Description
RP1-Enteropeptidase is a polyclonal antibody made to the serine protease enteropeptidase. The antibody is made to a synthetic peptide based on the aminoterminal end of human enteropeptidase. The antibody has been peptide-affinity purified, concentrated to 1.0 mg/ml, with the addition of 0.05% sodium azide as preservative and 50% glycerol as cryoprotectant.
Use
The name enteropeptidase replaced the name enterokinase, a name applied by the Pavlov laboratory in their pioneering work on digestion. The initial discovery indicated that enterokinase increased the catalytic activity of trypsin and other digestive enzymes, but it was unclear for another generation whether the activity was enzymatic of some sort of cofactor. Enteropeptidase is a member of the chymotrypsin-like PA clade, using the MEROPS terminology, in the S1A family. These serine proteinases all share a similar catalytic domain topology, with a canonical HDS catalytic triad in the catalytic domain. Unlike the other members, enterokinase has a much different domain structure for the rest of the molecule, and is localized to the brush border cells of the intestinal tract. The domain structure of enteropeptidase is perhaps more like the transmembrane serine proteinases, such as matriptase. The aminoterminal end is a cytoplasmic domain, followed by a transmembrane insertion domain, a SEA domain, an LDL domain, CUB domain, MAM, another CUB and LDL domain, a spacer region, and the catalytic domain at the carboxyterminal end. All of the different accessory domains (CUB, MAM, LDL, SEA) confer a much more regulated identity to enteropeptidase, relative to the soluble serine proteinases. In addition, the relatively strict substrate preference of DDDD'K limits enteropeptidase mainly to the activation of trypsin from trypsinogen. The relatively limited substrate specificity has led to enteropeptiodase being used as the scissile element in fusion proteins that have the enteropeptidase cleave site engineered between the carrier protein and the target sequence. Enteropeptidase is secreted as a zymogen, and it was thought that trypsin activates the enzyme, although this another enzyme, duodenase, has been proposed to fill this function in cattle. If there is a human ortholog for duodenase it has yet to be identified at this point. Based on the enteropeptidase cleavage specificity it seems unlikely that enteropeptidase autoactivates. The activation of trypsin is a key step in digestion, and leads to a cascade of enzyme activation in the intestines. The membrane attached enteropeptidase is cleaved at the start of the catalytic domain to yield the active form, the light chain. The light chain is held attached to the heavy chain by a disulfide bond. The 1019 amino acid enteropeptidase sequence encodes a protein with predicted mass of 112.9 kDa and a pI of 4.72. A significant amount of glycosylation increases the apparent molecular weight to 150 kDa, and when reduced the heavy and light chaind run separatly. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species. FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for approximately 12 months at -20C.
Description
RP2-Enteropeptidase is a polyclonal antibody made to the serine protease enteropeptidase. The antibody is made to a synthetic peptide based on the SEA domain of human enteropeptidase. The antibody has been peptide-affinity purified, concentrated to 1.0 mg/ml, with the addition of 0.05% sodium azide as preservative and 50% glycerol as cryoprotectant.
Use
The name enteropeptidase replaced the name enterokinase, a name applied by the Pavlov laboratory in their pioneering work on digestion. The initial discovery indicated that enterokinase increased the catalytic activity of trypsin and other digestive enzymes, but it was unclear for another generation whether the activity was enzymatic of some sort of cofactor. Enteropeptidase is a member of the chymotrypsin-like PA clade, using the MEROPS terminology, in the S1A family. These serine proteinases all share a similar catalytic domain topology, with a canonical HDS catalytic triad in the catalytic domain. Unlike the other members, enterokinase has a much different domain structure for the rest of the molecule, and is localized to the brush border cells of the intestinal tract. The domain structure of enteropeptidase is perhaps more like the transmembrane serine proteinases, such as matriptase. The aminoterminal end is a cytoplasmic domain, followed by a transmembrane insertion domain, a SEA domain, an LDL domain, CUB domain, MAM, another CUB and LDL domain, a spacer region, and the catalytic domain at the carboxyterminal end. All of the different accessory domains (CUB, MAM, LDL, SEA) confer a much more regulated identity to enteropeptidase, relative to the soluble serine proteinases. In addition, the relatively strict substrate preference of DDDD'K limits enteropeptidase mainly to the activation of trypsin from trypsinogen. The relatively limited substrate specificity has led to enteropeptiodase being used as the scissile element in fusion proteins that have the enteropeptidase cleave site engineered between the carrier protein and the target sequence. Enteropeptidase is secreted as a zymogen, and it was thought that trypsin activates the enzyme, although this another enzyme, duodenase, has been proposed to fill this function in cattle. If there is a human ortholog for duodenase it has yet to be identified at this point. Based on the enteropeptidase cleavage specificity it seems unlikely that enteropeptidase autoactivates. The activation of trypsin is a key step in digestion, and leads to a cascade of enzyme activation in the intestines. The membrane attached enteropeptidase is cleaved at the start of the catalytic domain to yield the active form, the light chain. The light chain is held attached to the heavy chain by a disulfide bond. The 1019 amino acid enteropeptidase sequence encodes a protein with predicted mass of 112.9 kDa and a pI of 4.72. A significant amount of glycosylation increases the apparent molecular weight to 150 kDa, and when reduced the heavy and light chaind run separatly. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species. FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for approximately 12 months at -20C.
