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  • 产品名称：HeatShockProtein90kDaalpha(Cytosolic),ClassAMember1(HSP90AA1)(AA535-732)(Active

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  • 产品厂商：ACROBiosystems
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简单介绍：
HeatShockProtein90kDaalpha(Cytosolic),ClassAMember1(HSP90AA1)(AA535-732)(Active)protein(GSTtag)
详情介绍：
Characteristics This protein carries a GST tag at the N-terminus. The protein has a calculated MW of 49.3 kDa. The protein migrates as 49 kDa under reducing (R) condition (SDS-PAGE).
Purity >85 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
Background Heat shock protein HSP 90-alpha (HSP90AA1 or HSP90A) is also known as Heat shock 86 kDa (HSP 86 or HSP86), Renal carcinoma antigen NY-REN-38, HSPC1, HSPCA, EL52, HSP89A, HSP90N, HSPCAL1, HSPCAL4, HSPN, Hsp89, Hsp90, LAP2, which belongs to the heat shock protein 90 family. HSP90AA1 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. HSP90AA1 interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.
Molecular Weight 49.3 kDa
NCBI Accession NP_005339
UniProt P07900
Pathways M Phase, Regulation of Cell Size, Signaling Events mediated by VEGFR1 and VEGFR2, VEGFR1 Specific Signals
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer 50 mM HEPES, 150 mM NaCl, pH 7.0
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).
Supplier Images
SDS-PAGE (SDS) image for Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1) (AA 535-732) (Active) protein (GST tag) (ABIN2181231) Human HSP90AA1, GST Tag on SDS-PAGE under reducing (R) condition. The gel was stained...
Background publications Martínez-Ruiz, Villanueva, González de Orduña, López-Ferrer, Higueras, Tarín, Rodríguez-Crespo, Vázquez, Lamas: "S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 102, Issue 24, pp. 8525-30, 2005 (PubMed).

Yang, Roe, Cliff, Williams, Ladbury, Cohen, Barford: "Molecular basis for TPR domain-mediated regulation of protein phosphatase 5." in: The EMBO journal, Vol. 24, Issue 1, pp. 1-10, 2005 (PubMed).

Forsythe, Jarvis, Turner, Elmore, Holt: "Stable association of hsp90 and p23, but Not hsp70, with active human telomerase." in: The Journal of biological chemistry, Vol. 276, Issue 19, pp. 15571-4, 2001 (PubMed).