Alternative Name(s):

HSP90AA1; HSP90A; HSPCAHeat shock protein HSP 90-alpha

Species: (Organism)

Sus scrofa (Pig)

Gene Names:

HSP90AA1

Tag info:

N-terminal 6xHis-tagged

Target Protein AA Sequence:

VEKERDKEVSDDEAEEKEDKEEEKEKEEKESEDKPEIEDVGSDEEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVR

Expression Region:

222-367aa

Subcellular Location:

Nucleus, Cytoplasm, Melanosome, Cell membrane

Tissue Specificity:

Preferentially expressed in pituitary gland, brain, adrenal gland, and testis, in comparison to other tissues.

Protein Length:

Partial

Pathway:

Mol. Weight:

19.7 kDa

Purity:

Greater than 90% as determined by SDS-PAGE.

Form:

Liquid or Lyophilized powder

Buffer:

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Research Areas:

Signal Transduction

Function:

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).

Involvement in disease:

Relevance:

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. 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 (By similarity). Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion (By similarity).

Reconstitution:

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. 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) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Families:

Heat shock protein 90 family

Reference:

"Molecular cloning and characterization of porcine cDNA encoding a 90-KDA heat shock protein and its expression following hyperthermia." Huang H.W., Lee W.C., Lin J.H., Jian S.C., Mao S.J., Yang P.C., Huang T.Y., Liu Y.C.Gene 226:307-315(1999) .