You Searched For: N-Oleoyl-L-Serine

Catalog Number: (BOSSBS-6728R-A680)

Supplier: Bioss

Description: Ca2+/calmodulin dependent protein kinase type IV (CAMKIV) belongs to the serine/threonine protein kinase family, and to the Ca(2+)/calmodulin-dependent protein kinase subfamily. This enzyme is a multifunctional serine/threonine protein kinase with limited tissue distribution, that has been implicated in transcriptional regulation in lymphocytes, neurons and male germ cells.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-6728R-FITC)

Supplier: Bioss

Description: Ca2+/calmodulin dependent protein kinase type IV (CAMKIV) belongs to the serine/threonine protein kinase family, and to the Ca(2+)/calmodulin-dependent protein kinase subfamily. This enzyme is a multifunctional serine/threonine protein kinase with limited tissue distribution, that has been implicated in transcriptional regulation in lymphocytes, neurons and male germ cells.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-6728R-A647)

Supplier: Bioss

Description: Ca2+/calmodulin dependent protein kinase type IV (CAMKIV) belongs to the serine/threonine protein kinase family, and to the Ca(2+)/calmodulin-dependent protein kinase subfamily. This enzyme is a multifunctional serine/threonine protein kinase with limited tissue distribution, that has been implicated in transcriptional regulation in lymphocytes, neurons and male germ cells.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3524R-A350)

Supplier: Bioss

Description: PED/PEA 15 (Phosphoprotein Enriched in Diabetes/Phosphoprotein Enriched in Astrocytes 15 kDa) is a widely expressed 15 kDa protein comprised of an N terminal region containing a canonical Death Effector Domain (DED) sequence and a nuclear export signal, and a C terminal region containing two serine phosphorylation sites. PED/PEA 15 has been implicated in the regulation of multiple cellular processes including apoptosis, integrin activation, and insulin sensitive glucose transport in insulin responsive cells. Phosphorylation of both serine 104 (a Protein Kinase C site) and serine 116 (a substrate of CaMKII and Akt) is required for PED/PEA 15 function.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3785R-A555)

Supplier: Bioss

Description: Apoptosis is mediated by death domain containing adapter molecules and a caspase family of proteases. Certain serine/threonine protein kinases, such as ASK1 and RIP, are mediators of apoptosis. Two novel serine/threonine kinases that induce apoptosis were recently identified and designated DRAK1 and DRAK2 (for DAP kinase related apoptosis inducing protein kinases). DRAKs contain an N terminal kinase domain and a C terminal regulation domain. Overexpression of DRAK2 induces apoptosis. DRAKs have high sequence homology to DAP and ZIP kinases, and they represent a novel family of serine/threonine kinases, which mediates apoptosis through their catalytic activities. DRAK2 is located in nucleus and the messenger RNA was ubiquitously expressed in human tissues.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3785R-A488)

Supplier: Bioss

Description: Apoptosis is mediated by death domain containing adapter molecules and a caspase family of proteases. Certain serine/threonine protein kinases, such as ASK1 and RIP, are mediators of apoptosis. Two novel serine/threonine kinases that induce apoptosis were recently identified and designated DRAK1 and DRAK2 (for DAP kinase related apoptosis inducing protein kinases). DRAKs contain an N terminal kinase domain and a C terminal regulation domain. Overexpression of DRAK2 induces apoptosis. DRAKs have high sequence homology to DAP and ZIP kinases, and they represent a novel family of serine/threonine kinases, which mediates apoptosis through their catalytic activities. DRAK2 is located in nucleus and the messenger RNA was ubiquitously expressed in human tissues.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3785R-HRP)

Supplier: Bioss

Description: Apoptosis is mediated by death domain containing adapter molecules and a caspase family of proteases. Certain serine/threonine protein kinases, such as ASK1 and RIP, are mediators of apoptosis. Two novel serine/threonine kinases that induce apoptosis were recently identified and designated DRAK1 and DRAK2 (for DAP kinase related apoptosis inducing protein kinases). DRAKs contain an N terminal kinase domain and a C terminal regulation domain. Overexpression of DRAK2 induces apoptosis. DRAKs have high sequence homology to DAP and ZIP kinases, and they represent a novel family of serine/threonine kinases, which mediates apoptosis through their catalytic activities. DRAK2 is located in nucleus and the messenger RNA was ubiquitously expressed in human tissues.

