You Searched For: N-Boc-L-serine

Catalog Number: (BOSSBS-3048R)

Supplier: Bioss

Description: Beta Arrestin 1 is a member of a family of proteins that are widely expressed but especially abundant in the central nervous system. Serving as an adaptor or scaffold molecule, beta Arrestin 1 is essential for mitogenic signaling. It mediates agonist dependent desensitization and internalization of G protein coupled receptors (GPCRs, e.g., beta 2 adrenergic receptor). After binding to their ligand and interacting with heterotrimeric G proteins, GPCRs are phosphorylated by G protein receptor kinases (GRKs) on serine residues. Beta Arrestin 1 has important roles in the cytoplasm and at the plasma membrane in the desensitization and internalization of G protein coupled receptors (GPCRs) and is increasingly appreciated to play an important role in the endocytosis and signaling of GPCRs. Beta Arrestin 1 in the cytosol is phosphorylated by ERK1 and 2 on serine 412 in a negative feedback mechanism and binds to the phosphorylated receptors at the plasma membrane. Serine 412 is then dephosphorylated and the GPCRs are internalized, leading to activation of the Ras, Raf, ERK1 and 2 signaling pathway.

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-3316R)

Supplier: Bioss

Description: In mammals, there are several identified isoforms of p21 Activated Protein Kinases or PAKs: PAK1 and PAK3 are mostly brain specific, while PAK2 is expressed ubiquitously. Mutations of the gene coding for PAK3 are associated with X linked mental retardation and PAK3 is a key regulator of synapse formation and plasticity in the hippocampus. PAK3 is thought to play a key role in regulation of cell shape and motility as well as cell death. P21-activated kinase (PAK) is actually a family of serine/threonine protein kinases, members of which are activated by small molecular weight GTPases. The three most common isoforms are PAK 1, PAK 2, and PAK 3 (also known as alpha PAK, gamma PAK, and beta PAK, respectively). These kinases contain numerous regulatory elements that trigger diverse signaling processes such as those initiated by activated GTPases, interaction with Src homology 3 (SH3) domains, and caspase mediated proteolytic cleavage. Autophosphorylation of serine 141 (serine 144 for PAK 1 and serine 139 PAK 3), catalyzed by Cdc42, is required for activation of PAK.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3315R)

Supplier: Bioss

Description: In mammals, there are several identified isoforms of p21 Activated Protein Kinases or PAKs: PAK1 and PAK3 are mostly brain specific, while PAK2 is expressed ubiquitously. Mutations of the gene coding for PAK3 are associated with X linked mental retardation and PAK3 is a key regulator of synapse formation and plasticity in the hippocampus. PAK3 is thought to play a key role in regulation of cell shape and motility as well as cell death. P21-activated kinase (PAK) is actually a family of serine/threonine protein kinases, members of which are activated by small molecular weight GTPases. The three most common isoforms are PAK 1, PAK 2, and PAK 3 (also known as alpha PAK, gamma PAK, and beta PAK, respectively). These kinases contain numerous regulatory elements that trigger diverse signaling processes such as those initiated by activated GTPases, interaction with Src homology 3 (SH3) domains, and caspase mediated proteolytic cleavage. Autophosphorylation of serine 141 (serine 144 for PAK 1 and serine 139 PAK 3), catalyzed by Cdc42, is required for activation of PAK.

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: (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-3785R-CY5.5)

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)

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-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-2270R-A647)

Supplier: Bioss

Description: p21-activated kinases (PAKs) belong to the family of serine/threonine kinases involved in the control of various cellular processes, including the cell cycle, dynamics of the cytoskeleton, apoptosis, oncogenic transformation, and transcription. All PAK family members are characterized by the presence of p21-binding domain. p21-activated kinases are regulated by the small GTP-binding proteins Rac and Cdc42, and lipids, which stimulate autophosphorylation and phosphorylation of exogenous substrates. Serine (Ser-474) is the likely autophosphorylation site in the kinase domain of PAK4 in vivo. Phosphospecific directed against serine 474 detect activated PAK4 on the Golgi membrane when PAK4 is co-expressed with activated Cdc42. Current data strongly implicates PAK-4 in oncogenesis. PAK4 is frequently overexpressed in human tumor cell lines of various tissue origins. Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates the proto-oncogene RAF1 and stimulates its kinase activity. Promotes cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Phosphorylates CTNND1, probably to regulate cytoskeletal organization and cell morphology. Keeps microtubules stable through MARK2 inhibition and destabilizes the F-actin network leading to the disappearance of stress fibers and focal adhesions.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-2270R-A488)

Supplier: Bioss

Description: p21-activated kinases (PAKs) belong to the family of serine/threonine kinases involved in the control of various cellular processes, including the cell cycle, dynamics of the cytoskeleton, apoptosis, oncogenic transformation, and transcription. All PAK family members are characterized by the presence of p21-binding domain. p21-activated kinases are regulated by the small GTP-binding proteins Rac and Cdc42, and lipids, which stimulate autophosphorylation and phosphorylation of exogenous substrates. Serine (Ser-474) is the likely autophosphorylation site in the kinase domain of PAK4 in vivo. Phosphospecific directed against serine 474 detect activated PAK4 on the Golgi membrane when PAK4 is co-expressed with activated Cdc42. Current data strongly implicates PAK-4 in oncogenesis. PAK4 is frequently overexpressed in human tumor cell lines of various tissue origins. Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates the proto-oncogene RAF1 and stimulates its kinase activity. Promotes cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Phosphorylates CTNND1, probably to regulate cytoskeletal organization and cell morphology. Keeps microtubules stable through MARK2 inhibition and destabilizes the F-actin network leading to the disappearance of stress fibers and focal adhesions.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-2270R-HRP)

Supplier: Bioss

Description: p21-activated kinases (PAKs) belong to the family of serine/threonine kinases involved in the control of various cellular processes, including the cell cycle, dynamics of the cytoskeleton, apoptosis, oncogenic transformation, and transcription. All PAK family members are characterized by the presence of p21-binding domain. p21-activated kinases are regulated by the small GTP-binding proteins Rac and Cdc42, and lipids, which stimulate autophosphorylation and phosphorylation of exogenous substrates. Serine (Ser-474) is the likely autophosphorylation site in the kinase domain of PAK4 in vivo. Phosphospecific directed against serine 474 detect activated PAK4 on the Golgi membrane when PAK4 is co-expressed with activated Cdc42. Current data strongly implicates PAK-4 in oncogenesis. PAK4 is frequently overexpressed in human tumor cell lines of various tissue origins. Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates the proto-oncogene RAF1 and stimulates its kinase activity. Promotes cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Phosphorylates CTNND1, probably to regulate cytoskeletal organization and cell morphology. Keeps microtubules stable through MARK2 inhibition and destabilizes the F-actin network leading to the disappearance of stress fibers and focal adhesions.

UOM: 1 * 100 µl