Description
RP1-Signal Peptide Peptidase is a rabbit polyclonal antibody made to the aspartic proteinase Signal Peptide Peptidase. The antibody is made to a synthetic peptide based on the aminoterminal end of human Signal Peptide Peptidase. 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
Signal Peptide Peptidase (Minor histocomaptibility antigen H13, Presenilin-Like protein-3, hIMP1, intermembrane proteinase-1) is a multi-pass transmembrane aspartic proteinase known principally for its role in degrading cleaved signal peptides. The overall topology of SPP is similar to the presenilins, although the primary sequence homology is low. Signal peptide Peptidase is thought to be a 7-pass transmembrane proteinase. The 377 amino acid form of SPP has the amino end presented to the ER lumen, followed by a membrane pass, a cytosolic loop of 24 residues, 2 more membrane passes, another cytosolic loop of 88 residues, another membrane pass, a luminal loop of 26 residues, another membrane pass, a cytosolic loop of 14 residues, 2 more membrane passes, and a carboxyterminal tail of 40 residues presented to the cytosol. Presenilins have the loops all presented to the cytoplasmic side, and the substrates enter the membrane from opposite orientations. The catalytic aspartic acids are found on the fourth and fifth TM domains in SPP. This model is evolving, since there is at present no crystal structure, but it seems that unlike the presenilins, SPP does not require a complex of accessory molecules for activity. In addition to cleaving and clearing signal peptides from the membrane, SPP also generates minor histocompatability peptides that are trafficked to the cell surface, and are used by surveiling NK cells to indicate cell health. Presentation of foreign peptides, or a lack of a normal flora of peptides indicated cell infection or damage, and the cells are eliminated by NK cells. The viral hepatitis C infection process is successful in part because the virus hijacks the SPP system, keeping it from presenting a warning peptide to the cell surface. The growing family of intermembrane proteinases includes the presenilins, SPP, SPPL2A, SPPL2B, SPPL2C, TPP and Rhomboid. Of these, the presenilins have received the bulk of the attention, and less is known about the other family members. Several different splice variants of Signal peptide peptidase have been identified, all with different truncations of the carboxyterminal end. The 143 amino acid form terminated before the second catalytic residue, and is unlikely to be active. The 393 and 426 amino acid forms have longer carboxyterminal ends than the 377 archtype sequence, but little is known about the specific activity of the different isoforms. 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 12 months at -20��C.
Description
RP2-Signal Peptide Peptidase is a rabbit polyclonal antibody made to the aspartic proteinase Signal Peptide Peptidase. The antibody is made to a synthetic peptide based on the second cytoplasmic loop of human Signal Peptide Peptidase. 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
Signal Peptide Peptidase (Minor histocomaptibility antigen H13, Presenilin-Like protein-3, hIMP1, intermembrane proteinase-1) is a multi-pass transmembrane aspartic proteinase known principally for its role in degrading cleaved signal peptides. The overall topology of SPP is similar to the presenilins, although the primary sequence homology is low. Signal peptide Peptidase is thought to be a 7-pass transmembrane proteinase. The 377 amino acid form of SPP has the amino end presented to the ER lumen, followed by a membrane pass, a cytosolic loop of 24 residues, 2 more membrane passes, another cytosolic loop of 88 residues, another membrane pass, a luminal loop of 26 residues, another membrane pass, a cytosolic loop of 14 residues, 2 more membrane passes, and a carboxyterminal tail of 40 residues presented to the cytosol. Presenilins have the loops all presented to the cytoplasmic side, and the substrates enter the membrane from opposite orientations. The catalytic aspartic acids are found on the fourth and fifth TM domains in SPP. This model is evolving, since there is at present no crystal structure, but it seems that unlike the presenilins, SPP does not require a complex of accessory molecules for activity. In addition to cleaving and clearing signal peptides from the membrane, SPP also generates minor histocompatability peptides that are trafficked to the cell surface, and are used by surveiling NK cells to indicate cell health. Presentation of foreign peptides, or a lack of a normal flora of peptides indicated cell infection or damage, and the cells are eliminated by NK cells. The viral hepatitis C infection process is successful in part because the virus hijacks the SPP system, keeping it from presenting a warning peptide to the cell surface. The growing family of intermembrane proteinases includes the presenilins, SPP, SPPL2A, SPPL2B, SPPL2C, TPP and Rhomboid. Of these, the presenilins have received the bulk of the attention, and less is known about the other family members. Several different splice variants of Signal peptide peptidase have been identified, all with different truncations of the carboxyterminal end. The 143 amino acid form terminated before the second catalytic residue, and is unlikely to be active. The 393 and 426 amino acid forms have longer carboxyterminal ends than the 377 archtype sequence, but little is known about the specific activity of the different isoforms. 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 12 months at -20��C.
Description
RP3-Signal Peptide Peptidase is a rabbit polyclonal antibody made to the aspartic proteinase Signal Peptide Peptidase. The antibody is made to a synthetic peptide based on the carboxytermianl end of human Signal Peptide Peptidase. 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
Signal Peptide Peptidase (Minor histocomaptibility antigen H13, Presenilin-Like protein-3, hIMP1, intermembrane proteinase-1) is a multi-pass transmembrane aspartic proteinase known principally for its role in degrading cleaved signal peptides. The overall topology of SPP is similar to the presenilins, although the primary sequence homology is low. Signal peptide Peptidase is thought to be a 7-pass transmembrane proteinase. The 377 amino acid form of SPP has the amino end presented to the ER lumen, followed by a membrane pass, a cytosolic loop of 24 residues, 2 more membrane passes, another cytosolic loop of 88 residues, another membrane pass, a luminal loop of 26 residues, another membrane pass, a cytosolic loop of 14 residues, 2 more membrane passes, and a carboxyterminal tail of 40 residues presented to the cytosol. Presenilins have the loops all presented to the cytoplasmic side, and the substrates enter the membrane from opposite orientations. The catalytic aspartic acids are found on the fourth and fifth TM domains in SPP. This model is evolving, since there is at present no crystal structure, but it seems that unlike the presenilins, SPP does not require a complex of accessory molecules for activity. In addition to cleaving and clearing signal peptides from the membrane, SPP also generates minor histocompatability peptides that are trafficked to the cell surface, and are used by surveiling NK cells to indicate cell health. Presentation of foreign peptides, or a lack of a normal flora of peptides indicated cell infection or damage, and the cells are eliminated by NK cells. The viral hepatitis C infection process is successful in part because the virus hijacks the SPP system, keeping it from presenting a warning peptide to the cell surface. The growing family of intermembrane proteinases includes the presenilins, SPP, SPPL2A, SPPL2B, SPPL2C, TPP and Rhomboid. Of these, the presenilins have received the bulk of the attention, and less is known about the other family members. Several different splice variants of Signal peptide peptidase have been identified, all with different truncations of the carboxyterminal end. The 143 amino acid form terminated before the second catalytic residue, and is unlikely to be active. The 393 and 426 amino acid forms have longer carboxyterminal ends than the 377 archtype sequence, but little is known about the specific activity of the different isoforms. 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 12 months at -20��C.
