HSP-90 alpha; HSP 86; HSP 86; Renal carcinoma antigen NY REN 38; Heat shock 86 kDa; Heat shock 90kDa protein 1 alpha; Heat shock protein 90kDa alpha (cytosolic) class A member 1; heat shock protein 90kDa alpha (cytosolic), class A member 2; Heat shock pro
Cat:
SLM51215M
Species Reactivity：
Human,Mouse,Rat,
Immunogen：
KLH conjugated synthetic peptide derived from human Hsp90
Format：
Liquid
Storage instructions：
Shipped at 4℃. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles.
Concentration：
1mg/ml
Clonality：
Monoclonal
Isotype：
IgG1
Applications：
WB=1:500-1000not yet tested in other applications.optimal dilutions/concentrations should be determined by the end user.
Host：
Mouse
Product Overview：
Sample: Lane 1: Mouse Testis tissue lysates Lane 2: Mouse Cerebrum tissue lysates Lane 3: Mouse Placenta tissue lysates Lane 4: Rat Cerebrum tissue lysates Lane 5: Rat Placenta tissue lysates Lane 6: Human U251 cell lysates Lane 7: Human Molt-4 cell lysates Lane 8: Human HL60 cell lysates Lane 9: Human A549 cell lysates Primary: Anti-HSP90 (SLM51215M) at 1/1000 dilutionSecondary: IRDye800CW Goat Anti-Mouse IgG at 1/20000 dilutionPredicted band size: 81 kDObserved band size: 85 kD
Hsp90 (heat shock protein 90) is a molecular chaperone and is one of the most abundant proteins in unstressed cells. It is an ubiquitous molecular chaperone found in eubacteria and all branches of eukarya, but it is apparently absent in archaea. Whereas cytoplasmic Hsp90 is essential for viability under all conditions in eukaryotes, the bacterial homologue HtpG is dispensable under non-heat stress conditions.
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.
Subunit: 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.
Subcellular Location: Cytoplasm. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Post-translational modifications: ISGylated.
S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1.
Similarity: Belongs to the heat shock protein 90 family.
Sample:
Lane 1: Mouse Testis tissue lysates
Lane 2: Mouse Cerebrum tissue lysates
Lane 3: Mouse Placenta tissue lysates
Lane 4: Rat Cerebrum tissue lysates
Lane 5: Rat Placenta tissue lysates
Lane 6: Human U251 cell lysates
Lane 7: Human Molt-4 cell lysates
Lane 8: Human HL60 cell lysates
Lane 9: Human A549 cell lysates
Primary: Anti-HSP90 (SLM51215M) at 1/1000 dilution
Secondary: IRDye800CW Goat Anti-Mouse IgG at 1/20000 dilution
Predicted band size: 81 kD
Observed band size: 85 kD
Product Feedback Wall
Specific References (1) | SLM51215M has been referenced in 1 publications.
[IF=4.749] Gaoqian Zhao. et al. Biomimetic Platform Based on Mesoporous Platinum for Multisynergistic Cancer Therapy. Acs Biomater Sci Eng. 2021;XXXX(XXX):XXX-XXX WB,IHC ; Human,Mouse.
