STI1 Antibody (E-10): sc-390225
- STI1 Antibody (E-10) is a mouse monoclonal IgM κ provided at 200 µg/ml
- raised against amino acids 203-453 mapping near the C-terminus of STI1 of human origin
- recommended for detection of STI1 of mouse, rat and human origin by WB, IP, IF, IHC(P) and ELISA
- At present, we have not yet completed the identification of the preferred secondary detection reagent(s) for STI1 Antibody (E-10). This work is in progress.
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STI1 Antibody (E-10) is a mouse monoclonal IgM antibody that detects stress-induced-phosphoprotein 1 (STI1) in mouse, rat, and human samples through various applications including western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), immunohistochemistry, and enzyme-linked immunosorbent assay (ELISA). STI1 plays a crucial role as a co-chaperone for heat shock proteins HSP70 and HSP90, particularly during the cellular heat shock response, which is vital for maintaining protein homeostasis under stress conditions. STI1 exists in both monomeric and dimeric forms, allowing conformational adaptation to effectively organize and facilitate HSP70 and HSP90 function. Such conformational flexibility is essential as HSP90 operates as an ATPase that requires proper recruitment of client proteins and correct folding to exert chaperoning effects. By acting as a scaffold, STI1 aids in recruiting client proteins to the relaxed, ADP-bound state of HSP90, thereby suppressing ATP turnover during the loading phase and ensuring optimal chaperone complex function. Anti-STI1 antibody (E-10) serves as an invaluable tool for researchers studying protein folding and stress response mechanisms in various biological contexts.
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LI-COR® and Odyssey® are registered trademarks of LI-COR Biosciences
STI1 Antibody (E-10) References:
- Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle. | Richter, K., et al. 2003. J Biol Chem. 278: 10328-33. PMID: 12525481
- Independent regulation of Hsp70 and Hsp90 chaperones by Hsp70/Hsp90-organizing protein Sti1 (Hop1). | Song, Y. and Masison, DC. 2005. J Biol Chem. 280: 34178-85. PMID: 16100115
- Dynamics of the regulation of Hsp90 by the co-chaperone Sti1. | Lee, CT., et al. 2012. EMBO J. 31: 1518-28. PMID: 22354036
- ¹H, ¹⁵N and ¹³C backbone resonance assignments of the TPR1 and TPR2A domains of mouse STI1. | Maciejewski, A., et al. 2013. Biomol NMR Assign. 7: 305-10. PMID: 23070844
- Polyglutamine-rich suppressors of huntingtin toxicity act upstream of Hsp70 and Sti1 in spatial quality control of amyloid-like proteins. | Wolfe, KJ., et al. 2014. PLoS One. 9: e95914. PMID: 24828240
- Escorted by chaperones: Sti1 helps to usher precursor proteins from the ribosome to mitochondria. | Hansen, KG., et al. 2016. FEBS J. 283: 3335-7. PMID: 27515587
- The STI1-domain is a flexible alpha-helical fold with a hydrophobic groove. | Fry, MY., et al. 2021. Protein Sci. 30: 882-898. PMID: 33620121
- The Hsp70-Hsp90 go-between Hop/Stip1/Sti1 is a proteostatic switch and may be a drug target in cancer and neurodegeneration. | Bhattacharya, K. and Picard, D. 2021. Cell Mol Life Sci. 78: 7257-7273. PMID: 34677645
- Stress-inducible phosphoprotein 1 (HOP/STI1/STIP1) regulates the accumulation and toxicity of α-synuclein in vivo. | Lackie, RE., et al. 2022. Acta Neuropathol. 144: 881-910. PMID: 36121476
- The structural and biophysical basis of substrate binding to the hydrophobic groove in Ubiquilin Sti1 domains. | Onwunma, J., et al. 2024. bioRxiv.. PMID: 39026758
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
STI1 Antibody (E-10) | sc-390225 | 200 µg/ml | $322.00 |