You Searched For: N-Boc-L-serine

Catalog Number: (BOSSBS-0500R-A350)

Supplier: Bioss

Description: Probable serine protease inhibitor.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-7536R)

Supplier: Bioss

Description: May modulates insulin action conceivably only in the presence of its yet undefined target proteases in white adipose tissues.Serpins are the largest and most diverse family of protease inhibitors. Most serpins control proteolytic cascades, certain serpins do not inhibit enzymes, but instead perform diverse functions such as storage (ovalbumin, in egg white), hormone carriage proteins (thyroxine-binding globulin, cortisol-binding globulin) and tumor suppressor genes (maspin). Most inhibitory serpins target chymotrypsin-like serine proteases. These enzymes are defined by the presence of a nucleophilic serine residue in their catalytic site. Some serpins inhibit other classes of protease. A number of such serpins have been shown to target cysteine proteases. These enzymes differ from serine proteases in that they are defined by the presence of a nucleophilic cysteine residue, rather than a serine residue, in their catalytic site. SerpinA12, also known as OL-64, Visceral adipose tissue-derived serine protease inhibitor, Vaspin, Visceral adipose-specific serpin and SERPINA12, is a secreted protein which belongs to the serpin family. SerpinA12 / Vaspin is expressed in visceral adipose tissues. It may modulates insulin action conceivably only in the presence of its yet undefined target proteases in white adipose tissues. SerpinA12 / Vaspin may be the compensatory molecule in the pathogenesis of metabolic syndrome and SerpinA12 / Vaspin recombinant protein or vaspin-mimicking agents such as vaspin analogs, or small molecule agents may be the link to drug discovery and development.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-2270R-A555)

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-A750)

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)

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-7536R-HRP)

Supplier: Bioss

Description: May modulates insulin action conceivably only in the presence of its yet undefined target proteases in white adipose tissues.Serpins are the largest and most diverse family of protease inhibitors. Most serpins control proteolytic cascades, certain serpins do not inhibit enzymes, but instead perform diverse functions such as storage (ovalbumin, in egg white), hormone carriage proteins (thyroxine-binding globulin, cortisol-binding globulin) and tumor suppressor genes (maspin). Most inhibitory serpins target chymotrypsin-like serine proteases. These enzymes are defined by the presence of a nucleophilic serine residue in their catalytic site. Some serpins inhibit other classes of protease. A number of such serpins have been shown to target cysteine proteases. These enzymes differ from serine proteases in that they are defined by the presence of a nucleophilic cysteine residue, rather than a serine residue, in their catalytic site. SerpinA12, also known as OL-64, Visceral adipose tissue-derived serine protease inhibitor, Vaspin, Visceral adipose-specific serpin and SERPINA12, is a secreted protein which belongs to the serpin family. SerpinA12 / Vaspin is expressed in visceral adipose tissues. It may modulates insulin action conceivably only in the presence of its yet undefined target proteases in white adipose tissues. SerpinA12 / Vaspin may be the compensatory molecule in the pathogenesis of metabolic syndrome and SerpinA12 / Vaspin recombinant protein or vaspin-mimicking agents such as vaspin analogs, or small molecule agents may be the link to drug discovery and development.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-6728R-CY5.5)

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-5777R-CY3)

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

Catalog Number: (BOSSBS-3785R-A680)

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-9010R-HRP)

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-FITC)

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: (USBI042413-BIOTIN)

Supplier: US Biological

Description: Anti-STK4 Rabbit Polyclonal Antibody (Biotin)

UOM: 1 * 200 µl

Catalog Number: (BOSSBS-9010R-A488)

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)

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-CY7)

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-3294R-A555)

Supplier: Bioss

Description: Protein which catalyzes the phosphorylation of serine or threonine residues on target proteins by using ATP as phosphate donor. Such phosphorylation may cause changes in the function of the target protein. Protein kinases share a conserved catalytic core common to both serine/ threonine and tyrosine protein kinases.

UOM: 1 * 100 µl