Catalog No.
Product Name
Application
Product Information
Citations
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HSP70 Inhibitor
DMT003096 is a selective inhibitor of HSP70, a heat shock protein that plays a critical role in cellular stress responses. Its upregulation has been associated with various cancers, including breast, lung, colon, and cervical cancer. This compound is valuable for research applications targeting cancer therapies and investigating the role of HSP70 in tumor progression and survival mechanisms. -
Hsp90 Inhibitor
Hsp90-IN-40 is a specific inhibitor targeting the C-terminal domain of heat shock protein 90 (Hsp90). It demonstrates significant antiproliferative activity against breast cancer cell lines SKBr3 and MCF-7, with IC50 values of 2.57 µM and 2.43 µM, respectively. By disrupting the function of Hsp90, Hsp90-IN-40 promotes the degradation of Hsp90-dependent proteins, thereby inhibiting cancer cell growth. This compound is valuable for research applications focusing on breast cancer therapeutics and mechanisms of Hsp90 inhibition. -
HSP90 Inhibitor
STA-1474 is a potent and selective inhibitor of Heat Shock Protein 90 (HSP90), primarily functioning by disrupting its chaperone activities, which are crucial for the stability and function of numerous oncogenic proteins. This compound induces apoptosis in tumor cells and exhibits significant antitumor efficacy in spontaneous canine cancer models, such as osteosarcoma and thyroid carcinoma. STA-1474 is valuable for research on solid tumors, including osteosarcoma and breast cancer, and offers insights into the role of HSP90 in cancer biology. -
Hsp90 Inhibitor
Hsp90-IN-15 is a potent Hsp90 inhibitor that exhibits significant anticancer activity. This compound promotes apoptosis in cancer cells and effectively induces cell cycle arrest at the S phase. Hsp90-IN-15 also reduces the expression levels of Hsp90 in HeLa cells, making it a valuable tool for research into cancer therapies targeting the Hsp90 chaperone pathway. -
HSP90 Inhibitor
Hsp90-IN-38 is a potent inhibitor of heat shock protein 90 (HSP90), displaying a strong binding affinity with a dissociation constant (Kd) of 87 nM. This compound effectively inhibits HSP90 ATPase activity, with an IC50 of 0.13 μM. Biological activity has been demonstrated in various cancer cell lines, including HCT116, MCF-7, SKBr3, K562, and A549, with reported IC50 values of 0.187, 0.072, 0.105, 0.403, and 0.31 μM, respectively. Hsp90-IN-38 serves as a valuable tool for research into cancer biology and HSP90-related pathways. -
Hsp90 Inhibitor
PU-20F is a potent Hsp90 inhibitor characterized by an EC50 value of 6.8 μM. This compound competes with Geldanamycin for binding to Hsp90, effectively regulating the activity of this crucial molecular chaperone. PU-20F promotes the degradation of the oncogenic Her2 tyrosine kinase and has demonstrated the ability to inhibit the proliferation of breast cancer cells. It serves as a valuable tool for research focused on breast cancer biology and therapeutic strategies. -
Hsp90β Inhibitor
KUNB106 is a selective inhibitor of Hsp90β, demonstrating binding affinities (KDs) of 91 nM for Hsp90β and 38 μM for Hsp90α. This compound exhibits notable antiproliferative activity against various cancer cell lines, including MDA-MB-231, A549, and SKOV-3, making it a valuable tool for studying triple negative breast cancer. KUNB106's selective inhibition of Hsp90β highlights its potential in oncology research focused on targeted therapies. -
Hsp90 Inhibitor
PU3 is an Hsp90 inhibitor that targets the conserved ATP/ADP pocket of the Hsp90 protein, competing effectively with geldanamycin and other compounds. This reagent has been shown to induce the degradation of key oncogenic proteins like Her2, subsequently inhibiting breast cancer cell proliferation through mechanisms such as retinoblastoma protein hypophosphorylation, G1 phase cell cycle arrest, and differentiation. PU3 presents a promising avenue for cancer research, particularly in the context of targeted cancer therapies. -
HSP70/SIRT2 Inhibitor
HSP70/SIRT2-IN-2 is a dual inhibitor targeting SIRT2 and HSP70, demonstrating an IC50 of 45.1±5.0 μM for SIRT2. This compound exhibits significant antitumor activity, making it a valuable tool for cancer research. Its ability to simultaneously inhibit these two proteins positions HSP70/SIRT2-IN-2 as a useful candidate for studies focused on tumor progression and potential therapeutic strategies. -
HSP Inhibitor