Description
RP3-Enteropeptidase is a polyclonal antibody made to the serine protease enteropeptidase. The antibody is made to a synthetic peptide based on the spacer region of human enteropeptidase. The antibody has been peptide-affinity purified, concentrated to 1.0 mg/ml, with the addition of 0.05% sodium azide as preservative and 50% glycerol as cryoprotectant.
Use
The name enteropeptidase replaced the name enterokinase, a name applied by the Pavlov laboratory in their pioneering work on digestion. The initial discovery indicated that enterokinase increased the catalytic activity of trypsin and other digestive enzymes, but it was unclear for another generation whether the activity was enzymatic of some sort of cofactor. Enteropeptidase is a member of the chymotrypsin-like PA clade, using the MEROPS terminology, in the S1A family. These serine proteinases all share a similar catalytic domain topology, with a canonical HDS catalytic triad in the catalytic domain. Unlike the other members, enterokinase has a much different domain structure for the rest of the molecule, and is localized to the brush border cells of the intestinal tract. The domain structure of enteropeptidase is perhaps more like the transmembrane serine proteinases, such as matriptase. The aminoterminal end is a cytoplasmic domain, followed by a transmembrane insertion domain, a SEA domain, an LDL domain, CUB domain, MAM, another CUB and LDL domain, a spacer region, and the catalytic domain at the carboxyterminal end. All of the different accessory domains (CUB, MAM, LDL, SEA) confer a much more regulated identity to enteropeptidase, relative to the soluble serine proteinases. In addition, the relatively strict substrate preference of DDDD'K limits enteropeptidase mainly to the activation of trypsin from trypsinogen. The relatively limited substrate specificity has led to enteropeptiodase being used as the scissile element in fusion proteins that have the enteropeptidase cleave site engineered between the carrier protein and the target sequence. Enteropeptidase is secreted as a zymogen, and it was thought that trypsin activates the enzyme, although this another enzyme, duodenase, has been proposed to fill this function in cattle. If there is a human ortholog for duodenase it has yet to be identified at this point. Based on the enteropeptidase cleavage specificity it seems unlikely that enteropeptidase autoactivates. The activation of trypsin is a key step in digestion, and leads to a cascade of enzyme activation in the intestines. The membrane attached enteropeptidase is cleaved at the start of the catalytic domain to yield the active form, the light chain. The light chain is held attached to the heavy chain by a disulfide bond. The 1019 amino acid enteropeptidase sequence encodes a protein with predicted mass of 112.9 kDa and a pI of 4.72. A significant amount of glycosylation increases the apparent molecular weight to 150 kDa, and when reduced the heavy and light chaind run separatly. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species. FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for approximately 12 months at -20C.
Description
RP4-Enteropeptidase is a polyclonal antibody made to the serine protease enteropeptidase. The antibody is made to a synthetic peptide based on the catalytic domain of human enteropeptidase. The antibody has been peptide-affinity purified, concentrated to 1.0 mg/ml, with the addition of 0.05% sodium azide as preservative and 50% glycerol as cryoprotectant.
Use
The name enteropeptidase replaced the name enterokinase, a name applied by the Pavlov laboratory in their pioneering work on digestion. The initial discovery indicated that enterokinase increased the catalytic activity of trypsin and other digestive enzymes, but it was unclear for another generation whether the activity was enzymatic of some sort of cofactor. Enteropeptidase is a member of the chymotrypsin-like PA clade, using the MEROPS terminology, in the S1A family. These serine proteinases all share a similar catalytic domain topology, with a canonical HDS catalytic triad in the catalytic domain. Unlike the other members, enterokinase has a much different domain structure for the rest of the molecule, and is localized to the brush border cells of the intestinal tract. The domain structure of enteropeptidase is perhaps more like the transmembrane serine proteinases, such as matriptase. The aminoterminal end is a cytoplasmic domain, followed by a transmembrane insertion domain, a SEA domain, an LDL domain, CUB domain, MAM, another CUB and LDL domain, a spacer region, and the catalytic domain at the carboxyterminal end. All of the different accessory domains (CUB, MAM, LDL, SEA) confer a much more regulated identity to enteropeptidase, relative to the soluble serine proteinases. In addition, the relatively strict substrate preference of DDDD'K limits enteropeptidase mainly to the activation of trypsin from trypsinogen. The relatively limited substrate specificity has led to enteropeptiodase being used as the scissile element in fusion proteins that have the enteropeptidase cleave site engineered between the carrier protein and the target sequence. Enteropeptidase is secreted as a zymogen, and it was thought that trypsin activates the enzyme, although this another enzyme, duodenase, has been proposed to fill this function in cattle. If there is a human ortholog for duodenase it has yet to be identified at this point. Based on the enteropeptidase cleavage specificity it seems unlikely that enteropeptidase autoactivates. The activation of trypsin is a key step in digestion, and leads to a cascade of enzyme activation in the intestines. The membrane attached enteropeptidase is cleaved at the start of the catalytic domain to yield the active form, the light chain. The light chain is held attached to the heavy chain by a disulfide bond. The 1019 amino acid enteropeptidase sequence encodes a protein with predicted mass of 112.9 kDa and a pI of 4.72. A significant amount of glycosylation increases the apparent molecular weight to 150 kDa, and when reduced the heavy and light chaind run separatly. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species. FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for approximately 12 months at -20C.
