You Searched For: N-Boc-L-serine

Catalog Number: (BOSSBS-13131R-A555)

Supplier: Bioss

Description: The complement pathway is an important host defense system that contributes to both innate and acquired immunity. There are three pathways of complement activation: the classical pathway, lectin pathway and alternative pathway. Complement protein Factor I is a key serine protease that modulates the complement cascade by regulating the levels of C3 convertases. It circulates in plasma as a heavily N-glycosylated heterodimer made up of two disulfide linked chains, each carrying three N-linked oligosaccharide chains that may have both structural and functional roles in the interactions with the natural substrate and the cofactor during catalysis. Factor I is a serine protease with a high degree of specificity for C3b and C4b. It requires protein cofactors for cleavage of these complement proteins; Factor H, CR1 or MCP are required for C3b cleavage, and C4bp or CR1 are required for C4b cleavage.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-0559R-A488)

Supplier: Bioss

Description: CDK5 is serine/threonine kinase involved in synaptic regulation and neuronal development; phosphorylates synaptic protein Pctaire1; regulates acetylcholine receptor expression.CDK5 is a member of the cyclindependent kinase family of serine/threonine kinases. It is present in numerous mammalian tissues including kidney, testes, and ovary. Its activity is detected almost exclusively in brain extracts. Neuronal and muscle cells contain the highest amount of this protein. Similar to other Cdks, monomeric Cdk5 displays no enzymatic activity, but Cdk5 is not activated by cyclins. Instead, the p35 protein, which is expressed solely in the brain, activates Cdk5. Cdk5 interacts with D1 and D3 type G1 cyclins and can phosphorylate histone H1, TAU, MAP2 and NF-H and NF-M. Cdk5 activity is involved in terminal differentiation of neurons and muscle cells.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13038R-CY3)

Supplier: Bioss

Description: Dynamin I is a GTPase enzyme required for the retrieval of synaptic vesicles after exocytosis and functions in endocytosis by stimulating assembly of invaginating synaptic vesicles (1). Dynamin I is phosphorylated in nerve terminals exclusively in the cytosolic compartment and in vitro by protein kinase C (PKC) (2–5). The phosphorylation site in PKC-phosphorylated Dynamin I is a single site at Serine 795, which is located near a binding site for the SH3 domain of p85, the regulatory subunit of phosphatidylinositol 3-kinase (2–5). Dephosphorylation is required for synaptic vesicle retrieval, suggesting that phosphorylation affects the subcellular localization of Dynamin I (5). Mouse, rat and human Dynamin I are phosphorylated on serine residues, including Ser 778, by Cdk5, regulating PACSIN1 recruitment and enabling synaptic vesicle endocytosis.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13038R-A555)

Supplier: Bioss

Description: Dynamin I is a GTPase enzyme required for the retrieval of synaptic vesicles after exocytosis and functions in endocytosis by stimulating assembly of invaginating synaptic vesicles (1). Dynamin I is phosphorylated in nerve terminals exclusively in the cytosolic compartment and in vitro by protein kinase C (PKC) (2–5). The phosphorylation site in PKC-phosphorylated Dynamin I is a single site at Serine 795, which is located near a binding site for the SH3 domain of p85, the regulatory subunit of phosphatidylinositol 3-kinase (2–5). Dephosphorylation is required for synaptic vesicle retrieval, suggesting that phosphorylation affects the subcellular localization of Dynamin I (5). Mouse, rat and human Dynamin I are phosphorylated on serine residues, including Ser 778, by Cdk5, regulating PACSIN1 recruitment and enabling synaptic vesicle endocytosis.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-1704R-HRP)

Supplier: Bioss

Description: Serine protease inhibitor. This inhibitor acts as 'bait' for tissue plasminogen activator, urokinase, protein C and matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11177R-CY7)

Supplier: Bioss

Description: Cysteine-rich secretory proteins (CRISPs) represent a family of evolutionarily conserved proteins which play a role in the innate immune system and are transcriptionally regulated by androgens in several tissues. CRISP-8 (Cysteine-rich secretory protein 8), also known as PI15 (Peptidase inhibitor 15), P25TI or SugarCrisp, is a 258 amino acid secreted protein that belongs to the CRISP family. Expressed at low levels in thyroid, prostate, salivary and mammary tissue, CRISP-8 functions as a serine protease inhibitor that exhibits weak inhibitory action against Trypsin, a serine protease found in the digestive system. In addition to its role as a protease inhibitor, CRISP-8 is secreted in neuroblastoma and glioblastoma cell lines, suggesting a role for CRISP-8 in tumor formation and metastasis within the central nervous system.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11177R-A488)

Supplier: Bioss

Description: Cysteine-rich secretory proteins (CRISPs) represent a family of evolutionarily conserved proteins which play a role in the innate immune system and are transcriptionally regulated by androgens in several tissues. CRISP-8 (Cysteine-rich secretory protein 8), also known as PI15 (Peptidase inhibitor 15), P25TI or SugarCrisp, is a 258 amino acid secreted protein that belongs to the CRISP family. Expressed at low levels in thyroid, prostate, salivary and mammary tissue, CRISP-8 functions as a serine protease inhibitor that exhibits weak inhibitory action against Trypsin, a serine protease found in the digestive system. In addition to its role as a protease inhibitor, CRISP-8 is secreted in neuroblastoma and glioblastoma cell lines, suggesting a role for CRISP-8 in tumor formation and metastasis within the central nervous system.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11177R-A680)

