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Magic™ Membrane Protein Sus scrofa (Pig) HSP90AA1 (Heat shock protein 90 alpha family class A member 1) for Antibody Discovery (CAT#: MP1417J)

Datasheet
This product is a 19.7 kDa Sus scrofa (Pig) HSP90AA1 membrane protein expressed in Baculovirus. The protein is for research use only and is not approved for use in humans or in clinical diagnosis.

Product Specifications

  • Host Species
  • Sus scrofa (Pig)
  • Target Protein
  • HSP90AA1
  • Protein Length
  • Partial (222-367aa)
  • Protein Class
  • ATP-binding Cassette Transporter
  • Molecular Weight
  • 19.7 kDa
  • Sequence
  • VEKERDKEVSDDEAEEKEDKEEEKEKEEKESEDKPEIEDVGSDEEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVR

Product Description

  • Expression Systems
  • Baculovirus
  • Tag
  • N-6xHis
  • Reconstitution
  • Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration).
  • Purity
  • >90% as determined by SDS-PAGE
  • Buffer
  • Liquid: Tris/PBS-based buffer, 5%-50% glycerol
    Lyophilized powder: Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Target

  • Target Protein
  • HSP90AA1
  • Full Name
  • Heat shock protein 90 alpha family class A member 1
  • Introduction
  • Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Interacts with HECTD1 (via N-terminus) (By similarity).
  • Alternative Names
  • HSP90AA1; HSP90A; HSPCA; Heat shock protein HSP 90-alpha

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