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Targeted therapy! The Capetin Prize winning "Click Chemistry" can be used like this!Targeted therapy! The Nobel Prize winning "Click Chemistry" can be used like this!2025-02-06
10 Results for "
human Hsp90α
" in MedChemExpress (MCE) Product Catalog:
Products (10)
10 Results for "human Hsp90α" in MCE Product Catalog:
CH5138303 is a potent and orally active Hsp90 inhibitor. CH5138303 shows high binding affinity for N-terminal Hsp90α, with Kd of 0.52 nM. CH5138303 shows potent anti-proliferative activity against human cancer cell lines (HCT116 and NCI-N87), with IC50 values of 0.098 and 0.066 μM, respectively. CH5138303 shows high oral bioavailability in mice (F=44.0%). CH5138303 shows potent antitumor efficacy in a human NCI-N87 gastric cancer xenograft model .
PU-H54, a Grp94-selective inhibitor, can be used for the research of breast cancer. Hsp90 chaperone family, comprised in humans of four paralogs, Hsp90α, Hsp90β, Grp94 and Trap-1, has important roles in malignancy . PU-H54 is a click chemistry reagent, it contains an Alkyne group and can undergo copper-catalyzed azide-alkyne cycloaddition (CuAAc) with molecules containing Azide groups.
Research Areas:
Hsp90-IN-17 hydrochloride is a Hsp90 inhibitor. Hsp90-IN-17 hydrochloride binds to the N-terminal ATP-binding pocket of Hsp90, inhibits its chaperone function, and induces the degradation of Hsp90 client proteins. Hsp90-IN-17 hydrochloride inhibits cancer cell proliferation. Hsp90-IN-17 hydrochloride can be used in the research of ovarian cancer .
Cat. No.: HY-148215
CAS No.: 1253584-78-9
Hsp90-IN-17 is a Hsp90 inhibitor. Hsp90-IN-17 binds to the N-terminal ATP-binding pocket of Hsp90, inhibits its chaperone function, and induces the degradation of Hsp90 client proteins. Hsp90-IN-17 inhibits cancer cell proliferation. Hsp90-IN-17 can be used in the research of ovarian cancer .
Cat. No.: HY-155064
CAS No.: 3031102-92-5
Target:
Research Areas:
TRAP1-IN-2 is a TRAP1-selective inhibitor, with a Kd value of 0.04 μM against human TRAP1. TRAP1-IN-2 exhibits more than 250-fold selectivity for Grp94 and shows no detectable affinity for cytosolic Hsp90α/β. TRAP1-IN-2 selectively induces the degradation of TRAP1 client proteins by inhibiting its ATPase activity, without triggering the heat shock response or affecting cytosolic Hsp90 client proteins. TRAP1-IN-2 suppresses oxidative phosphorylation, shifts cellular metabolism toward glycolysis, disrupts the stability of the TRAP1 tetramer and the mitochondrial membrane potential. TRAP1-IN-2 can be used in studies related to prostate cancer, cervical cancer, and ovarian cancer .
Cat. No.: HY-111300
CAS No.: 848952-37-4
G3130 is a reversible HSP90 inhibitor with a Kd value of 280 nM for the N-terminal ATP-binding domain of purified human Hsp90α. G3130 binds to the adenine site via a multi-hydrogen bond network . G3130 induces the degradation of Hsp90 client protein Her-2 in breast cancer cells. G3130 activates Hsp70 promoter-driven luciferase expression in 293T cells. G3130 can be used in breast cancer-related research .
Cat. No.: HY-180195
Research Areas:
Grp94-IN-3 (Compound 47) is a selective ATP competitive inhibitor of Grp94, with a Kd value of 76 nM. Grp94-IN-3 has a much lower affinity for Hsp90α, with a Kd value of 9.17 μM. Grp94-IN-3 induces the degradation of integrin α2 (Integrin α2) in MDA-MB-231 cells and reduces the intracellular accumulation of mutant cardiac proteins in human trabecular meshwork cells. Grp94-IN-3 can be used for the study of metastatic cancer and open-angle glaucoma .
