Hledali jste: JNK-IN-8

Katalogové číslo: (BOSSBS-3009R-CY5)

Dodavatel: Bioss

Popis: Bad is a member of the Bcl2 family and acts to promote apoptosis by forming heterodimers with the survival proteins Bcl2 and BclxL, thus preventing them from binding with BAX. Bad is found on the outer mitochondrial membrane and, once phosphorylated in response to growth stimuli, translocates to the cytoplasm. The phosphorylation status of Bad represents a key checkpoint for death or cell survival. JNK-induced phosphorylation of BAD serine 128 promotes the apoptotic role of Bad by opposing the inhibitory effect of growth factor on Bad-mediated apoptosis. Cdc2-induced phosphorylation of Bad serine 128 has an inhibitory effect on its interaction with 14-3-3 proteins. The latter interaction is critical for Bad phosphorylation at serine 155, a site within the BH3 domain that leads to the release of BclxL and the promotion of cell survival. Alternative splicing of this gene results in two transcript variants which encode the same isoform.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-3009R-A488)

Dodavatel: Bioss

Popis: Bad is a member of the Bcl2 family and acts to promote apoptosis by forming heterodimers with the survival proteins Bcl2 and BclxL, thus preventing them from binding with BAX. Bad is found on the outer mitochondrial membrane and, once phosphorylated in response to growth stimuli, translocates to the cytoplasm. The phosphorylation status of Bad represents a key checkpoint for death or cell survival. JNK-induced phosphorylation of BAD serine 128 promotes the apoptotic role of Bad by opposing the inhibitory effect of growth factor on Bad-mediated apoptosis. Cdc2-induced phosphorylation of Bad serine 128 has an inhibitory effect on its interaction with 14-3-3 proteins. The latter interaction is critical for Bad phosphorylation at serine 155, a site within the BH3 domain that leads to the release of BclxL and the promotion of cell survival. Alternative splicing of this gene results in two transcript variants which encode the same isoform.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-2592R-A488)

Dodavatel: Bioss

Popis: Serine/threonine-protein kinase involved in various processes such as neuronal proliferation, differentiation, migration and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK1/JNK3. In turn, MAPK1/JNK3 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. Plays regulatory roles in the signaling pathways during neuronal apoptosis. Phosphorylates the neuronal microtubule regulator STMN2. Acts in the regulation of the beta-amyloid precursor protein/APP signaling during neuronal differentiation by phosphorylating APP. Participates also in neurite growth in spiral ganglion neurons.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-12567R-CY5)

Dodavatel: Bioss

Popis: Bad is a member of the Bcl2 family and acts to promote apoptosis by forming heterodimers with the survival proteins Bcl2 and BclxL, thus preventing them from binding with BAX. Bad is found on the outer mitochondrial membrane and, once phosphorylated in response to growth stimuli, translocates to the cytoplasm. The phosphorylation status of Bad represents a key checkpoint for death or cell survival. JNK-induced phosphorylation of BAD serine 128 promotes the apoptotic role of Bad by opposing the inhibitory effect of growth factor on Bad-mediated apoptosis. Cdc2-induced phosphorylation of Bad serine 128 has an inhibitory effect on its interaction with 14-3-3 proteins. The latter interaction is critical for Bad phosphorylation at serine 155, a site within the BH3 domain that leads to the release of BclxL and the promotion of cell survival. Alternative splicing of this gene results in two transcript variants which encode the same isoform.This antibody recognise the phosphorylation site of human Ser75, mouse Ser111, rat Ser112.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (PRSI90-262)

Dodavatel: ProSci Inc.

Popis: BCMA is a receptor for BAFF and APRIL. It promotes B cell survival and plays a role in the regulation of humoral immunity. It's downstream signalling is dependent on NF-kappaB and JNK.

Měrná jednotka: 1 * 50 µG

Akce

Katalogové číslo: (BOSSBS-9241R-CY5.5)

Dodavatel: Bioss

Popis: E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-9241R-CY3)

Dodavatel: Bioss

Popis: E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-13741R-A680)

Dodavatel: Bioss

Popis: Vinexin is a 671 amino acid protein that is expressed as two isoforms, designated Vinexin alpha and Vinexin beta. Localized to cell junctions in both the cytoplasm and the cytoskeleton, Vinexin alpha functions to promote Actin stress fiber formation, playing an important role in modification of the Actin cytoskeleton. Like Vinexin alpha, Vinexin beta is localized to cell junctions in the cytoplasm, but is also found in the nucleus where it plays an important role in cell spreading and in activation of the JNK pathway in response to EGF stimulation. Although Vinexin alpha and Vinexin beta have different roles within the cell, both proteins contain three SH3 domains in their carboxy terminus and are expressed in a variety of tissues, including placenta, heart, liver, brain, pancreas and skeletal muscle. Together, Vinexin alpha and Vinexin beta are involved in cell-cell adhesion, signal transduction and cytoskeletal organization throughout the cell.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-13741R-A555)

Dodavatel: Bioss

Popis: Vinexin is a 671 amino acid protein that is expressed as two isoforms, designated Vinexin alpha and Vinexin beta. Localized to cell junctions in both the cytoplasm and the cytoskeleton, Vinexin alpha functions to promote Actin stress fiber formation, playing an important role in modification of the Actin cytoskeleton. Like Vinexin alpha, Vinexin beta is localized to cell junctions in the cytoplasm, but is also found in the nucleus where it plays an important role in cell spreading and in activation of the JNK pathway in response to EGF stimulation. Although Vinexin alpha and Vinexin beta have different roles within the cell, both proteins contain three SH3 domains in their carboxy terminus and are expressed in a variety of tissues, including placenta, heart, liver, brain, pancreas and skeletal muscle. Together, Vinexin alpha and Vinexin beta are involved in cell-cell adhesion, signal transduction and cytoskeletal organization throughout the cell.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-13741R-A350)