BMS-358233 is a small molecule inhibitor targeting heat shock protein 90 (Hsp90). By competing with geldanamycin, BMS-358233 induces the degradation of various proteins, including HER2, leading to the inhibition of breast cancer cell growth. This compound causes hypophosphorylation of the retinoblastoma protein, resulting in G1 phase cell cycle arrest and differentiation. BMS-358233 represents a novel class of synthetic Hsp90 inhibitors, offering potential therapeutic strategies for treating various cancers. -
Hsp90 Inhibitor
Flavokawain 1i is a potent Hsp90 inhibitor, targeting the heat shock protein 90, which plays a critical role in protein folding and stability. This compound demonstrates significant anti-cell proliferation activity, making it a valuable tool in cancer research. Its ability to disrupt Hsp90 function can provide insights into cancer cell growth mechanisms and therapeutic strategies. -
Cathepsin D/HSP90 Inhibitor
Tasiamide B is a potent inhibitor of Cathepsin D and HSP90, derived from the marine cyanobacteria Symploca sp. This linear peptide serves as a valuable scaffold for the development of inhibitors targeting aspartic proteases. Tasiamide B has demonstrated significant efficacy in skin cancer studies by effectively interacting with HSP90, highlighting its potential in cancer research and therapeutic applications. -
HSP90 Inhibitor
17-DMAP-GA is a potent inhibitor of Heat Shock Protein 90 (HSP90), derived from the Geldanamycin structure. This compound disrupts HSP90's chaperone function, leading to cell cycle abnormalities and apoptosis in cancer cells. It is utilized in research to study the role of HSP90 in tumorigenesis and to explore therapeutic strategies in cancer treatment. -
HSPA5 Inhibitor
HM03 trihydrochloride is a selective inhibitor of HSPA5 (Heat shock 70kDa protein 5, also known as Bip or Grp78). It exhibits potent anticancer activity, making it a valuable tool for research in cancer biology. This compound facilitates the exploration of HSPA5's role in cellular stress responses and its implications in tumor progression and treatment resistance. -
Hsp90 Inhibitor
HSP90-IN-32 is a selective inhibitor of the C-terminal domain of heat shock protein 90 (Hsp90). It exhibits significant anti-proliferative effects in various melanoma cell lines, including SKMel173, SKMel103, SKMel19, and A375, with IC50 values of 1.01 μM, 0.782 μM, 0.607 μM, and 1.413 μM, respectively. This compound holds potential for research focused on developing novel anti-cancer therapeutics targeting Hsp90. -
Aha1/Hsp90 Disruptor
KU-177 is an effective disruptor of the Aha1/Hsp90 complex. It inhibits Aha1-driven enhancement of Hsp90-dependent tau aggregation, demonstrating an IC50 of 4.08 μM in disrupting Aha1/Hsp90 interactions without affecting Hsp90's ATPase activity. This compound is applicable in research focused on tauopathies, providing valuable insights into neurodegenerative processes. -
HSP90 Inhibitor
Hsp90-IN-39 is a selective inhibitor of the HSP90α isoform. This compound exhibits significant antiproliferative activity across multiple cancer cell lines, including MCF-7, HCT116, SKBr3, K562, and A549. Hsp90-IN-39 is a valuable tool for cancer research, providing insights into HSP90-related pathways and therapeutic potential in oncology. -
HSP90/MAO-A inhibitor
MAO A/HSP90-IN-2 is a dual inhibitor targeting HSP90 and MAO A, exhibiting IC50 values of 0.016 μM and 4.58 μM, respectively. This compound enhances HSP70 expression while concurrently decreasing HER2, phospho-Akt, and IFN-γ induced PD-L1 levels in GL26 cells. It effectively inhibits the growth of both Temozolomide-sensitive and resistant glioblastoma cells, alongside other cancer types such as colon cancer, leukemia, and non-small cell lung cancer. MAO A/HSP90-IN-2 shows promise in addressing tumor immune evasion, making it a valuable tool for cancer research. -
Hsp90 Inhibitor
Hsp90-IN-44 is a selective Hsp90 inhibitor with an IC50 of 9.8 µM. This compound demonstrates significant inhibitory activity, making it a valuable tool for cancer research. Hsp90-IN-44 can be utilized in studies aimed at understanding Hsp90's role in oncogenesis and evaluating potential therapeutic strategies targeting this chaperone protein. -
HSP90 Antagonist
17-AEP-GA is a selective antagonist of HSP90, demonstrating potent inhibition of glioblastoma cell proliferation, survival, migration, and invasion. This compound is valuable for research applications focused on cancer biology, particularly in elucidating the role of HSP90 in oncogenic processes and therapeutic interventions in glioblastoma. -
