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Rat Proteasomal Ubiquitin-Dependent Protein Catabolic Process

$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: 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, 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, Mouse, Rat

Application Methods: Western Blotting

Background: Ubiquitin is a conserved polypeptide unit that plays an important role in the ubiquitin-proteasome pathway. Ubiquitin can be covalently linked to many cellular proteins by the ubiquitination process, which targets proteins for degradation by the 26S proteasome. Three components are involved in the target protein-ubiquitin conjugation process. Ubiquitin is first activated by forming a thiolester complex with the activation component E1; the activated ubiquitin is subsequently transferred to the ubiquitin-carrier protein E2, then from E2 to ubiquitin ligase E3 for final delivery to the epsilon-NH2 of the target protein lysine residue (1-3). The ubiquitin-proteasome pathway has been implicated in a wide range of normal biological processes and in disease-related abnormalities. Several proteins such as IκB, p53, cdc25A, and Bcl-2 have been shown to be targets for the ubiquitin-proteasome process as part of regulation of cell cycle progression, differentiation, cell stress response, and apoptosis (4-7).

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

Application Methods: Immunofluorescence (Immunocytochemistry), 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: Immunofluorescence (Immunocytochemistry), 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: 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).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Parkin is a protein of 465 amino acids with an amino-terminal ubiquitin domain and a carboxy-terminal RING-box (1). In the case of autosomal recessive juvenile Parkinsonism (AR-JP), deletions have been found in the gene on chromosome 6 encoding the protein Parkin (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: 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: PSMD10/Gankyrin is an ankyrin-repeat chaperone protein that is involved in the assembly of the 19S regulatory particle of the proteasome (1). Reasearch studies have demonstrated that PSMD10 is oncogenic and is overexpressed in hepatocullar carcinomas (2). Investigators believe the oncogenicity of PSMD10 may be linked to its ability to bind and regulate the stability and activity of pRB, CDK4, MDM2, and RelA (2-5).

$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, 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: Western Blotting

Background: Parkin is a protein of 465 amino acids with an amino-terminal ubiquitin domain and a carboxy-terminal RING-box (1). In the case of autosomal recessive juvenile Parkinsonism (AR-JP), deletions have been found in the gene on chromosome 6 encoding the protein Parkin (2).

$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, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: β-transducin repeat-containing protein (β-TrCP or FBW1A) is an F-box family protein characterized by the presence of the protein-protein mediating F-box domain first described in cyclin F. F-box proteins act as substrate adaptors that target proteins containing a specific phosphorylated sequence element, referred to as a phosphodegron, to the SCF E3 ubiquitin ligase complex for ubiquitination (1,2). β-TrCP targets many important proteins with diverse functions, such as p53, H-Ras, Smad4, IκBα, β-catenin, and the cell cycle checkpoint protein claspin, for ubiquitin-mediated degradation (3-5). Research studies have shown that inhibition of β-TrCP expression has a demonstrated benefit in the treatment of prostate cancer (6).

$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, 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).