Rabbit anti-Human HSP90AB1 Polyclonal Antibody

Uniprot Id

P08238

Target Species

Human

Target Name

HSP90AB1

Target Full Name

Heat shock protein HSP 90-beta

Target 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 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. 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. They first 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. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery. Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription. Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10.

Target Subcellular Location

Cytoplasm. Melanosome. Nucleus. Secreted. Cell membrane. Dynein axonemal particle.

Target Protein Families

Heat shock protein 90 family

Target Research Area

Signal Transduction

Target Synonyms

90 kda heat shock protein beta HSP90 beta; D6S182; FLJ26984; Heat shock 84 kDa; Heat shock 90kD protein 1; beta ; Heat shock 90kDa protein 1 beta; Heat shock protein 90 alpha family class B member 1; Heat shock protein 90 kDa; Heat shock protein 90kDa alpha (cytosolic) class B member 1; Heat shock protein 90kDa alpha family class B member 1; Heat shock protein beta ; Heat shock protein HSP 90 beta ; Heat shock protein HSP 90-beta; HS90B_HUMAN; HSP 84; HSP 90; HSP 90 b; HSP 90b; HSP84; HSP90 BETA ; hsp90ab1; HSP90B; HSPC2; HSPCB

Target Background

This gene encodes a member of the heat shock protein 90 family; these proteins are involved in signal transduction, protein folding and degradation and morphological evolution. This gene encodes the constitutive form of the cytosolic 90 kDa heat-shock protein and is thought to play a role in gastric apoptosis and inflammation. Alternative splicing results in multiple transcript variants. Pseudogenes have been identified on multiple chromosomes.