Supplier: Bioss

Description: Cysteine-rich secretory proteins (CRISPs) represent a family of evolutionarily conserved proteins which play a role in the innate immune system and are transcriptionally regulated by androgens in several tissues. CRISP-8 (Cysteine-rich secretory protein 8), also known as PI15 (Peptidase inhibitor 15), P25TI or SugarCrisp, is a 258 amino acid secreted protein that belongs to the CRISP family. Expressed at low levels in thyroid, prostate, salivary and mammary tissue, CRISP-8 functions as a serine protease inhibitor that exhibits weak inhibitory action against Trypsin, a serine protease found in the digestive system. In addition to its role as a protease inhibitor, CRISP-8 is secreted in neuroblastoma and glioblastoma cell lines, suggesting a role for CRISP-8 in tumour formation and metastasis within the central nervous system.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-10339R-CY7)

Supplier: Bioss

Description: The complement pathway is an important host defense system that contributes to both innate and acquired immunity. There are three pathways of complement activation: the classical pathway, lectin pathway and alternative pathway. Complement protein Factor I is a key serine protease that modulates the complement cascade by regulating the levels of C3 convertases. It circulates in plasma as a heavily N-glycosylated heterodimer made up of two disulfide linked chains, each carrying three N-linked oligosaccharide chains that may have both structural and functional roles in the interactions with the natural substrate and the cofactor during catalysis. Factor I is a serine protease with a high degree of specificity for C3b and C4b. It requires protein cofactors for cleavage of these complement proteins; Factor H, CR1 or MCP are required for C3b cleavage, and C4bp or CR1 are required for C4b cleavage.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13131R-CY7)

Supplier: Bioss

Description: The complement pathway is an important host defense system that contributes to both innate and acquired immunity. There are three pathways of complement activation: the classical pathway, lectin pathway and alternative pathway. Complement protein Factor I is a key serine protease that modulates the complement cascade by regulating the levels of C3 convertases. It circulates in plasma as a heavily N-glycosylated heterodimer made up of two disulfide linked chains, each carrying three N-linked oligosaccharide chains that may have both structural and functional roles in the interactions with the natural substrate and the cofactor during catalysis. Factor I is a serine protease with a high degree of specificity for C3b and C4b. It requires protein cofactors for cleavage of these complement proteins; Factor H, CR1 or MCP are required for C3b cleavage, and C4bp or CR1 are required for C4b cleavage.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-0559R-CY3)

Supplier: Bioss

Description: CDK5 is serine/threonine kinase involved in synaptic regulation and neuronal development; phosphorylates synaptic protein Pctaire1; regulates acetylcholine receptor expression.CDK5 is a member of the cyclindependent kinase family of serine/threonine kinases. It is present in numerous mammalian tissues including kidney, testes, and ovary. Its activity is detected almost exclusively in brain extracts. Neuronal and muscle cells contain the highest amount of this protein. Similar to other Cdks, monomeric Cdk5 displays no enzymatic activity, but Cdk5 is not activated by cyclins. Instead, the p35 protein, which is expressed solely in the brain, activates Cdk5. Cdk5 interacts with D1 and D3 type G1 cyclins and can phosphorylate histone H1, TAU, MAP2 and NF-H and NF-M. Cdk5 activity is involved in terminal differentiation of neurons and muscle cells.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9500R-CY7)

Supplier: Bioss

Description: Hemostasis following tissue injury involves the deployment of essential plasma procoagulants (prothrombin, and factors X, IX, V, and VIII), which are involved in a blood coagulation cascade that leads to the formation of insoluble fibrin clots and the promotion of platelet aggregation (1-3). Coagulation factor IX (plasma thromboplastic component, F9, F.IX, HEMB) is a vitamin K-dependent, single chain serine protease that is synthesized in the liver and circulates as an inactive precursor (3,4). Factor XIa mediated proteolytic cleavage of factor IX generates factor IXa, an active serine protease composed of a 145 amino acid light chain and a 236 amino acid catalytic heavy chain, linked through disulfide bonds (5). Genetic alterations at the Factor IX locus such as point mutations, insertions and deletions, can lead to hemophilia B, also known as Christmas disease (6).

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-8613R-FITC)

Supplier: Bioss

Description: Component C2 which is part of the classical pathway of the complement system is cleaved by activated factor C1 into two fragments: C2b and C2a. C2a, a serine protease, then combines with complement factor C4b to generate the C3 or C5 convertase.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-1636R-A350)

Supplier: Bioss

Description: Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-8613R-HRP)

Supplier: Bioss

Description: Component C2 which is part of the classical pathway of the complement system is cleaved by activated factor C1 into two fragments: C2b and C2a. C2a, a serine protease, then combines with complement factor C4b to generate the C3 or C5 convertase.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-1636R-A488)

Supplier: Bioss

Description: Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin.

UOM: 1 * 100 µl