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17-AAG ≥98% (by TLC)

Catalog Number: (89158-030)
Supplier: Enzo Life Sciences
Description: HSP90 inhibitor
Image Unavailable-102125-504

17-AAG (synthetic)

Catalog Number: (102125-504)
Supplier: Novus Biologicals
Description: Glendanamycin (GA), a benzoquinone ansamycin antibiotic, interferes with the action of Hsp90 leading to degradation of Hsp90 client proteins. GA itself however has undesirable properties such as poor aqueous solubility and liver toxicity; therefore, numerous analogs have been synthesized, such as 17-AAG. 17-AAG is an HSP-90 inhibitor that displays a 100-fold higher affinity for HSP-90 derived from tumor cells compared to HSP-90 from normal cells. 17-AAG inhibits Akt activation and expression in tumors and synergizes with a number of antitumor agents such as taxol, cisplatin and UCN-01 (400 nM 17-AAG, U937 cells).
Product Image-76344-648

17-AAG

Supplier: RPI
Description: 17-AAG (17-Allylamino-17-demethoxygeldanamycin) is a synthetic derivative of geldanamycin. Like geldanamycin, 17-AAG is recognised for its role as an inhibitor of heat shock protein 90 (Hsp90), a molecular chaperone involved in protein folding and stabilisation.

Image Unavailable-77192-882

17-AAG 98%

Supplier: Ambeed
Description: (4E,6Z,8S,9S,10E,12S,13R,14S,16R)-19-(Allylamino)-13-hydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3,20,22-trioxo-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl carbamate, Purity: 98%, CAS Number: 75747-14-7, Appearance: Form: solid, Storage: Store in freezer, under -20 C, Size: 10mg

Image Unavailable-AAJ66960-MC

17-AAG 99%

Supplier: Thermo Scientific Chemicals
Description: 17-(Allylamino)-17-demethoxygeldanamycin (17-AAG) inhibits heat shock protein 90 (Hsp90), the expression of heat shock factor-1, and the activity of oncogenic proteins such as N-ras, Ki-ras, c-Akt, and p185erB2

SDS Certificates

Image Unavailable-ALA126970-5MG

17-AAG ≥98%

Catalog Number: (ALA126970-5MG)
Supplier: ALADDIN SCIENTIFIC CORPORATION
Description: 17-AAG (Tanespimycin) is a potent HSP90 inhibitor with IC50 of 5 nM, having a 100-fold higher binding affinity for HSP90 derived from tumour cells than HSP90 from normal cells.A potent Hsp90 inhibitor for tumor cells

New Product


Product Image-101972-482

17-Allylaminogeldanamycin [allylamino-2,3-3H] ≥95% (by HPLC)

Supplier: MORAVEK BIOCHEMICALS MS
Description: 17-Allylaminogeldanamycin [allylamino-2,3-3H] ≥95% (by HPLC)

Image Unavailable-102513-634

17-AAG ≥98% (by HPLC)

Supplier: Adipogen
Description: Potent, less toxic analog of geldanamycin (Prod. No. BVT-0196). Inhibits the essential ATPase activity of HSP90. Telomerase activity inhibitor. Apoptosis inducer. Antitumor compound.

Small Business Enterprise

Image Unavailable-102513-660

17-DMAG ≥98% (by HPLC)

Supplier: Adipogen
Description: Less toxic, more potent synthetic derivative of geldanamycin (Prod. No. BVT-0196). Angiogenesis inhibitor. Heat shock protein 90 (HSP90) inhibitor. Apoptosis inducer. Shows higher antitumor activity than 17-AAG (Prod. No. BVT-0244).

Small Business Enterprise

Product Image-95057-936

Anti-HSP90 Rabbit Polyclonal Antibody

Supplier: Enzo Life Sciences
Description: The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.

Product Image-89106-714

Anti-HSP90 Mouse Monoclonal Antibody (DyLight® 488)

Supplier: Enzo Life Sciences
Description: The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.

SDS

Product Image-200062-754

Anti-HSP90 Mouse Monoclonal Antibody

Supplier: Enzo Life Sciences
Description: The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.

Product Image-10049-526

Anti-HSP90B Rabbit Polyclonal Antibody (PE (Phycoerythrin))

Catalog Number: (10049-526)
Supplier: Enzo Life Sciences
Description: The 90 kDa molecular chaperone family includes 90 kDa heat shock protein Hsp90 and 94 kDa glucose-regulated protein grp94, both major molecular chaperones of the cytosol and the endoplasmic reticulum. Mammalian cells express inducible Hsp90α and constitutive Hsp90β isoforms that are encoded by separate genes. The amino acid sequences of human and yeast Hsp90α are 85% and 90% homologous to those of Hsp90β, respectively. All known members of the Hsp90 protein family are highly conserved, especially in the N-terminal and C-terminal regions containing independent chaperone sites with different substrate specificity. These ubiquitous and highly conserved proteins account for 1-2% of all cellular protein in most cells. Hsp90 functions as part of the cell's powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by non-physiological conditions. In the absence of stress, however, Hsp90 provides a necessary component of such fundamental cellular processes as hormone signaling and cell cycle control by serving as a chaperone for many key signaling molecules including steroid receptors, cell cycle kinases involved in signal transduction, and p53. As many of these client proteins are known oncogenes, Hsp90 inhibitors such as 17-AAG, a geldanamycin analog, have been of benefit in the treatment of many cancers.
Product Image-89142-092

Anti-HSP90 Mouse Monoclonal Antibody (PE (Phycoerythrin))

Supplier: Enzo Life Sciences
Description: The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.

Product Image-10049-548

Anti-HSP90A Rabbit Polyclonal Antibody

Catalog Number: (10049-548)
Supplier: Enzo Life Sciences
Description: The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.
Product Image-10049-514

Anti-HSP90A Mouse Monoclonal Antibody [clone: K41009]

Catalog Number: (10049-514)
Supplier: Enzo Life Sciences
Description: The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90α/β), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.
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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us at 1-800-932-5000.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at Regulatory_Affairs@vwr.com
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