protein

Recombinant Human Hsp90 alpha

MBS197044

0.01 mg

145 USD

Recombinant Protein

Recombinant Human Hsp90 alpha

Hsp90 alpha

heat shock protein HSP 90-alpha isoform 1; Heat shock protein HSP 90-alpha; heat shock protein HSP 90-alpha; HSP 86; heat shock 86 kDa; heat shock 90kD protein 1, alpha; heat shock 90kDa protein 1, alpha; renal carcinoma antigen NY-REN-38; heat shock 90kD protein, alpha-like 4; heat shock 90kD protein 1, alpha-like 4; heat shock protein 90kDa alpha (cytosolic), class A member 1; Heat shock 86 kDa; HSP 86; HSP86; Renal carcinoma antigen NY-REN-38

Hsp90 alpha

HSP90AA1; HSP90AA1; HSPN; LAP2; HSP86; HSPC1; HSPCA; Hsp89; Hsp90; HSP89A; HSP90A; HSP90N; HSPCAL1; HSPCAL4; FLJ31884; HSP90A; HSPC1; HSPCA

HS90A_HUMAN

E Coli

Human Hsp90 alpha

Greater than 95% as determined by SDS-PAGE and RP-HPLC.

Sterile-filtered colorless solution in 20mM Tris-HCl, pH 7.4 and 100mM NaCl. Purified by proprietary chromatographic techniques.

Store at 4 degree C if entire vial will be used within 2-4 weeks. Store at or below - 20 degree C for longer periods of time. Addition of a carrier protein (such as 0.1% HSA or BSA) is recommended for long-term storage.

Hsp90, a mammalian heat shock protein, is a molecular chaperone that helps to keep a target protein in a folding-competent state. It has been found in cell cytosol, nucleus, and endoplasmic reticulum of many different tissues. Hsp90 functions as a dimer. It has an ATP-binding site and low ATPase activity. Its chaperone activity is enhanced at high temperatures, and its function is sensitive to bivalent cation concentrations. Recombinant human Hsp90 produced in E. coli is a single, non-glycosylated polypeptide containing 732 amino acids with a molecular weight of 86.8kDa. It is expressed with a 6X His-tag.

153792590

NP_001017963.2

NM_001017963.2

P07900

84,660 Da

Antigen Processing And Presentation Pathway 83074!!Antigen Processing And Presentation Pathway 485!!Axon Guidance Pathway 105688!!Cell Cycle, Mitotic Pathway 105765!!Centrosome Maturation Pathway 105807!!Class I PI3K Signaling Events Pathway 138022!!Class I PI3K Signaling Events Mediated By Akt Pathway 138020!!EBV LMP1 Signaling Pathway 198790!!ErbB Receptor Signaling Network Pathway 138016!!G2/M Transition Pathway 105801

HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. There are 2 major cytosolic HSP90 proteins, HSP90AA1, an inducible form, and HSP90AB1 (MIM 140572), a constitutive form. Other HSP90 proteins are found in endoplasmic reticulum (HSP90B1; MIM 191175) and mitochondria (TRAP1; MIM 606219) (Chen et al., 2005 [PubMed 16269234]).[supplied by OMIM]

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.15 Ref.21. Subunit structure: Homodimer. Interacts with AHSA1, FNIP1, HSF1, SMYD3 and TOM34. Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex. Interacts with CHORDC1 and DNAJC7. Interacts with STUB1 and UBE2N; may couple the chaperone and ubiquitination systems. Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.32 Ref.45 Ref.46. Subcellular location: Cytoplasm. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.30. Domain: The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1. Post-translational modification: ISGylated. Ref.27S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1. Sequence similarities: Belongs to the heat shock protein 90 family.

0.01 mg

145 USD