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Monoclonal Antibody Endopeptidase Activity

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents. Control of autophagy was largely discovered in yeast and involves proteins encoded by a set of autophagy-related genes (Atg) (1). Formation of autophagic vesicles requires a pair of essential ubiquitin-like conjugation systems, Atg12-Atg5 and Atg8-phosphatidylethanolamine (Atg8-PE), which are widely conserved in eukaryotes (2). Numerous mammalian counterparts to yeast Atg proteins have been described, including three Atg8 proteins (GATE-16, GABARAP, and LC3) and four Atg4 homologs (Atg4A/autophagin-2, Atg4B/autophagin-1, Atg4C/autophagin-3, and Atg4D/autophagin-4) (3-5). The cysteine protease Atg4 is pivotal to autophagosome membrane generation and regulation. Atg4 primes the Atg8 homolog for lipidation by cleaving its carboxy terminus and exposing its glycine residue for E1-like enzyme Atg7. The Atg8 homolog is transferred to the E2-like enzyme Atg3 before forming the Atg8-PE conjugate. During later stages of autophagy, Atg4 can reverse this lipidation event by cleaving PE, thereby recycling the Atg8 homolog (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents. Control of autophagy was largely discovered in yeast and involves proteins encoded by a set of autophagy-related genes (Atg) (1). Formation of autophagic vesicles requires a pair of essential ubiquitin-like conjugation systems, Atg12-Atg5 and Atg8-phosphatidylethanolamine (Atg8-PE), which are widely conserved in eukaryotes (2). Numerous mammalian counterparts to yeast Atg proteins have been described, including three Atg8 proteins (GATE-16, GABARAP, and LC3) and four Atg4 homologs (Atg4A/autophagin-2, Atg4B/autophagin-1, Atg4C/autophagin-3, and Atg4D/autophagin-4) (3-5). The cysteine protease Atg4 is pivotal to autophagosome membrane generation and regulation. Atg4 primes the Atg8 homolog for lipidation by cleaving its carboxy terminus and exposing its glycine residue for E1-like enzyme Atg7. The Atg8 homolog is transferred to the E2-like enzyme Atg3 before forming the Atg8-PE conjugate. During later stages of autophagy, Atg4 can reverse this lipidation event by cleaving PE, thereby recycling the Atg8 homolog (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The 26S proteasome is a highly abundant proteolytic complex involved in the degradation of ubiquitinated substrate proteins. It consists largely of two sub-complexes, the 20S catalytic core particle (CP) and the 19S/PA700 regulatory particle (RP) that can cap either end of the CP. The CP consists of two stacked heteroheptameric β-rings (β1-7) that contain three catalytic β-subunits and are flanked on either side by two heteroheptameric α-rings (α1-7). The RP includes a base and a lid, each having multiple subunits. The base, in part, is composed of a heterohexameric ring of ATPase subunits belonging to the AAA (ATPases Associated with diverse cellular Activities) family. The ATPase subunits function to unfold the substrate and open the gate formed by the α-subunits, thus exposing the unfolded substrate to the catalytic β-subunits. The lid consists of ubiquitin receptors and DUBs that function in recruitment of ubiquitinated substrates and modification of ubiquitin chain topology (1,2). Other modulators of proteasome activity, such as PA28/11S REG, can also bind to the end of the 20S CP and activate it (1,2).

