You Searched For: N-Boc-L-serine

Catalog Number: (BOSSBS-9500R-A350)

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-0559R-HRP)

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-A555)

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-10339R-A750)

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-1271R-A647)

Supplier: Bioss

Description: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins(also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Isoform 2 seems to be proteolytically inactive. [CATALYTIC ACTIVITY] Cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues. [SUBUNIT] Homotrimer. Interacts with MXI2. The mature protein, but not the precursor, binds to BIRC2, BIRC3 and XIAP.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9844R-A750)

Supplier: Bioss

Description: Cleavage of the serine proteinase plasminogen to form plasmin is the central event in the dissolution of blood clots by the fibrinolytic system.Plasminogen related protein B is encoded by the PLGLB1 and PLGLB2 genes. It may bind to lysine binding sites present in the kringle structures of plasminogen interfering with the binding of fibrin or alpha-2-antiplasmin to plasminogen. Within the fibrinolytic cascade, the serine proteinases urokinase-type plasminogen activator (uPA) and tissue-type plasminogen activator (tPA) activate the proenzyme plasminogen by cleaving plasminogen to form the fibrinolytically active enzyme plasmin. PLGLB2 (plasminogen-like B2), also known as PLGP1, is a 96 amino acid protein that resembles the N-terminal plasminogen activation peptide, which is released from plasminogen during conversion to plasmin.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-1271R-CY3)

Supplier: Bioss

Description: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins(also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Isoform 2 seems to be proteolytically inactive. [CATALYTIC ACTIVITY] Cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues. [SUBUNIT] Homotrimer. Interacts with MXI2. The mature protein, but not the precursor, binds to BIRC2, BIRC3 and XIAP.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9845R-A750)

Supplier: Bioss

Description: The serine protease inhibitors (serpins) compose a superfamily of proteins with a diverse set of functions, including the control of blood coagulation, complement activation, programmed cell death and development. Serpins are secreted glycoproteins that contain a stretch of peptide that mimics a true substrate for a corresponding serine protease. Protease nexin-1 (PN-1) is a serpin that inactivates several proteases, including thrombin, urokinase, plasminogen activators (PA) and plasmin. It is involved in tissue remodeling, cellular invasiveness, matrix degradation and tumor growth. PN-1 expression is abundant in the nervous system, where it inhibits thrombin, thereby playing a role in neural injury and repair processes. An imbalance between PN-1 and thrombin may be a contributing factor in the pathology of Alzheimer's disease.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-1271R-HRP)

Supplier: Bioss

Description: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins(also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Isoform 2 seems to be proteolytically inactive. [CATALYTIC ACTIVITY] Cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues. [SUBUNIT] Homotrimer. Interacts with MXI2. The mature protein, but not the precursor, binds to BIRC2, BIRC3 and XIAP.

UOM: 1 * 100 µl

Catalog Number: (USBIP2488-05F)

Supplier: US Biological

Description: Anti-PAK1 Rabbit Polyclonal Antibody

UOM: 1 * 100 µG

Catalog Number: (BOSSBS-10339R-A488)

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-FITC)

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-10339R-CY5)

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-9921R-A680)

Supplier: Bioss

Description: The Ca²⁺/calmodulin-dependent protein kinases (CaM kinases) comprise a structurally related subfamily of serine/threonine kinases which include CaMKI, CaMKII and CaMKIV. CaMKII is a ubiquitously expressed serine/threonine protein kinase that is activated by Ca²⁺and calmodulin (CaM) and has been implicated in regulation of the cell cycle and transcription. There are four CaMKII isozymes designated å, , © and ∂, which may or may not be co-expressed in the same tissue type. CaMKIV is stimulated by Ca²⁺ and CaM but phosphorylation by a CaMK is also required for full activation. Stimulation of the T cell receptor CD3 Signalling complex with an anti-CD3 monoclonal antibody leads to a 10 to 40 fold increase in CaMKIV activity. An additional kinase, CaMKK, functions to activate CaMKI through the specific phosphorylation of the regulatory threonine residue at position 177.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9500R-CY5.5)

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: (USBIS5382-01)

Supplier: US Biological

Description: Anti-SPTLC1 Rabbit Polyclonal Antibody

UOM: 1 * 200 µl