Product Name Hsp90 alpha (11102P-1000)
Description 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 an N-terminal 6X His-tag
Target Hsp90 alpha
Product Background 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.
Species Reactivity Human
Source Escherichia coli
Concentration Lot Specific
Formulation Sterile-filtered colorless solution (1mg/ml) in 20mM Tris-HCl, pH 7.4 and 100mM NaCl.
Buffer Formulation 20 mM Tris
Buffer pH pH 7.4
Molecular Mass Molecular weight of 86.8 kDa
Purity >90% as determined by RP- HPLC and SDS-PAGE
Target Name Heat shock protein 90kDa alpha (cytosolic), member A1
Target ID Hsp90 alpha
Alternative Names Hsp90alpha
Sequence Location Nucleus , Cytoplasm , Melanosome , Cell membrane , Mitochondrion , Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Sequence MGSSHHHHHH SSGLVPRGSH MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIR YESLTDPSKL DSGKELHINL IPNKQDRTLT IVDTGIGMTK ADLINNLGTI AKSGTKAFME ALQAGADISM IGQFGVGFYS AYLVAEKVTV ITKHNDDEQY AWESSAGGSF TVRTDTGEPM GRGTKVILHL KEDQTEYLEE RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKED KEEEKEKEEK ESEDKPEIED VGSDEEEEKK DGDKKKKKKI KEKYIDQEEL NKTKPIWTRN PDDITNEEYG EFYKSLTNDW EDHLAVKHFS VEGQLEFRAL LFVPRRAPFD LFENRKKKNN IKLYVRRVFI MDNCEELIPE YLNFIRGVVD SEDLPLNISR EMLQQSKILK VIRKNLVKKC LELFTELAED KENYKKFYEQ FSKNIKLGIH EDSQNRKKLS ELLRYYTSAS GDEMVSLKDY CTRMKENQKH IYYITGETKD QVANSAFVER LRKHGLEVIY MIEPIDEYCV QQLKEFEGKT LVSVTKEGLE LPEDEEEKKK QEEKKTKFEN LCKIMKDILE KKVEKVVVSN RLVTSPCCIV TSTYGWTANM ERIMKAQALR DNSTMGYMAA KKHLEINPDH SIIETLRQKA EADKNDKSVK DLVILLYETA LLSSGFSLEDPQTHANRIYR MIKLGLGIDE DDPTADDTSA AVTEEMPPLE GDDDTSRMEE VD
Biological 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 rPubMed:11274138, PubMed:11276205, PubMed:12526792, PubMed:15577939, PubMed:15937123, PubMed:20628368, PubMed:24613385, PubMed:25609812, PubMed:27353360, PubMed:29127155, PubMed:25973397, PubMed:26991466, PubMed:27295069}.
Background 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.
Storage Store at 2 - 8ºC. Do not Freeze.
Dilution Instructions Dilute in PBS or medium that is identical to that used in the assay system.