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Rat Serine-Type Endopeptidase Activity

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: High temperature requirement protein A2 (HtrA2)/Omi is a serine protease with homology to the E. coli HtrA protein (DegP) and is thought to be involved in apoptosis and stress-induced degradation of misfolded proteins (1). While HtrA2 was orignally identified to be present in either the nucleus (1) or endoplasmic reticulum (2), subsequent studies have shown that it localizes in mitochondria and is released during apoptosis (3-8). HtrA2 is produced as a 50 kDa zymogen that is cleaved to generate a 36 kDa mature protein that exposes an amino terminal motif (AVPS) resembling that of the IAP inhibitor Smac/Diablo (3-8). Like Smac, interaction between HtrA2 and IAP family members, such as XIAP, antagonizes their inhibition of caspase activity and protection from apoptosis (3-8). Interestingly, HtrA2 knock-out mice did not show signs of reduced apoptosis, but rather had a loss of neurons in the striatum and a Parkinson's-like phenotype, suggesting that HtrA2 might have a neuroprotective function (9-11). This activity is associated with the protease activity of HtrA2 (9). Furthermore, research studies have shown that loss of function mutations in the HtrA2 gene are associated with Parkinson's disease (12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The proprotein convertases (PCs) are enzymes that activate precursor proteins through proteolytic cleavage within the secretory pathway. PCs comprise several enzymes that are basic amino acid-specific proteinases (furin, PC1/3, PC2, PC4, PACE4, PC5/6, and PC7), as well as nonbasic amino acid convertases (S1P and PC9) (1). PCs have a common structure that includes an N-terminal signal peptide for secretory pathway targeting; a pro-domain that is thought to act as an intramolecular chaperone; a catalytic domain containing the active site; a P-domain that contributes to the overall folding of the enzyme by regulating stability, calcium-, and pH-dependence; and a C-terminal domain that interacts with the membrane (2). PCs act in a tissue- and substrate-specific fashion to generate an array of bioactive peptides and proteins from precursors, both in the brain and the periphery (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: High temperature requirement protein A2 (HtrA2)/Omi is a serine protease with homology to the E. coli HtrA protein (DegP) and is thought to be involved in apoptosis and stress-induced degradation of misfolded proteins (1). While HtrA2 was orignally identified to be present in either the nucleus (1) or endoplasmic reticulum (2), subsequent studies have shown that it localizes in mitochondria and is released during apoptosis (3-8). HtrA2 is produced as a 50 kDa zymogen that is cleaved to generate a 36 kDa mature protein that exposes an amino terminal motif (AVPS) resembling that of the IAP inhibitor Smac/Diablo (3-8). Like Smac, interaction between HtrA2 and IAP family members, such as XIAP, antagonizes their inhibition of caspase activity and protection from apoptosis (3-8). Interestingly, HtrA2 knock-out mice did not show signs of reduced apoptosis, but rather had a loss of neurons in the striatum and a Parkinson's-like phenotype, suggesting that HtrA2 might have a neuroprotective function (9-11). This activity is associated with the protease activity of HtrA2 (9). Furthermore, research studies have shown that loss of function mutations in the HtrA2 gene are associated with Parkinson's disease (12).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: The proprotein convertases (PCs) are enzymes that activate precursor proteins through proteolytic cleavage within the secretory pathway. PCs comprise several enzymes that are basic amino acid-specific proteinases (furin, PC1/3, PC2, PC4, PACE4, PC5/6, and PC7), as well as nonbasic amino acid convertases (S1P and PC9) (1). PCs have a common structure that includes an N-terminal signal peptide for secretory pathway targeting; a pro-domain that is thought to act as an intramolecular chaperone; a catalytic domain containing the active site; a P-domain that contributes to the overall folding of the enzyme by regulating stability, calcium-, and pH-dependence; and a C-terminal domain that interacts with the membrane (2). PCs act in a tissue- and substrate-specific fashion to generate an array of bioactive peptides and proteins from precursors, both in the brain and the periphery (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Tripeptidyl-peptidase 2 (TPP2) is a well-conserved subtilisin-like amino peptidase that is expressed predominantly in the cytoplasmic compartment (1,2). The amino-terminal region of TPP2 harbors a catalytic triad that is characteristic of serine proteases and allows for TPP2 cleavage of tripeptides from the free amino terminus of oligopeptide substrates (3). TPP2 is a large (>5MDa) homooligomeric protease in which proteolytic activity is regulated by subunit oligomerization (4,5). While TPP2 plays a general role in amino acid homeostasis, research studies demonstrate that