of proteins required for tumor growth, which is why Hsp90 inhibitors are investigated as anti-cancer drugs.

Heat shock proteins, as a class, are among the most highly expressed cellular proteins across all species.

Heat shock protein 90 (Hsp90) is one of the most common of the heat-related proteins. The "90" comes from the fact that it weighs roughly 90 kiloDaltons. A 90 kDa protein is considered fairly large for a non-fibrous protein. Hsp90 is found in bacteria and all branches of eukarya, but it is apparently absent in archaea.

This protein was first isolated by extracting proteins from cells stressed by heating, dehydrating or by other means, all of which caused the cell’s proteins to begin to denature. However it was later discovered that Hsp90 also has essential functions in unstressed cells.

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