Heat Shock Protein 90 alpha Active Protein | HSP90AA1 active protein

Heat Shock Protein 90 alpha, Recombinant, Human (HSP90a)

Cat. Num. AAA636190

• Gene Names: HSP90AA1; HSPCA
• Purity: Purified; ~60%
• Synonyms: Heat Shock Protein 90 alpha; Recombinant; Human (HSP90a); HSP90AA1 active protein

• Host: E Coli
• Purity/Purification: Purified; ~60%
• Form/Format: Supplied as a liquid in 45mM Tris-HCl, pH 8.0, 124mM sodium chloride, 2.4mM potassium chloride, 225mM imidazole, 3mM DTT, 10% glycerol.

• Application Notes: Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
• Specific Activity: Kd of 5.2nM
• Preparation and Storage: Aliquot to avoid repeated freezing and thawing and store at -70 degree C. Stable for 6 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

SDS-Page

(10% SDS-PAGE Coomassie staining using H1832-85A. Lane 1: 4ug H1832-85A. Lane 2: Protein Marker.)

Testing Data

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Related Product Information for HSP90AA1 active protein

The 90kD molecular chaperone family comprises several proteins including the 90kD heat shock protein, Hsp90 and the 94kD glucose-regulated protein, grp94 which are major molecular chaperones of the cytosol and of the endoplasmic reticulum. In mammalian cells there are at least two Hsp90 isoforms, Hsp90alpha and Hsp90beta which are encoded by separate genes. The amino acid sequence of human and yeast Hsp90alpha is 85% and 90% homologous to that of Hsp90beta respectively. All known members of the Hsp90 protein family are highly conserved, especially in the N-terminal and C-terminal regions which have been shown to contain independent chaperone sites with different substrate specificity. These ubiquitous and highly conserved proteins account for 1-2% of all cellular proteins in most cells. Hsp90 is part of the cellís powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by non-physiological conditions. However, in the absence of stress, Hsp90 is a necessary component of fundamental cellular processes such as hormone signalling and cell cycle control. In this context, several key regulatory proteins such as steroid receptors, cell cycle kinases involved in signal transduction and p53 have been identified as substrates of Hsp90. It has been suggested that Hsp90 acts as a capacitor for morphological evolution by buffering widespread variation, which may affect morphogenic pathways. Recent studies indicate that when Drosophila Hsp90 buffering is compromised by temperature for example, cryptic variants are expressed and selection can lead to the continued expression of these traits, even if Hsp90 function is restored.

Recombinant protein corresponding to human Heat Shock Protein 90 alpha, full length, with C-terminal His tag, expressed in E. coli. (NM_005348).

Product Categories/Family for HSP90AA1 active protein

Molecular Biology; MB-Heat Shock Proteins

NCBI and Uniprot Product Information

• NCBI GI #: 255653030
• NCBI GeneID: 100033837
• NCBI Accession #: NP_001157427.1
• NCBI GenBank Nucleotide #: NM_001163955.1
• UniProt Accession #: Q9GKX7
• Molecular Weight: 85.5kD
• NCBI Official Full Name: heat shock protein HSP 90-alpha
• NCBI Official Symbol: HSP90AA1
• NCBI Official Synonym Symbols: HSPCA
• NCBI Protein Information: heat shock protein HSP 90-alpha; Hsp90 alpha; heat shock protein 90 alpha; Heat shock protein HSP 90-alpha-like protein
• UniProt Protein Name: Heat shock protein HSP 90-alpha
• Protein Family: Heat shock protein
• UniProt Gene Name: HSP90AA1
• UniProt Synonym Gene Names: HSPCA
• UniProt Entry Name: HS90A_HORSE

Uniprot Description

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

By similarity.

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. Interacts with PPP5C (via TPR repeats); the interaction is direct and activates PPP5C phosphatase activity

By similarity.

Subcellular location: Cytoplasm

By similarity. Melanosome

By similarity.

Domain: The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1

By similarity.

Post-translational modification: S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1

By similarity.ISGylated

By similarity.

Sequence similarities: Belongs to the heat shock protein 90 family.