TPP2 is involved in MHC class I antigen presentation (6,7) and DNA-damage repair (8). TPP2 activity is required for the survival of Burkitt's lymphoma cells, suggesting a possible role for TPP2 in oncogenesis (9). Additional research studies show that TPP2 proteolytic activity is important for regulating lysosome abundance and glycolytic metabolism and that TPP2 deficiency leads to defects in adaptive immunity, innate immunity, and nervous system development (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: PRSS15/LONP1 is an ATP-dependent serine protease that selectively degrades misfolded, misassembled, or damaged proteins in mitochondrial matrix. PRSS15/LONP1 is induced by hypoxic, proteotoxic, and endoplasmic reticulum (ER) stress to support cell survival (1). It has been reported that PRSS15/LONP1 inducibility is decreased during aging and chronic stress (2-4). PRSS15/LONP1 is found to be substantially elevated in lymphoma cells compared to resting or activated B cells, and knock-down or inhibition of PRSS15/LONP1 induces apoptosis in lymphoma cells (5). Mutation in PRSS15/LONP1 is associated with CODAS syndrome, a multi-system developmental disorder characterized by cerebral, ocular, dental, auricular, and skeletal anomalies (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: The Kazal type 3 serine peptidase inhibitor (SPINK3) is a serine peptidase inhibitor expressed in the adult pancreas that protects acinar cells from trypsin-induced cell damage (1). Ingestion of milk by newborn SPINK3 knock out mice triggers autophagic cell death in pancreatic acinar cells and the complete disappearance of the pancreas (2). Mutations in the human SPINK3 homolog (known as SPINK1) are associated with chronic pancreatitis, presumably through decreased protection against trypsin-induced autophagic cell death (1,3). SPINK3 may be involved in the embryonic development of several other tissues (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: RECK (reversion-inducing cysteine-rich protein with Kazal motif) is a GPI-anchored membrane glycoprotein that negatively regulates members of the matrix metalloproteinase (MMP) family and functions as a suppressor of transformation (1,2). Its function in MMP inhibition makes RECK a crucial factor in the regulation of extracellular matrix formation and stability during development (2-4). RECK has also been linked to the regulation of other extracellar matrix proteases such as ADAM10 and CD13 and functions in modulating target protein endocytosis and Notch signaling (5,6). RECK is widely expressed in normal tissue and decreased expression of RECK due to promoter methylation has been correlated with tumor transformation, angiogenesis and metastasis (1,7-9). Therefore, loss of RECK expression serves as a prognostic hallmark for cancer malignancy (10,11)

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Maspin (SERPINB5) was discovered as a mammary tumor suppressor that is expressed in normal mammary epithelium but lost in most breast cancer cell lines (1). While maspin is related to the serpin family of serine protease inhibitors, it may not function as a protease inhibitor (2). It plays an essential role in embryonic development through critical roles in cell adhesion (3). While the precise mechanism of maspin signaling is unclear (4), the tumor suppressing activity of maspin has been attributed to its ability to inhibit cell invasion/metastasis (5,6) and angiogenesis (7), while promoting apoptosis (8). Nuclear translocation of active IKKα has been shown to repress maspin transcription and promote prostate cancer metastasis (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Raf kinase inhibitor protein (RKIP) is a member of the phosphatidylethanolamine-binding protein (PEBP) family that associates with Raf-1 and the MEK and MAP kinases (1). RKIP has been shown to form a complex with Raf-1, MEK, and Erk (2). Although MEK and Erk can simultaneously bind RKIP, the association between Raf-1 and RKIP and that of RKIP and MEK are mutually exclusive. Thus, RKIP competitively disrupts the Raf-1-MEK complex and effectively terminates signal transmission from Raf-1 to MAP kinases (2). The inhibitory effect of RKIP on MAP kinase signaling is eliminated by PKC phosphorylation of RKIP at Ser153 (3). PKC phosphorylation on Ser153 also promotes the association of RKIP with GRK2, which prevents GRK2-dependent internalization of GPCR (4). RKIP also interacts with modules of the NF-κB pathway, including NF-κB-inducing kinase (NIK), TAK1, IKKα and IKKβ (5). These interactions antagonize cytokine-induced activation of the NF-κB pathway (5). Restoration of RKIP expression is associated with the inhibition of prostate cancer metastasis, implying that RKIP may be a potential clinical target as a suppressor of tumor metastasis through inhibition of vascular invasion (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Raf kinase inhibitor protein (RKIP) is a member of the phosphatidylethanolamine-binding protein (PEBP) family that associates with Raf-1 and the MEK and MAP kinases (1). RKIP has been shown to form a complex with