Esta buscando: N-tert-Butylnicotinamide

Numero del catalogo: (BOSSBS-11271R-CY3)

Proveedor: Bioss

Descripción: Hip (HSP70-interacting protein), also known as ST13 (suppression of tumorigenicity protein 13), is one of several co-chaperones that regulate activities of the HSP70 chaperone family (1,2). The homo-oligomeric protein Hip cooperates with HSP70 in protein folding by stabilizing the ADP-bound state of HSP70. Hip directly binds to the ATPase domain of HSP70 when it is converted to the ADP-bound state by proteins of the HSP40 family (3). By collaborating with other positive co-factors such as HSP40 and Hop, or competing with negative co-factors such as Bag1, Hip may facilitate the chaperone function of HSP70 in protein folding and repair, and in controlling the activity of regulatory proteins such as steroid receptors and various regulators of proliferation or apoptosis (4-8).

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11271R-A680)

Proveedor: Bioss

Descripción: Hip (HSP70-interacting protein), also known as ST13 (suppression of tumourigenicity protein 13), is one of several co-chaperones that regulate activities of the HSP70 chaperone family. The homo-oligomeric protein Hip cooperates with HSP70 in protein folding by stabilizing the ADP-bound state of HSP70. Hip directly binds to the ATPase domain of HSP70 when it is converted to the ADP-bound state by proteins of the HSP40 family. By collaborating with other positive co-factors such as HSP40 and Hop, or competing with negative co-factors such as Bag1, Hip may facilitate the chaperone function of HSP70 in protein folding and repair, and in controlling the activity of regulatory proteins such as steroid receptors and various regulators of proliferation or apoptosis.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11271R-A350)

Proveedor: Bioss

Descripción: Hip (HSP70-interacting protein), also known as ST13 (suppression of tumorigenicity protein 13), is one of several co-chaperones that regulate activities of the HSP70 chaperone family (1,2). The homo-oligomeric protein Hip cooperates with HSP70 in protein folding by stabilizing the ADP-bound state of HSP70. Hip directly binds to the ATPase domain of HSP70 when it is converted to the ADP-bound state by proteins of the HSP40 family (3). By collaborating with other positive co-factors such as HSP40 and Hop, or competing with negative co-factors such as Bag1, Hip may facilitate the chaperone function of HSP70 in protein folding and repair, and in controlling the activity of regulatory proteins such as steroid receptors and various regulators of proliferation or apoptosis (4-8).

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11271R-A647)

Proveedor: Bioss

Descripción: Hip (HSP70-interacting protein), also known as ST13 (suppression of tumorigenicity protein 13), is one of several co-chaperones that regulate activities of the HSP70 chaperone family (1,2). The homo-oligomeric protein Hip cooperates with HSP70 in protein folding by stabilizing the ADP-bound state of HSP70. Hip directly binds to the ATPase domain of HSP70 when it is converted to the ADP-bound state by proteins of the HSP40 family (3). By collaborating with other positive co-factors such as HSP40 and Hop, or competing with negative co-factors such as Bag1, Hip may facilitate the chaperone function of HSP70 in protein folding and repair, and in controlling the activity of regulatory proteins such as steroid receptors and various regulators of proliferation or apoptosis (4-8).

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11271R-A488)

Proveedor: Bioss

Descripción: Hip (HSP70-interacting protein), also known as ST13 (suppression of tumorigenicity protein 13), is one of several co-chaperones that regulate activities of the HSP70 chaperone family (1,2). The homo-oligomeric protein Hip cooperates with HSP70 in protein folding by stabilizing the ADP-bound state of HSP70. Hip directly binds to the ATPase domain of HSP70 when it is converted to the ADP-bound state by proteins of the HSP40 family (3). By collaborating with other positive co-factors such as HSP40 and Hop, or competing with negative co-factors such as Bag1, Hip may facilitate the chaperone function of HSP70 in protein folding and repair, and in controlling the activity of regulatory proteins such as steroid receptors and various regulators of proliferation or apoptosis (4-8).