HSP90 Inhibitor
HSP90i is a potent inhibitor of the heat shock protein 90 (HSP90), a key molecular chaperone involved in the stabilization and folding of client proteins. This compound demonstrates significant biological activity relevant to cancer research and therapeutic applications, particularly in the development of targeted therapies. HSP90i can also serve as an important intermediate for synthesizing ligand-mediated targeted protein degradation agents, such as dPDL1-4, facilitating advancements in targeted drug delivery systems. -
HSP Inhibitor
STA-2842 is a selective inhibitor of heat shock protein HSP90, demonstrating potential therapeutic effects in the context of autosomal dominant polycystic kidney disease (ADPKD). By modulating signaling pathways activated by mutations in PKD1 or PKD2 genes, STA-2842 effectively reduces renal cyst formation and inhibits kidney growth. In preclinical models, this compound has shown promise in slowing the progression of ADPKD, making it a valuable tool for understanding disease mechanisms and developing targeted interventions. -
HSP Inhibitor
17-GMB-APA-GA is a potent inhibitor of Heat Shock Protein 90 (HSP90), known for its role in protein folding and cellular stress responses. This compound is particularly useful in research focused on latent Toxoplasma gondii infections. Its ability to disrupt HSP90 function presents valuable opportunities for studying therapeutic strategies targeting this essential chaperone in infectious disease contexts. -
Hsp90 Inhibitor
HSP90-IN-14 is a potent inhibitor of heat shock protein 90 (Hsp90), exhibiting a dissociation constant (Kd) of 0.26 μM. This compound demonstrates significant antiviral activity against influenza viruses, showing EC50 values of 2.6 μM for A/H3N2, 3.9 μM for A/H1N1, and 17 μM for influenza B in MDCK cell assays. HSP90-IN-14 is a valuable tool for research into Hsp90's role in viral infections and therapeutic interventions. -
Hsp70 Inhibitor
YM-1 tosylate is a stable analog of MKT-077 that functions as an orally active inhibitor of Hsp70. This compound has been shown to induce cell death in HeLa cells, while also up-regulating p53 and p21 protein levels. YM-1 tosylate is valuable for research applications focused on cancer biology and cellular stress responses. -
HSP90 Inhibitor
DDO-6691 is a potent inhibitor of heat shock protein 90 (HSP90), targeting its role in protein folding and stabilization. This compound demonstrates significant antiproliferative activity against various tumor cell lines, particularly HCT-116 colon cancer cells, with an IC50 of 1.08 μM. DDO-6691 also effectively inhibits tumor growth in the HCT-116 xenograft mouse model, highlighting its potential for cancer research and therapeutic applications. -
Combined with Hsp90
AMP-PCP is a potent ATP analogue that selectively binds to the N-terminal domain of Hsp90 with a Kd value of 3.8 μM. This binding promotes the formation of the active homodimeric structure of Hsp90, enhancing its chaperone activity. AMP-PCP is valuable in research applications focused on understanding the molecular mechanisms of Hsp90 modulation and its role in protein folding and stability in various cellular contexts. -
HSP Inhibitor
Monorden diacetate is an effective Hsp90 inhibitor that demonstrates significant potential in the development of new fungicides. By targeting the heat shock protein 90 (HSP90), it disrupts the molecular chaperone activity essential for the stability and function of various client proteins. This compound is valuable for research applications focused on fungal biology and disease management. -
HSP Induction Inhibitor
NSC-134754 is a dehydroemetine derivative that functions as a heat shock protein induction inhibitor. It specifically targets Hsp72 and Hsp27 at the post-transcriptional level, without affecting overall protein synthesis, HSF-1 transcriptional activity, or Hsp mRNA levels. Preclinical studies indicate that NSC-134754 exhibits minimal toxicity while enhancing the sensitivity of cancer cells to proteasome and Hsp90 inhibitors. This reagent is applicable in research involving multiple myeloma, prostate carcinoma, and colon carcinoma. -
HSP
HSP90-IN-12 is a potent inhibitor of Heat Shock Protein 90 (HSP90), a chaperone protein essential for protein folding and stability. This compound exhibits significant anti-proliferative effects across various cancer cell lines, making it a valuable tool in cancer research. HSP90-IN-12 disrupts the regulation of HSP90-related proteins and effectively inhibits the HSP90-mediated refolding of luciferase in vitro, highlighting its potential for studying HSP90 dynamics and therapeutic applications in oncology. -