UOM: 1 * 100 µl

Catalog Number: (BWRLBS4802)

Supplier: Bioworld Technology

Description: Synthetic phosphopeptide derived from human Synapsin I around the phosphorylation site of Serine 9.

UOM: 1 * 100 µG

Catalog Number: (BWRLBS4149)

Supplier: Bioworld Technology

Description: Synthetic phosphopeptide derived from human p53 around the phosphorylation site of Serine 9.

UOM: 1 * 100 µG

Catalog Number: (BOSSBS-9010R-A750)

Supplier: Bioss

Description: DPP6 is a Type-II serine proteinase of the clan SC. The clan SC proteinases have a catalytic triad of Ser-Asp-His, and like other Serine proteinases, the active site serine is in a Gly-Xaa-Ser-Xaa -Gly orientation. DPP6 has an Asp instead of Ser in the catalytic site. DPP6 is a member of a broader family of dipeptidyl peptidases including DPP4, FAP/Seprase, DPP2, DPP8, DPP9, DPP10, which have differing substrate specificity and tissue localisations. The surface-bound DPP6 is a homodimer, and cleavage of in the stalk region releases a shed form of DPP6. The shed is the form found in serum. DPP6 has been found in highest abundance in the brain, but also in the kidney, liver and lung.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9010R-A350)

Supplier: Bioss

Description: DPP6 is a Type-II serine proteinase of the clan SC. The clan SC proteinases have a catalytic triad of Ser-Asp-His, and like other Serine proteinases, the active site serine is in a Gly-Xaa-Ser-Xaa -Gly orientation. DPP6 has an Asp instead of Ser in the catalytic site. DPP6 is a member of a broader family of dipeptidyl peptidases including DPP4, FAP/Seprase, DPP2, DPP8, DPP9, DPP10, which have differing substrate specificity and tissue localizations. The surface-bound DPP6 is a homodimer, and cleavage of in the stalk region releases a shed form of DPP6. The shed is the form found in serum. DPP6 has been found in highest abundance in the brain, but also in the kidney, liver and lung.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9010R-A680)

Supplier: Bioss

Description: DPP6 is a Type-II serine proteinase of the clan SC. The clan SC proteinases have a catalytic triad of Ser-Asp-His, and like other Serine proteinases, the active site serine is in a Gly-Xaa-Ser-Xaa -Gly orientation. DPP6 has an Asp instead of Ser in the catalytic site. DPP6 is a member of a broader family of dipeptidyl peptidases including DPP4, FAP/Seprase, DPP2, DPP8, DPP9, DPP10, which have differing substrate specificity and tissue localisations. The surface-bound DPP6 is a homodimer, and cleavage of in the stalk region releases a shed form of DPP6. The shed is the form found in serum. DPP6 has been found in highest abundance in the brain, but also in the kidney, liver and lung.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-5219R)

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-9010R-CY5)

Supplier: Bioss

Description: DPP6 is a Type-II serine proteinase of the clan SC. The clan SC proteinases have a catalytic triad of Ser-Asp-His, and like other Serine proteinases, the active site serine is in a Gly-Xaa-Ser-Xaa -Gly orientation. DPP6 has an Asp instead of Ser in the catalytic site. DPP6 is a member of a broader family of dipeptidyl peptidases including DPP4, FAP/Seprase, DPP2, DPP8, DPP9, DPP10, which have differing substrate specificity and tissue localizations. The surface-bound DPP6 is a homodimer, and cleavage of in the stalk region releases a shed form of DPP6. The shed is the form found in serum. DPP6 has been found in highest abundance in the brain, but also in the kidney, liver and lung.

UOM: 1 * 100 µl

Supplier: APOLLO SCIENTIFIC

Description: A predominant, rather hydrophobic natural ceramide. Activates a cytosolic serine/threonine protein phosphate & stimulates ceramide-activated protein kinase.

Catalog Number: (BWRLAP0149)

Supplier: Bioworld Technology

Description: Synthetic phosphopeptide derived from human GFAP around the phosphorylation site of Serine 38.

UOM: 1 * 100 µG