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11697R-CY3)

Proveedor: Bioss

Descripción: Programmed neuronal cell death is a feature of neurodegenerative disorders such as Alzheimer's and Huntington's disease, which occur later in human life. Huntington’s disease at the molecular and cell level is characterized by polyglutamine expansion of the protein huntingtin (Htt) that leads to apoptotis-mediated neurodegenerative loss of medium spiny neurons throughout the striatum. Polyglutamine expansion reduces the level of association between Hip-1 and Htt, thereby increasing levels of free Hip-1 that then can be the candidate protein Hippi (Hip-1 protein interactor). The Hippi-Hip-1 heterodimer is a pro-apoptotic complex that recruits procaspase-8 and initiates caspase-8 activation, which may contribute to the neuronal cell death observed in individuals diagnosed with Huntington’s disease. The human hippi gene maps to chromosome 3q13.13 and encodes a 429 amino acid protein.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11271R-CY7)

Proveedor: Bioss

Descripción: Hip (HSP70-interacting protein), also known as ST13 (suppression of tumorigenicity protein 13), is one of several co-chaperones that regulate activities of the HSP70 chaperone family (1,2). The homo-oligomeric protein Hip cooperates with HSP70 in protein folding by stabilizing the ADP-bound state of HSP70. Hip directly binds to the ATPase domain of HSP70 when it is converted to the ADP-bound state by proteins of the HSP40 family (3). By collaborating with other positive co-factors such as HSP40 and Hop, or competing with negative co-factors such as Bag1, Hip may facilitate the chaperone function of HSP70 in protein folding and repair, and in controlling the activity of regulatory proteins such as steroid receptors and various regulators of proliferation or apoptosis (4-8).

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (ABCAAB76005-100)

Proveedor: Abcam

Descripción: Anti-HSC70 Interacting Protein HIP Rabbit Monoclonal Antibody [clone: EP3264]

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11271R-HRP)

Proveedor: Bioss

Descripción: Hip (HSP70-interacting protein), also known as ST13 (suppression of tumorigenicity protein 13), is one of several co-chaperones that regulate activities of the HSP70 chaperone family (1,2). The homo-oligomeric protein Hip cooperates with HSP70 in protein folding by stabilizing the ADP-bound state of HSP70. Hip directly binds to the ATPase domain of HSP70 when it is converted to the ADP-bound state by proteins of the HSP40 family (3). By collaborating with other positive co-factors such as HSP40 and Hop, or competing with negative co-factors such as Bag1, Hip may facilitate the chaperone function of HSP70 in protein folding and repair, and in controlling the activity of regulatory proteins such as steroid receptors and various regulators of proliferation or apoptosis (4-8).

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11697R-CY5)

Proveedor: Bioss

Descripción: Programmed neuronal cell death is a feature of neurodegenerative disorders such as Alzheimer's and Huntington's disease, which occur later in human life. Huntington’s disease at the molecular and cell level is characterized by polyglutamine expansion of the protein huntingtin (Htt) that leads to apoptotis-mediated neurodegenerative loss of medium spiny neurons throughout the striatum. Polyglutamine expansion reduces the level of association between Hip-1 and Htt, thereby increasing levels of free Hip-1 that then can be the candidate protein Hippi (Hip-1 protein interactor). The Hippi-Hip-1 heterodimer is a pro-apoptotic complex that recruits procaspase-8 and initiates caspase-8 activation, which may contribute to the neuronal cell death observed in individuals diagnosed with Huntington’s disease. The human hippi gene maps to chromosome 3q13.13 and encodes a 429 amino acid protein.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11271R-CY5)

Proveedor: Bioss

Descripción: Hip (HSP70-interacting protein), also known as ST13 (suppression of tumorigenicity protein 13), is one of several co-chaperones that regulate activities of the HSP70 chaperone family (1,2). The homo-oligomeric protein Hip cooperates with HSP70 in protein folding by stabilizing the ADP-bound state of HSP70. Hip directly binds to the ATPase domain of HSP70 when it is converted to the ADP-bound state by proteins of the HSP40 family (3). By collaborating with other positive co-factors such as HSP40 and Hop, or competing with negative co-factors such as Bag1, Hip may facilitate the chaperone function of HSP70 in protein folding and repair, and in controlling the activity of regulatory proteins such as steroid receptors and various regulators of proliferation or apoptosis (4-8).