HSP90 Inhibitor
MPC-0767 is a selective and potent inhibitor of heat shock protein 90 (HSP90). As an L-alanine ester proagent of MPC-3100, it exhibits enhanced chemical stability, making it suitable for in vivo applications. MPC-0767 is primarily utilized in research applications focused on cancer biology, as it disrupts the chaperone function of HSP90 and thereby influences the stability of various oncogenic client proteins. -
Hsp90-TPR2A Interaction Inhibitor
Hsp90-IN-43 is a potent inhibitor of the Hsp90-TPR2A interaction, exhibiting an IC50 value of 360 nM and a Kd of 928 nM. This compound effectively inhibits the proliferation of BT474 breast cancer cells, making it a valuable tool for research in breast cancer biology. Its specific activity allows for deeper investigation into the role of Hsp90 in cancer progression and therapeutic response. -
Dye Tethered Hsp90 Inhibitor
HS-131 is a dye-tethered inhibitor that targets heat shock protein 90 (Hsp90). This compound exhibits the ability to selectively bind to and inhibit Hsp90, facilitating the detection of oncogene-driven breast cancers across various molecular subtypes. HS-131 is a valuable research tool for studying the role of Hsp90 in cancer biology and for developing novel therapeutic strategies targeting breast cancer. -
Hsp90α/Hsp90β Inhibitor
PU-11 is a selective inhibitor of Hsp90α and Hsp90β, targeting the ATP-binding pocket of these heat shock proteins. It exhibits IC50 values of 18.6 μM and 89.8 μM, along with Kd values of 2 μM for Hsp90α and 4.2 μM for Hsp90β, demonstrating a preference for Hsp90α due to the unique Ser52 residue. PU-11 is applicable in research related to neurodegenerative disorders, providing insights into the role of Hsp90 in cellular stress responses and protein homeostasis. -
HSP Inhibitor
HSP90-IN-28 is a selective inhibitor of heat shock protein 90 (Hsp90), demonstrating an IC50 value of 0.46 μM for Hsp90α and approximately 48-fold selectivity over Hsp90β (IC50 = 22.28 μM). This compound is instrumental in research focused on cellular stress responses, cancer biology, and protein homeostasis. Its specificity makes HSP90-IN-28 an effective tool for studying the role of Hsp90 in various physiological and pathological processes. -
FKBP51-Hsp90 Inhibitor
FKBP51-Hsp90-IN-2 is a selective inhibitor of the FKBP51-Hsp90 protein-protein interaction, demonstrating IC50 values of 0.4 µM for FKBP51 and 5 µM for FKBP52. This compound has been shown to enhance cellular energy metabolism and promote neurite growth. Its efficacy makes FKBP51-Hsp90-IN-2 a valuable tool in research focused on neurodegenerative diseases and cancer. -
MAO A/HSP90 Inhibitor
MAO A/HSP90-IN-1 is a dual inhibitor targeting MAO A and HSP90, exhibiting IC50 values of 1.77 μM in glioblastoma GL26 cells and 0.019 μM for HSP90α. This compound effectively inhibits MAO A activity, disrupts HSP90 binding, and downregulates HER2 and phospho-Akt expression, leading to reduced growth of glioblastoma cells. Additionally, MAO A/HSP90-IN-1 decreases PD-L1 expression, which may hinder tumor immune escape and suppress T cell activation. This reagent serves as a valuable tool for research on brain tumor-related diseases. -
HSP90 Inhibitor
HSP90-IN-29 is a selective inhibitor of heat shock protein 90 (HSP90), exhibiting a potent IC50 value of 30 nM. This benzoxazole derivative demonstrates significant antitumor activity, making it a valuable tool for cancer research. Its specific targeting of HSP90 allows for the exploration of its role in oncogenesis and the development of therapeutic strategies against malignancies. -
p38 Kinase/HSP Activator
(±)-Iroxanadine serves as a p38 kinase and heat shock protein (HSP) activator, demonstrating vasculoprotective properties. This compound is pertinent for research into atherosclerosis and various vascular diseases, facilitating studies aimed at understanding the molecular mechanisms underlying these conditions. Its activation of key signaling pathways makes it a valuable tool for exploring therapeutic targets in cardiovascular research. -
Hsp90 Inhibitor
HSP90-IN-35 is a selective Hsp90 inhibitor that exhibits potent antitumor activity, with an IC50 value for Her2 in the range of 0.05 to 0.5 μM. This compound is valuable for research applications focused on cancer biology and therapeutic development. Additionally, HSP90-IN-35 can be utilized in the synthesis of PROTACs, facilitating the exploration of targeted protein degradation strategies in cellular models. -