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

Application Methods: Western Blotting

Background: The 20S proteasome is the major proteolytic enzyme complex involved in intracellular protein degradation. It consists of four stacked rings, each with seven distinct subunits. The two outer layers are identical rings composed of α subunits (called PSMAs), and the two inner layers are identical rings composed of β subunits. While the catalytic sites are located on the β rings (1-3), the α subunits are important for assembly and as binding sites for regulatory proteins (4). Seven different α and ten different β proteasome genes have been identified in mammals (5). PA700, PA28, and PA200 are three major protein complexes that function as activators of the 20S proteasome. PA700 binds polyubiquitin with high affinity and associates with the 20S proteasome to form the 26S proteasome, which preferentially degrades poly-ubiquitinated proteins (1-3). The proteasome has a broad substrate spectrum that includes cell cycle regulators, signaling molecules, tumor suppressors, and transcription factors. By controlling the degradation of these intracellular proteins, the proteasome functions in cell cycle regulation, cancer development, immune responses, protein folding, and disease progression (6-9).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The 26S proteasome is a highly abundant proteolytic complex involved in the degradation of ubiquitinated substrate proteins. It consists largely of two sub-complexes, the 20S catalytic core particle (CP) and the 19S/PA700 regulatory particle (RP) that can cap either end of the CP. The CP consists of two stacked heteroheptameric β-rings (β1-7) that contain three catalytic β-subunits and are flanked on either side by two heteroheptameric α-rings (α1-7). The RP includes a base and a lid, each having multiple subunits. The base, in part, is composed of a heterohexameric ring of ATPase subunits belonging to the AAA (ATPases Associated with diverse cellular Activities) family. The ATPase subunits function to unfold the substrate and open the gate formed by the α-subunits, thus exposing the unfolded substrate to the catalytic β-subunits. The lid consists of ubiquitin receptors and DUBs that function in recruitment of ubiquitinated substrates and modification of ubiquitin chain topology (1,2). Other modulators of proteasome activity, such as PA28/11S REG, can also bind to the end of the 20S CP and activate it (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The 26S proteasome is a highly abundant proteolytic complex involved in the degradation of ubiquitinated substrate proteins. It consists largely of two sub-complexes, the 20S catalytic core particle (CP) and the 19S/PA700 regulatory particle (RP) that can cap either end of the CP. The CP consists of two stacked heteroheptameric β-rings (β1-7) that contain three catalytic β-subunits and are flanked on either side by two heteroheptameric α-rings (α1-7). The RP includes a base and a lid, each having multiple subunits. The base, in part, is composed of a heterohexameric ring of ATPase subunits belonging to the AAA (ATPases Associated with diverse cellular Activities) family. The ATPase subunits function to unfold the substrate and open the gate formed by the α-subunits, thus exposing the unfolded substrate to the catalytic β-subunits. The lid consists of ubiquitin receptors and DUBs that function in recruitment of ubiquitinated substrates and modification of ubiquitin chain topology (1,2). Other modulators of proteasome activity, such as PA28/11S REG, can also bind to the end of the 20S CP and activate it (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Legumain (LGMN) is an asparaginyl endopeptidase that mediates lysosomal processing of antigen for class II MHC presentation. Under normal conditions, LGMN is mostly found in lysosomes. However, its expression level, cellular compartmentalization, and function may change under certain conditions, including cancer (1, 2, 3). In colorectal cancer, LGMN is upregulated and is found extracellularly and in the nucleus in both primary tumors and colorectal cancer cell lines (4, 5). Legumain forms homodimers and may be activated by postranstranslational modifications, including autoproteolytic cleavage, as it moves from one cellular compartment to another (6).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Kallikrein 3 (KLK3), also known as Prostate Specific Antigen (PSA), is a member of the glandular kallikrein subfamily of serine proteases (1). It is produced by prostate epithelial cells and is secreted into prostatic ducts. Upon cleavage of 7 amino-terminal amino acids (2), it is activated to liquefy semen in the seminal coagulum. Although PSA/KLK3 is produced in healthy individuals, investigators have found abnormally high levels in the blood of men with advanced prostate cancer (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Ubiquitinating enzymes (UBEs) catalyze protein ubiquitination, a reversible process countered by deubiquitinating enzyme (DUB) action (1,2). Five DUB subfamilies are recognized, including the USP, UCH, OTU, MJD, and JAMM enzymes. In humans, there are three proteasomal DUBs: PSMD14 (POH1/RPN11), UCH37 (UCH-L5), and Ubiquitin-Specific Protease 14, which is also known as the 60 kDa subunit of tRNA-guanine transglycosylase (USP14/TGT60 kDa). USP14 is recruited to the proteasome through its reversible association with the PSMD2 (S2/hRPN1) subunit of the 19S regulatory particle. Whereas PSMD14 appears to promote substrate degradation (3,4), USP14 is thought to antagonize substrate degradation (5-8). While the underlying mechanism for the opposing roles of these two proteasomal DUBs is still uncertain, it is thought that USP14 removes ubiquitin from substrate upon docking of the substrate with the 26S proteasome. Furthermore, USP14 trims ubiquitin residues from the distal end of the polyubiquitin chain, thus decreasing the affinity of the chain for the ubiquitin receptors of the proteasome, and allowing for enhanced substrate stability (6,9,10). Studies have elucidated a physiologic role for USP14 in regulating synaptic activity in mammals (11). Research studies have shown that targeting this activity with small molecule inhibitors has potential benefits for the treatment of neurodegenerative diseases and cancer (5,12).