Cat. No.: HY-116053
CAS No.: 1454619-18-1
Target:
Research Areas:
PU-11 is a Hsp90α/Hsp90β inhibitor with IC50 values of 18.6 μM and 89.8 μM and Kd values of 2 and 4.2 μM. PU-11 binds to the ATP-binding pocket of Hsp90α and Hsp90β and displays selective binding preference for Hsp90α over Hsp90β, mediated by the nonconserved Hsp90α Ser52 residue. PU-11 can be used for the research of neurodegenerative disorders .
Cat. No.: HY-P703083
Purity: ≥ 85%, as determined by reducing SDS-PAGE.
Synonyms: Hsp90AA1; Heat Shock 86 KDa; Prev. HspC1; FLJ31884; Prev. HspCA; Hsp90A; Prev. HspCAL4; Hsp 86; Hsp90N; Hsp86; Hsp89; LAP-2; Hsp90; Heat Shock Protein 90kDa Alpha Family Class A Member 1; Heat Shock Protein 90kDa Alpha (Cytosolic), Class A Member 1; Heat Shock 90kD Protein 1, Alpha-Like 4; Epididymis Secretory Sperm Binding Protein Li 65p; Heat Shock 90kD Protein, Alpha-Like 4; Epididymis Luminal Secretory Protein 52; Hsp90AA1 Protein; Lipopolysaccharide-Associated Protein 2; HspCAL1; Heat Shock Protein Family C Member 1; Hsp89A; Heat Shock 90kDa Protein 1, Alpha; Hsp103; Renal Carcinoma Antigen NY-REN-38; EL52; Heat Shock 90kD Protein 1, Alpha; HspN; Heat Shock Protein Hsp 90-Alpha; LAP2; LPS-Associated Protein 2; Heat Shock Protein 90 Alpha Family Class A Member 1; HEL-S-65p
Species:
Human
Source:
E. coli
Cat. No.: HY-P706229
Purity: ≥ 90%, as determined by reducing SDS-PAGE.
Synonyms: Hsp90AA1; Heat Shock 86 KDa; Prev. HspC1; FLJ31884; Prev. HspCA; Hsp90A; Prev. HspCAL4; Hsp 86; Hsp90N; Hsp86; Hsp89; LAP-2; Hsp90; Heat Shock Protein 90kDa Alpha Family Class A Member 1; Heat Shock Protein 90kDa Alpha (Cytosolic), Class A Member 1; Heat Shock 90kD Protein 1, Alpha-Like 4; Epididymis Secretory Sperm Binding Protein Li 65p; Heat Shock 90kD Protein, Alpha-Like 4; Epididymis Luminal Secretory Protein 52; Hsp90AA1 Protein; Lipopolysaccharide-Associated Protein 2; HspCAL1; Heat Shock Protein Family C Member 1; Hsp89A; Heat Shock 90kDa Protein 1, Alpha; Hsp103; Renal Carcinoma Antigen NY-REN-38; EL52; Heat Shock 90kD Protein 1, Alpha; HspN; Heat Shock Protein Hsp 90-Alpha; LAP2; LPS-Associated Protein 2; Heat Shock Protein 90 Alpha Family Class A Member 1; HEL-S-65p
Species:
Human
Source:
E. coli
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Protocols
Targeted therapy! The Capetin Prize winning "Click Chemistry" can be used like this!Targeted therapy! The Nobel Prize winning "Click Chemistry" can be used like this!A suitable model is crucial in drug screening experiments. Organs can mimic the three-dimensional functional structure of internal organs, have similar spatial organization to corresponding organs, maintain some key characteristics, and reproduce some physiological functions. They are widely used for modeling and personalized drug screening physiological functions.2025-02-06