Raf-1, MEK, and Erk (2). Although MEK and Erk can simultaneously bind RKIP, the association between Raf-1 and RKIP and that of RKIP and MEK are mutually exclusive. Thus, RKIP competitively disrupts the Raf-1-MEK complex and effectively terminates signal transmission from Raf-1 to MAP kinases (2). The inhibitory effect of RKIP on MAP kinase signaling is eliminated by PKC phosphorylation of RKIP at Ser153 (3). PKC phosphorylation on Ser153 also promotes the association of RKIP with GRK2, which prevents GRK2-dependent internalization of GPCR (4). RKIP also interacts with modules of the NF-κB pathway, including NF-κB-inducing kinase (NIK), TAK1, IKKα and IKKβ (5). These interactions antagonize cytokine-induced activation of the NF-κB pathway (5). Restoration of RKIP expression is associated with the inhibition of prostate cancer metastasis, implying that RKIP may be a potential clinical target as a suppressor of tumor metastasis through inhibition of vascular invasion (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Raf kinase inhibitor protein (RKIP) is a member of the phosphatidylethanolamine-binding protein (PEBP) family that associates with Raf-1 and the MEK and MAP kinases (1). RKIP has been shown to form a complex with Raf-1, MEK, and Erk (2). Although MEK and Erk can simultaneously bind RKIP, the association between Raf-1 and RKIP and that of RKIP and MEK are mutually exclusive. Thus, RKIP competitively disrupts the Raf-1-MEK complex and effectively terminates signal transmission from Raf-1 to MAP kinases (2). The inhibitory effect of RKIP on MAP kinase signaling is eliminated by PKC phosphorylation of RKIP at Ser153 (3). PKC phosphorylation on Ser153 also promotes the association of RKIP with GRK2, which prevents GRK2-dependent internalization of GPCR (4). RKIP also interacts with modules of the NF-κB pathway, including NF-κB-inducing kinase (NIK), TAK1, IKKα and IKKβ (5). These interactions antagonize cytokine-induced activation of the NF-κB pathway (5). Restoration of RKIP expression is associated with the inhibition of prostate cancer metastasis, implying that RKIP may be a potential clinical target as a suppressor of tumor metastasis through inhibition of vascular invasion (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Raf kinase inhibitor protein (RKIP) is a member of the phosphatidylethanolamine-binding protein (PEBP) family that associates with Raf-1 and the MEK and MAP kinases (1). RKIP has been shown to form a complex with Raf-1, MEK, and Erk (2). Although MEK and Erk can simultaneously bind RKIP, the association between Raf-1 and RKIP and that of RKIP and MEK are mutually exclusive. Thus, RKIP competitively disrupts the Raf-1-MEK complex and effectively terminates signal transmission from Raf-1 to MAP kinases (2). The inhibitory effect of RKIP on MAP kinase signaling is eliminated by PKC phosphorylation of RKIP at Ser153 (3). PKC phosphorylation on Ser153 also promotes the association of RKIP with GRK2, which prevents GRK2-dependent internalization of GPCR (4). RKIP also interacts with modules of the NF-κB pathway, including NF-κB-inducing kinase (NIK), TAK1, IKKα and IKKβ (5). These interactions antagonize cytokine-induced activation of the NF-κB pathway (5). Restoration of RKIP expression is associated with the inhibition of prostate cancer metastasis, implying that RKIP may be a potential clinical target as a suppressor of tumor metastasis through inhibition of vascular invasion (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Amyloid β (Aβ) precursor protein (APP) is a 100-140 kDa transmembrane glycoprotein that exists as several isoforms (1). The amino acid sequence of APP contains the amyloid domain, which can be released by a two-step proteolytic cleavage (1). The extracellular deposition and accumulation of the released Aβ fragments form the main components of amyloid plaques in Alzheimer's disease (1). APP can be phosphorylated at several sites, which may affect the proteolytic processing and secretion of this protein (2-5). Phosphorylation at Thr668 (a position corresponding to the APP695 isoform) by cyclin-dependent kinase is cell-cycle dependent and peaks during G2/M phase (4). APP phosphorylated at Thr668 exists in adult rat brain and correlates with cultured neuronal differentiation (5,6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Amyloid β (Aβ) precursor protein (APP) is a 100-140 kDa transmembrane glycoprotein that exists as several isoforms (1). The amino acid sequence of APP contains the amyloid domain, which can be released by a two-step proteolytic cleavage (1). The extracellular deposition and accumulation of the released Aβ fragments form the main components of amyloid plaques in Alzheimer's disease (1). APP can be phosphorylated at several sites, which may affect the proteolytic processing and secretion of this protein (2-5). Phosphorylation at Thr668 (a position corresponding to the APP695 isoform) by cyclin-dependent kinase is cell-cycle dependent and peaks during G2/M phase (4). APP phosphorylated at Thr668 exists in adult rat brain and correlates with cultured neuronal differentiation (5,6).