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

Application Methods: Western Blotting

Background: The 26S proteasome is a highly abundant proteolytic complex involved in the degradation of ubiquitinated substrate proteins. It consists largely of two sub-complexes, the 20S catalytic core particle (CP) and the 19S/PA700 regulatory particle (RP) that can cap either end of the CP. The CP consists of two stacked heteroheptameric β-rings (β1-7) that contain three catalytic β-subunits and are flanked on either side by two heteroheptameric α-rings (α1-7). The RP includes a base and a lid, each having multiple subunits. The base, in part, is composed of a heterohexameric ring of ATPase subunits belonging to the AAA (ATPases Associated with diverse cellular Activities) family. The ATPase subunits function to unfold the substrate and open the gate formed by the α-subunits, thus exposing the unfolded substrate to the catalytic β-subunits. The lid consists of ubiquitin receptors and DUBs that function in recruitment of ubiquitinated substrates and modification of ubiquitin chain topology (1,2). Other modulators of proteasome activity, such as PA28/11S REG, can also bind to the end of the 20S CP and activate it (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: The 26S proteasome is a highly abundant proteolytic complex involved in the degradation of ubiquitinated substrate proteins. It consists largely of two sub-complexes, the 20S catalytic core particle (CP) and the 19S/PA700 regulatory particle (RP) that can cap either end of the CP. The CP consists of two stacked heteroheptameric β-rings (β1-7) that contain three catalytic β-subunits and are flanked on either side by two heteroheptameric α-rings (α1-7). The RP includes a base and a lid, each having multiple subunits. The base, in part, is composed of a heterohexameric ring of ATPase subunits belonging to the AAA (ATPases Associated with diverse cellular Activities) family. The ATPase subunits function to unfold the substrate and open the gate formed by the α-subunits, thus exposing the unfolded substrate to the catalytic β-subunits. The lid consists of ubiquitin receptors and DUBs that function in recruitment of ubiquitinated substrates and modification of ubiquitin chain topology (1,2). Other modulators of proteasome activity, such as PA28/11S REG, can also bind to the end of the 20S CP and activate it (1,2).

