You Searched For: N-Boc-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

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Catalog Number: (BWRLBS4864)

Supplier: Bioworld Technology

Description: Synthetic phosphopeptide derived from human PLC beta3 around the phosphorylation site of Serine 537.

UOM: 1 * 100 µG

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Supplier: Apollo Scientific

Description: (S)-Trityl-2-amino-3-hydroxypropionic acid triethyl ammonium salt

Catalog Number: (BOSSBS-15535R)

Supplier: Bioss

Description: Eukaryotic protein kinases are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. This gene encodes an intestinal serine/threonine kinase harboring a dual phosphorylation site found in mitogen-activating protein (MAP) kinases. The protein localizes to the intestinal crypt region and is thought to be important in intestinal epithelial cell proliferation and differentiation. Alternative splicing has been observed at this locus and two variants, encoding the same isoform, have been identified.

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Catalog Number: (BOSSBS-15536R-A680)

Supplier: Bioss

Description: Eukaryotic protein kinases are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. This gene encodes an intestinal serine/threonine kinase harboring a dual phosphorylation site found in mitogen-activating protein (MAP) kinases. The protein localises to the intestinal crypt region and is thought to be important in intestinal epithelial cell proliferation and differentiation. Alternative splicing has been observed at this locus and two variants, encoding the same isoform, have been identified.

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Catalog Number: (BOSSBS-15536R-A555)

Supplier: Bioss

Description: Eukaryotic protein kinases are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. This gene encodes an intestinal serine/threonine kinase harboring a dual phosphorylation site found in mitogen-activating protein (MAP) kinases. The protein localises to the intestinal crypt region and is thought to be important in intestinal epithelial cell proliferation and differentiation. Alternative splicing has been observed at this locus and two variants, encoding the same isoform, have been identified.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-7918R-CY7)

Supplier: Bioss

Description: PLK5 (Serine/threonine-protein kinase PLK5) belongs to the protein kinase superfamily and Ser/Thr protein kinase family and CDC5/Polo subfamily. PLK5P contains 1 POLO box domain and 1 Serine/Threonine protein kinase catalytic domain.

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Catalog Number: (BOSSBS-7918R-A680)

Supplier: Bioss

Description: PLK5 (Serine/threonine-protein kinase PLK5) belongs to the protein kinase superfamily and Ser/Thr protein kinase family and CDC5/Polo subfamily. PLK5P contains 1 POLO box domain and 1 Serine/Threonine protein kinase catalytic domain.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-3009R-HRP)

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

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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

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Supplier: ENZO LIFE SCIENCES

Description: Glycogen Synthase Kinase 3β (GSK-3β) is a unique serine/threonine kinase that is inactivated by phosphorylation. In response to insulin binding, PKB/AKT phosphorylates GSK-3β on serine 9, which prevents GSK-3β from phosphorylating glycogen synthase. Unphosphorylated glycogen synthase is active and able to synthesize glycogen. GSK-3β is also unique in that it requires a substrate that has been phosphorylated by a distinct kinase before it can phosphorylate the substrate. This phosphate priming mechanism explains why phosphorylation of serine 9 inactivates GSK-3β. The phosphorylated serine binds to the GSK-3β priming phosphate position and prevents binding of alternative substrates. In addition to insulin signaling, GSK-3β participates in the Wnt signaling pathway, where it forms a complex with axin, beta-catenin and adenomatous polyposis coli (APC) protein. In the presence of Wnts, GSK-3β is unable to phosphorylate beta-catenin, which leads to stabilization of beta-catenin. The Wnt pathway inactivates GSK-3β via the proteins, Dishevelled and FRAT, which disrupt the interaction of GSK-3β with axin, beta-catenin, and APC. Clinically, there is considerable interest in GSK-3β inhibitors because they may mimic the effect of insulin or reduce the hyperphosphorylation of Tau that is observed in Alzheimer's Disease.

New Product

Catalog Number: (BOSSBS-5777R-CY5)

Supplier: Bioss

Description: Serine/threonine protein kinase which forms a receptor complex on ligand binding. The receptor complex consisting of 2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators, SMAD2 and SMAD3. Receptor for activin AB, activin B and NODAL. Plays a role in cell differentiation, growth arrest and apoptosis.

UOM: 1 * 100 µl

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Catalog Number: (BWRLBS4854)

Supplier: Bioworld Technology

Description: Synthetic phosphopeptide derived from human PAK4 around the phosphorylation site of Serine 474.

UOM: 1 * 100 µG

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Catalog Number: (BOSSBS-6281R-CY5)

Supplier: Bioss

Description: This gene encodes a type II transmembrane serine protease. The encoded protein has an extracellular region that consists of two domains, a catalytic serine protease domain and a non-catalytic scavenger receptor cysteine-rich domain. This protein may be involved in diverse cellular functions including blood coagulation, maintenance of cell morphology and the growth and progression of certain cancers, particularly prostate cancer. Alternative splicing results in multiple transcript variants.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11993R)

Supplier: Bioss

Description: Changes in the serine/threonine phosphorylation state of a protein in response to various external stimuli can have profound effects on cellular signal transduction, apoptosis and carcinogenesis. The reagents, including phosphorylated protein/peptides, antibodies against the phosphospecific amino acid, are important tools to explore the activation of serine, threonine or tyrosine containing proteins. An aberrant protein phosphorylation is a hallmark of human disease, and the enzymes, particularly protein kinases, which control protein phosphorylation are recognized as a major new drug target family.

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Supplier: Apollo Scientific

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