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11271R-A750)

Proveedor: Bioss

Descripción: Hip (HSP70-interacting protein), also known as ST13 (suppression of tumourigenicity protein 13), is one of several co-chaperones that regulate activities of the HSP70 chaperone family. The homo-oligomeric protein Hip cooperates with HSP70 in protein folding by stabilizing the ADP-bound state of HSP70. Hip directly binds to the ATPase domain of HSP70 when it is converted to the ADP-bound state by proteins of the HSP40 family. By collaborating with other positive co-factors such as HSP40 and Hop, or competing with negative co-factors such as Bag1, Hip may facilitate the chaperone function of HSP70 in protein folding and repair, and in controlling the activity of regulatory proteins such as steroid receptors and various regulators of proliferation or apoptosis.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11271R-A555)

Proveedor: Bioss

Descripción: Hip (HSP70-interacting protein), also known as ST13 (suppression of tumorigenicity protein 13), is one of several co-chaperones that regulate activities of the HSP70 chaperone family (1,2). The homo-oligomeric protein Hip cooperates with HSP70 in protein folding by stabilizing the ADP-bound state of HSP70. Hip directly binds to the ATPase domain of HSP70 when it is converted to the ADP-bound state by proteins of the HSP40 family (3). By collaborating with other positive co-factors such as HSP40 and Hop, or competing with negative co-factors such as Bag1, Hip may facilitate the chaperone function of HSP70 in protein folding and repair, and in controlling the activity of regulatory proteins such as steroid receptors and various regulators of proliferation or apoptosis (4-8).

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11697R)

Proveedor: Bioss

Descripción: Programmed neuronal cell death is a feature of neurodegenerative disorders such as Alzheimer's and Huntington's disease, which occur later in human life. Huntington’s disease at the molecular and cell level is characterized by polyglutamine expansion of the protein huntingtin (Htt) that leads to apoptotis-mediated neurodegenerative loss of medium spiny neurons throughout the striatum. Polyglutamine expansion reduces the level of association between Hip-1 and Htt, thereby increasing levels of free Hip-1 that then can be the candidate protein Hippi (Hip-1 protein interactor). The Hippi-Hip-1 heterodimer is a pro-apoptotic complex that recruits procaspase-8 and initiates caspase-8 activation, which may contribute to the neuronal cell death observed in individuals diagnosed with Huntington’s disease. The human hippi gene maps to chromosome 3q13.13 and encodes a 429 amino acid protein.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11271R-FITC)

Proveedor: Bioss

Descripción: Hip (HSP70-interacting protein), also known as ST13 (suppression of tumorigenicity protein 13), is one of several co-chaperones that regulate activities of the HSP70 chaperone family (1,2). The homo-oligomeric protein Hip cooperates with HSP70 in protein folding by stabilizing the ADP-bound state of HSP70. Hip directly binds to the ATPase domain of HSP70 when it is converted to the ADP-bound state by proteins of the HSP40 family (3). By collaborating with other positive co-factors such as HSP40 and Hop, or competing with negative co-factors such as Bag1, Hip may facilitate the chaperone function of HSP70 in protein folding and repair, and in controlling the activity of regulatory proteins such as steroid receptors and various regulators of proliferation or apoptosis (4-8).

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-11697R-CY7)

Proveedor: Bioss

Descripción: Programmed neuronal cell death is a feature of neurodegenerative disorders such as Alzheimer's and Huntington's disease, which occur later in human life. Huntington’s disease at the molecular and cell level is characterized by polyglutamine expansion of the protein huntingtin (Htt) that leads to apoptotis-mediated neurodegenerative loss of medium spiny neurons throughout the striatum. Polyglutamine expansion reduces the level of association between Hip-1 and Htt, thereby increasing levels of free Hip-1 that then can be the candidate protein Hippi (Hip-1 protein interactor). The Hippi-Hip-1 heterodimer is a pro-apoptotic complex that recruits procaspase-8 and initiates caspase-8 activation, which may contribute to the neuronal cell death observed in individuals diagnosed with Huntington’s disease. The human hippi gene maps to chromosome 3q13.13 and encodes a 429 amino acid protein.

UOM: 1 * 100 µl

Promoción