Dodavatel: Bioss

Popis: Vinexin is a 671 amino acid protein that is expressed as two isoforms, designated Vinexin alpha and Vinexin beta. Localized to cell junctions in both the cytoplasm and the cytoskeleton, Vinexin alpha functions to promote Actin stress fiber formation, playing an important role in modification of the Actin cytoskeleton. Like Vinexin alpha, Vinexin beta is localized to cell junctions in the cytoplasm, but is also found in the nucleus where it plays an important role in cell spreading and in activation of the JNK pathway in response to EGF stimulation. Although Vinexin alpha and Vinexin beta have different roles within the cell, both proteins contain three SH3 domains in their carboxy terminus and are expressed in a variety of tissues, including placenta, heart, liver, brain, pancreas and skeletal muscle. Together, Vinexin alpha and Vinexin beta are involved in cell-cell adhesion, signal transduction and cytoskeletal organization throughout the cell.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-5219R-A680)

Dodavatel: Bioss

Popis: Bad is a member of the Bcl2 family and acts to promote apoptosis by forming heterodimers with the survival proteins Bcl2 and BclxL, thus preventing them from binding with BAX. Bad is found on the outer mitochondrial membrane and, once phosphorylated in response to growth stimuli, translocates to the cytoplasm. The phosphorylation status of Bad represents a key checkpoint for death or cell survival. JNK-induced phosphorylation of BAD serine 128 promotes the apoptotic role of Bad by opposing the inhibitory effect of growth factor on Bad-mediated apoptosis. Cdc2-induced phosphorylation of Bad serine 128 has an inhibitory effect on its interaction with 14-3-3 proteins. The latter interaction is critical for Bad phosphorylation at serine 155, a site within the BH3 domain that leads to the release of BclxL and the promotion of cell survival. Alternative splicing of this gene results in two transcript variants which encode the same isoform.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-5217R-A680)

Dodavatel: Bioss

Popis: Bad is a member of the Bcl2 family and acts to promote apoptosis by forming heterodimers with the survival proteins Bcl2 and BclxL, thus preventing them from binding with BAX. Bad is found on the outer mitochondrial membrane and, once phosphorylated in response to growth stimuli, translocates to the cytoplasm. The phosphorylation status of Bad represents a key checkpoint for death or cell survival. JNK-induced phosphorylation of BAD serine 128 promotes the apoptotic role of Bad by opposing the inhibitory effect of growth factor on Bad-mediated apoptosis. Cdc2-induced phosphorylation of Bad serine 128 has an inhibitory effect on its interaction with 14-3-3 proteins. The latter interaction is critical for Bad phosphorylation at serine 155, a site within the BH3 domain that leads to the release of BclxL and the promotion of cell survival. Alternative splicing of this gene results in two transcript variants which encode the same isoform.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-5217R-A750)

Dodavatel: Bioss

Popis: Bad is a member of the Bcl2 family and acts to promote apoptosis by forming heterodimers with the survival proteins Bcl2 and BclxL, thus preventing them from binding with BAX. Bad is found on the outer mitochondrial membrane and, once phosphorylated in response to growth stimuli, translocates to the cytoplasm. The phosphorylation status of Bad represents a key checkpoint for death or cell survival. JNK-induced phosphorylation of BAD serine 128 promotes the apoptotic role of Bad by opposing the inhibitory effect of growth factor on Bad-mediated apoptosis. Cdc2-induced phosphorylation of Bad serine 128 has an inhibitory effect on its interaction with 14-3-3 proteins. The latter interaction is critical for Bad phosphorylation at serine 155, a site within the BH3 domain that leads to the release of BclxL and the promotion of cell survival. Alternative splicing of this gene results in two transcript variants which encode the same isoform.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-5436R-A750)

Dodavatel: Bioss

Popis: Mitogen-activated protein kinase (MAPK) signaling cascades include MAPK or extracellular signal-regulated kinase (ERK), MAPK kinase (MKK or MEK), and MAPK kinase kinase (MAPKKK or MEKK). MAPKK kinase/MEKK phosphorylates and activates its downstream protein kinase, MAPK kinase/MEK, which in turn activates MAPK. The kinases of these signaling cascades are highly conserved, and homologs exist in yeast, Drosophila, and mammalian cells. MAPKKK5 contains 1,374 amino acids with all 11 kinase subdomains. Northern blot analysis shows that MAPKKK5 transcript is abundantly expressed in human heart and pancreas. The MAPKKK5 protein phosphorylates and activates MKK4 (aliases SERK1, MAPKK4) in vitro, and activates c-Jun N-terminal kinase (JNK)/stress-activated protein kinase (SAPK) during transient expression in COS and 293 cells; MAPKKK5 does not activate MAPK/ERK.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-6246R-CY3)

Dodavatel: Bioss

Popis: The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene maps in a region that contains the BRCA1 locus which confers susceptibility to breast and ovarian cancer. Although DUSP3 is expressed in both breast and ovarian tissues, mutation screening in breast cancer pedigrees and in sporadic tumors was negative, leading to the conclusion that this gene is not BRCA1.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-9241R-A647)

Dodavatel: Bioss

Popis: E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types.

Měrná jednotka: 1 * 100 µl

Akce