Hsp90 Inhibitor
C086 is a potent inhibitor of Heat Shock Protein 90 (Hsp90), a crucial chaperone involved in protein folding and stability. This compound has been shown to inhibit cell cycle progression and induce apoptosis across various cell types. It also exhibits anti-metastatic properties, making it a valuable tool for research in cancer biology and therapeutic development targeting Hsp90. -
Hsp90 Activator
Araloside C is an Hsp90 activator primarily derived from the natural saponin found in Aralia elata. This compound demonstrates significant anti-inflammatory properties and has shown protective effects against myocardial ischemia/reperfusion injury. Its ability to modulate Hsp90 activity makes it a valuable tool for research in cardiovascular protection and inflammation-related studies. -
HSP70 Inhibitor
HSP70-IN-5 is a selective inhibitor of the heat shock protein 70 (HSP70). It demonstrates an IC₅₀ of 0.6 μM in HSP70/DnaJ-mediated luciferase reconstitution assays. This compound serves as a valuable biochemical probe for investigating the functional role of HSP70 and its co-chaperone DnaJ in diverse biological processes, including protein folding and stress response pathways. -
Aha1-Hsp90 Complex Inhibitor
Hsp90-IN-34 is a potent inhibitor of the Aha1-Hsp90 chaperone complex, displaying a high affinity for Hsp90 and Aha1 with a dissociation constant (KDapp) of 23.5 µM. This compound interferes with the ATPase activity of Hsp90 by disrupting its interaction with Aha1, thereby influencing chaperone-mediated protein folding and stability. Hsp90-IN-34 is valuable for research into cancer biology and the modulation of protein homeostasis. -
HSP90 Inhibitor
ML189 is a selective inhibitor of HSP90, a critical chaperone involved in protein folding and stability. By disrupting HSP90 activity, ML189 induces the degradation of client proteins, which can affect cellular proliferation and survival. This compound is primarily utilized in research related to infectious diseases, including candidiasis, and provides insights into the role of HSP90 in pathogen biology and therapeutic development. -
HSP90 Inhibitor
ML229 is a high-affinity inhibitor of HSP90, a chaperone protein crucial for the stability and function of various client proteins. This compound demonstrates significant biological activity in modulating heat shock protein activity, making it a valuable tool for investigating the role of HSP90 in various cellular processes. ML229 has potential applications in the research of infectious diseases, including candidiasis, as it can interfere with the growth and survival of pathogenic organisms reliant on HSP90 for their virulence. -
HSP90 Inhibitor
BIIB-028 is an orally active inhibitor of heat shock protein 90 (Hsp90), primarily targeting its ATP-binding site. By disrupting Hsp90 function, BIIB-028 promotes the degradation of client proteins essential for cancer cell survival and proliferation. This compound is valuable for research in cancer biology and therapeutic development aimed at targeting Hsp90. -
Hsp70 Inhibitor
JG-48 is an inhibitor of the heat shock protein 70 (Hsp70), a molecular chaperone involved in protein folding and stabilization. This compound effectively reduces tau protein levels in various tauopathy models, making it a valuable tool for studying neurodegenerative diseases. Its specific targeting of Hsp70 provides insights into the role of protein aggregation in tau-related pathologies. -
HSP60 Inhibitor
DCEM1 is a potent inhibitor of heat shock protein 60 (HSP60), disrupting its interaction with ClpP and thereby impeding the mitochondrial unfolded protein response. This compound has been shown to significantly inhibit β-catenin expression and ATP production in both PC-3 and TKO cell lines. DCEM1 is a valuable tool for investigating the role of HSP60 in prostate cancer research and understanding its impact on cellular metabolism and signaling pathways. -
Hsp90 Inhibitor
BIIB021 mesylate is a potent inhibitor of the heat shock protein 90 (Hsp90). This orally active compound effectively inhibits the proliferation of chronic myeloid leukemia (CML) cells, demonstrating IC50 values of 513.99 nM for K562, 603.53 nM for K562/G, 110.08 nM for 32Dp210, and 148.07 nM for 32Dp210-T315I cell lines. BIIB021 promotes the degradation of the BCR-ABL protein and suppresses the β-catenin/c-Myc pathway, while also inducing autophagy in CML cells. This compound serves as a valuable tool for research focused on CML and Hsp90-related pathways.
