Hledali jste: B-Raf+inhibitor+1

Dodavatel: Apollo Scientific

Popis: MAPK/ERK Signalling Pathway

Katalogové číslo: (USBIR0495-55C)

Dodavatel: US Biological

Popis: Anti-Raf kinase inhibitor protein Rabbit Polyclonal Antibody

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (USBIR0495-52)

Dodavatel: US Biological

Popis: Anti-Raf Kinase Inhibitor Protein Mouse Monoclonal Antibody [clone: 6A175]

Měrná jednotka: 1 * 100 µG

Akce

Katalogové číslo: (USBIR0495-55B)

Dodavatel: US Biological

Popis: Anti-Raf kinase inhibitor protein Rabbit Polyclonal Antibody

Měrná jednotka: 1 * 100 µl

Akce

Dodavatel: ENZO LIFE SCIENCES

Popis: Potent B-Raf inhibitor.

Dodavatel: Apollo Scientific

Popis: Sorafenib is a multikinase inhibitor of Raf-1 B-Raf and VEGFR-2 with IC50 of 6 nM 22 nM and 90 nM in cell-free assays respectively.

Dodavatel: Apollo Scientific

Popis: Selective inhibitor of the mitogen-activated protein kinase kinases, MEK-1 and MEK-2, with 100-fold higher potency than PD 98059, but is, at most, a weak inhibitor of PKC, Raf, ERK, JNK, MEKK, MKK-3, MKK-4/SEK, MKK-6, Abl, Cdk2 and Cdk4. U0126 is an inhibitor of AP-1 transactivation in cell-based reporter assays. J. Biol. Chem. 273: 18623-18632 (1998).

Dodavatel: ENZO LIFE SCIENCES

Popis: Potent and specific inhibitor of the protein kinase c-Raf (IC50=70nM). Has no significant effect on many other protein kinases tested (even at 50µM) with the exception of p38 (SAPK2a) (IC50=2µM) and SAPK2b (p38β) (IC50=2µM). Induces a paradoxical >100-fold activation of c-Raf in whole cells.

Katalogové číslo: (APOSBISN0240-50MG)

Dodavatel: Apollo Scientific

Popis: MAPK/ERK Signalling Pathway

Měrná jednotka: 1 * 50 mg

Akce

Dodavatel: ENZO LIFE SCIENCES

Popis: The Screen-Well™ Kinase Inhibitor Library contains 80 known kinase inhibitors of well-defined activity. Inhibitors are supplied dissolved in DMSO at 10 mM and aliquoted into deep-well plates at either 100 or 500 ml per well. The library is an ideal tool for chemical genomics, assay development and other pharmacological applications. Includes inhibitors of these important kinases: Insulin/IGF Receptors, PI 3-Kinase, CaM Kinase II, JAK, PKA, CDK, JNK, PKC, CKI II, MAPK, RAF, EGFR, MEK, SAPK, GSK, MLCK, Src-family, IKK, PDGFR, VEGFR and many more.

Dodavatel: ENZO LIFE SCIENCES

Popis: Potent and selective cell permeable inhibitor of cRAF1 kinase (IC50 = 9 nM) with 100-fold selectivity over CDK1, CDK2, c-src, ERK2, MEK, p38, Tie2, VEGFR2 and c-fm. A useful tool for assessing the involvement of the Ras/Raf-1/ERK pathway in various signaling pathways. Displays neuroprotective effects in vivo through a MEK-ERK and Akt-independent mechanism.

Dodavatel: ENZO LIFE SCIENCES

Popis: 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.

Dodavatel: ENZO LIFE SCIENCES

Popis: 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.

Dodavatel: ENZO LIFE SCIENCES

Popis: 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.

Dodavatel: ENZO LIFE SCIENCES

Popis: 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.

Dodavatel: ENZO LIFE SCIENCES

Popis: 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.