You Searched For: N-Boc-L-serine

Catalog Number: (BWRLBS4027)

Supplier: Bioworld Technology

Description: Synthetic phosphopeptide derived from human BRCA1 around the phosphorylation site of Serine 1524.

UOM: 1 * 100 µG

Catalog Number: (BWRLBS4795)

Supplier: Bioworld Technology

Description: Synthetic phosphopeptide derived from human HSF1 around the phosphorylation site of Serine 303.

UOM: 1 * 100 µG

Catalog Number: (BWRLBS4879)

Supplier: Bioworld Technology

Description: Synthetic phosphopeptide derived from human Synapsin I around the phosphorylation site of Serine 62.

UOM: 1 * 100 µG

Catalog Number: (BWRLBS4673)

Supplier: Bioworld Technology

Description: Synthetic phosphopeptide derived from human Csk around the phosphorylation site of Serine 364.

UOM: 1 * 100 µG

Catalog Number: (BWRLBS5027)

Supplier: Bioworld Technology

Description: Synthetic phosphopeptide derived from human p53 around the phosphorylation site of Serine 20.

UOM: 1 * 100 µG

Catalog Number: (BWRLBS4839)

Supplier: Bioworld Technology

Description: Synthetic phosphopeptide derived from human c-Rel around the phosphorylation site of Serine 503.

UOM: 1 * 100 µG

Catalog Number: (BWRLBS4147)

Supplier: Bioworld Technology

Description: Synthetic phosphopeptide derived from human p53 around the phosphorylation site of Serine 46.

UOM: 1 * 100 µG

Catalog Number: (BWRLBS4146)

Supplier: Bioworld Technology

Description: Synthetic phosphopeptide derived from human p53 around the phosphorylation site of Serine 33.

UOM: 1 * 100 µG

Catalog Number: (BOSSBS-5217R-FITC)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-5219R-A647)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3009R-A750)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-5219R-FITC)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-5217R-A555)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9734R-CY5)

Supplier: Bioss

Description: The phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions in eukaryotes, including cell division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the serine/threonine (Ser/Thr) protein kinases. TSSK 6 (testis-specific serine kinase 6), also known as SSTK, TSSK4, FKSG82 or CT72, is a 273 amino acid protein that contains one protein kinase domain and belongs to the Ser/Thr protein kinase family. Highly expressed in testis with lower expression in ovary, colon, thymus, small intestine and spleen, TSSK 6 catalyzes the ATP-dependent phosphorylation of proteins involved in sperm production and chromatin remodeling. TSSK 6 uses magnesium as a cofactor and is thought to be required for proper sperm development and function, as well as DNA condensation events. Defects in the gene encoding TSSK 6 are associated with male infertility characterized by low sperm count and decreased sperm motility.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-5216R-CY5.5)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-5216R-A750)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl