catalog number :
MBS515103
products type :
Recombinant Protein
products full name :
HSP90 beta recombinant protein
products short name :
HSP90 beta
products name syn :
HSP90AB1; HSPC2; HSPCB; D6S182; HSP90B; HSP90beta Protein; HSP90b Protein
other names :
Homo sapiens heat shock protein 90kDa alpha (cytosolic), class B member 1 (HSP90AB1), transcript variant 2, mRNA; Heat shock protein HSP 90-beta; heat shock protein HSP 90-beta; HSP90-beta; heat shock 84 kDa; heat shock 90kD protein 1, beta; heat shock protein 90kDa alpha (cytosolic), class B member 1; Heat shock 84 kDa
products gene name :
HSP90 beta
products gene name syn :
HSP90AB1; HSPC2; HSPCB; D6S182; HSP90B
other gene names :
HSP90AB1; HSP90AB1; HSP84; HSPC2; HSPCB; D6S182; HSP90B; HSP90B; HSPC2; HSPCB; HSP 90; HSP 84; HSP84
uniprot entry name :
HS90B_HUMAN
form :
Recombinant protein stored in 50mM MOPS, pH7.0, 300mM NaCl, 150mM imidazole, 0.1mM PMSF, 0.2mM DTT, 25% glycerol.
storage stability :
Store product at -70 degree C. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles. Stability: 1yr at -70 degree C fo shipment.
tested application :
ATPase Assay, Western Blot (WB)
other info1 :
Type: Recombinant Fusion Protein. Species: Human. Tag Information: His tag. Expression System: Sf9 insect cells using baculovirus. Source Note: Recombinant full length human HSP90beta was expressed by baculovirus in Sf9 insect cells using C-terminal His tag. Acession Number: NM 007355
products categories :
Cell Stress & Chaperone Proteins; Signaling Proteins - Cell Stress & Chaperone Proteins
products description :
Recombinant full length human HSP90beta was expressed by baculovirus in Sf9 insect cells using a C-terminal His tag. Scientific Background: HSP90 is a member of the HSP90 family of proteins which are important molecular chaperones involved in signal transduction, cell cycle control, stress management, and folding, degradation, and transport of proteins (1). HSP90 proteins have been found in a variety of organisms suggesting that they are ancient and conserved. HSP90 binds to client proteins (such as steroid receptors, AKT, Bcr-Abl, Apaf-1, survivin, cyclin dependent kinases) and acts as a molecular chaperone. Failure of Hsp90 chaperone activity leads to misfolding of client proteins, which leads to ubiquitination and proteasome degradation, and thus deregulation of cellular homeostasis (2).
products references :
1. Csermely, P. et al: The 90-kDa molecular chaperone family: structure, function, and clinical applications. Pharmacol Ther. 1998 Aug;79(2):129-68. 2. Georgakis, G.V. et al: Heat-shock protein 90 inhibitors in cancer therapy: 17AAG and beyond. Future Oncol. 2005 Apr;1(2):273-81.
ncbi acc num :
NP_031381.2
ncbi gb acc num :
NM_007355
ncbi mol weight :
~91 kDa
ncbi pathways :
Antigen Processing And Presentation Pathway (83074); Antigen Processing And Presentation Pathway (485); Axon Guidance Pathway (105688); Developmental Biology Pathway (477129); Estrogen Signaling Pathway (799177); Estrogen Signaling Pathway (799197); Fcgamma Receptor (FCGR) Dependent Phagocytosis Pathway (771577); Immune System Pathway (106386); Inflammasomes Pathway (366166); Innate Immune System Pathway (106387)
ncbi summary :
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. [provided by RefSeq, Dec 2012]
uniprot summary :
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. 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. Ref.22 Ref.29. Subunit structure: Homodimer. Interacts with p53/TP53 . By similarity. Forms a complex with CDK6 and Hsp90/HSP90AB1. Interacts with UNC45A. Binding to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer. Interacts with CHORDC1 and DNAJC7 . By similarity. Interacts with FKBP4. Ref.17 Ref.22 Ref.25. Subcellular location: Cytoplasm. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.17 Ref.21. Domain: The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins . By similarity. Post-translational modification: Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro). Ref.24ISGylated. Ref.18S-nitrosylated; negatively regulates the ATPase activity . Probable. Sequence similarities: Belongs to the heat shock protein 90 family. Sequence caution: The sequence AAD14062.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.The sequence CAB66478.1 differs from that shown. Reason: Frameshift at position 709.