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

Application Methods: Western Blotting

Background: The 26S proteasome is a highly abundant proteolytic complex involved in the degradation of ubiquitinated substrate proteins. It consists largely of two sub-complexes, the 20S catalytic core particle (CP) and the 19S/PA700 regulatory particle (RP) that can cap either end of the CP. The CP consists of two stacked heteroheptameric β-rings (β1-7) that contain three catalytic β-subunits and are flanked on either side by two heteroheptameric α-rings (α1-7). The RP includes a base and a lid, each having multiple subunits. The base, in part, is composed of a heterohexameric ring of ATPase subunits belonging to the AAA (ATPases Associated with diverse cellular Activities) family. The ATPase subunits function to unfold the substrate and open the gate formed by the α-subunits, thus exposing the unfolded substrate to the catalytic β-subunits. The lid consists of ubiquitin receptors and DUBs that function in recruitment of ubiquitinated substrates and modification of ubiquitin chain topology (1,2). Other modulators of proteasome activity, such as PA28/11S REG, can also bind to the end of the 20S CP and activate it (1,2).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Napsin A is an aspartic proteinase that is expressed in normal lung and kidney (1). In the lung, napsin A is expressed by type II pneumocytes and alveolar macrophages, where it plays a role in processing surfactant protein B (2). Napsin A is expressed in lung adenocarcinomas, where it can be used to identify primary and metastatic lesions with greater sensitivity compared to TTF-1 (3,4). Napsin A expression has also been described in other types of cancer, such as kidney and thyroid cancer (5).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated PSA/KLK3 (D6B1) XP® Rabbit mAb #5365.
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Kallikrein 3 (KLK3), also known as Prostate Specific Antigen (PSA), is a member of the glandular kallikrein subfamily of serine proteases (1). It is produced by prostate epithelial cells and is secreted into prostatic ducts. Upon cleavage of 7 amino-terminal amino acids (2), it is activated to liquefy semen in the seminal coagulum. Although PSA/KLK3 is produced in healthy individuals, investigators have found abnormally high levels in the blood of men with advanced prostate cancer (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: Napsin A is an aspartic proteinase that is expressed in normal lung and kidney (1). In the lung, napsin A is expressed by type II pneumocytes and alveolar macrophages, where it plays a role in processing surfactant protein B (2). Napsin A is expressed in lung adenocarcinomas, where it can be used to identify primary and metastatic lesions with greater sensitivity compared to TTF-1 (3,4). Napsin A expression has also been described in other types of cancer, such as kidney and thyroid cancer (5).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Neutrophil elastase is hematopoietic serine protease that belongs to the chymotrypsin superfamily and plays a critical role in the innate immune function of mature neutrophils and monocytes (1,2). Neutrophil elastase is actively synthesized as an inactive zymogen in myelocytic precursor cells of the bone marrow, which then undergoes activation by limited proteolysis and sorting to primary (azurophil) storage granules of mature neutrophil granulocytes for regulated release (3,4). Research studies have shown that neutrophils play a significant role in mediating the inflammatory response through the release of neutrophil elastase, which activates pro-inflammatory cytokines and degrades components of the extracellular matrix and Gram-negative bacteria (5). Mutations in the gene encoding neutrophil elastase, ELA2, have been implicated in hematological diseases such as cyclic and severe congenital neutropenia, which is characterized by defects in promyelocyte maturation (6,7).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Caspase-1, or interleukin-1ß converting enzyme (ICE/ICEα), is a class I cysteine protease, which also includes caspases -4, -5, -11, and -12. Caspase-1 cleaves inflammatory cytokines such as pro-IL-1ß and interferon-γ inducing factor (IL-18) into their mature forms (1,2). Like other caspases, caspase-1 is proteolytically activated from a proenzyme to produce a tetramer of its two active subunits, p20 and p10. Caspase-1 has a large amino-terminal pro-domain that contains a caspase recruitment domain (CARD). Overexpression of caspase-1 can induce apoptosis (3). Mice deficient in caspase-1, however, have no overt defects in apoptosis but do have defects in the maturation of pro-IL-1β and are resistant to endotoxic shock (4,5). At least six caspase-1 isoforms have been identified, including caspase-1 α, β, γ, δ, ε and ζ (6). Most caspase-1 isoforms (α, β, γ and δ) produce products between 30-48 kDa and induce apoptosis upon over-expression. Caspase-1 ε typically contains only the p10 subunit, does not induce apoptosis and may act as a dominant negative. The widely expressed ζ isoform of caspase-1 induces apoptosis and lacks 39 amino-terminal residues found in the α isoform (6). Activation of caspase-1 occurs through an oligomerization molecular platform designated the "inflammasome" that includes caspase-5, Pycard/Asc, and NALP1 (7).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Caspase-3 (CPP-32, Apoptain, Yama, SCA-1) is a critical executioner of apoptosis, as it is either partially or totally responsible for the proteolytic cleavage of many key proteins, such as the nuclear enzyme poly (ADP-ribose) polymerase (PARP) (1). Activation of caspase-3 requires proteolytic processing of its inactive zymogen into activated p17 and p12 fragments. Cleavage of caspase-3 requires the aspartic acid residue at the P1 position (2).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Caspase-3 (8G10) Rabbit mAb #9665.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Caspase-3 (CPP-32, Apoptain, Yama, SCA-1) is a critical executioner of apoptosis, as it is either partially or totally responsible for the proteolytic cleavage of many key proteins, such as the nuclear enzyme poly (ADP-ribose) polymerase (PARP) (1). Activation of caspase-3 requires proteolytic processing of its inactive zymogen into activated p17 and p12 fragments. Cleavage of caspase-3 requires the aspartic acid residue at the P1 position (2).

$111
20 µl
$261
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Caspase-1, or interleukin-1ß converting enzyme (ICE/ICEα), is a class I cysteine protease, which also includes caspases -4, -5, -11, and -12. Caspase-1 cleaves inflammatory cytokines such as pro-IL-1ß and interferon-γ inducing factor (IL-18) into their mature forms (1,2). Like other caspases, caspase-1 is proteolytically activated from a proenzyme to produce a tetramer of its two active subunits, p20 and p10. Caspase-1 has a large amino-terminal pro-domain that contains a caspase recruitment domain (CARD). Overexpression of caspase-1 can induce apoptosis (3). Mice deficient in caspase-1, however, have no overt defects in apoptosis but do have defects in the maturation of pro-IL-1β and are resistant to endotoxic shock (4,5). At least six caspase-1 isoforms have been identified, including caspase-1 α, β, γ, δ, ε and ζ (6). Most caspase-1 isoforms (α, β, γ and δ) produce products between 30-48 kDa and induce apoptosis upon over-expression. Caspase-1 ε typically contains only the p10 subunit, does not induce apoptosis and may act as a dominant negative. The widely expressed ζ isoform of caspase-1 induces apoptosis and lacks 39 amino-terminal residues found in the α isoform (6). Activation of caspase-1 occurs through an oligomerization molecular platform designated the "inflammasome" that includes caspase-5, Pycard/Asc, and NALP1 (7).