Description
RP1-Serpin-A10 is a polyclonal antibody made to the serine proteinase inhibitor Protein Z-dependent protease inhibitor (Serpin-A10). The antibody is made to a synthetic peptide based on the aminoterminal end of mature human serpin-A10. 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
Serpin-A10 is a serine proteinase inhibitor found in plasma at concentrations of approximately 3.8 ug/ml. In circulation Serpin-A10 is primarily bound to protein-Z, a vitamin-K-dependent catalytically inactive serine proteinase found at approximately 2.6 ug/ml in serum. The protein-Z binding acts as a cofactor for serpin-A10, and the combination of protein-Z, calcium and phospholipids makes serpin-A10 maximally active. Factor-Xa is thought to be the principle target of serpin-A10, but the inhibition is overturned by factor-Va. In addition to factor-Xa, serpin-A10 is thought to inhibit factor-IXa, and cleavage is stimulated by but not dependent on protein-Z. Serpin-A10 is an A-clade serpin, the archetype of which is alpha-1 antitrypsin. The mode of action of most A-clade serpins involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of A-clade serpins is in a stressed state, and cleavage converts the molecule to a relaxed, more energetically favorable state. The structural change traps the proteinase that cleaves the reactive center loop (RCL), like a mousetrap. Factor-Xa is also inhibited by serpin-C1 (antithrombin) in the typical mousetrap fashion. The inhibition of factor-Xa by serpin-A10 is not thought to form an irreversible complex, as is the case with serpin-C1. Rather, serpin-A10/Factor-Xa complexes are thought to be reversible, more like the cotisol and thyroxin-binding serpins, serpins A6 and A7. Several nonsense and stop-codon mutations have been reported for serpin-A10, and associations have been suggested for venous thrombosis. The full length serpin-A10 sequence codes for a 444 amino acid protein, with a predicted mass of 50.7 kDa and a pI of 8.4. The basic pI may explain the association with the plasma membrane, where serpin-A10 may be associated with GAGs. A longer sequence of 484 amino acids is reported, with a 44 amino acid extension on the aminoterminus, and if expressed this would have a predicted mass of 55.1 kDa, and a pI of 7.5. A recommended starting concentration for Western blots is 1:1000 when using colorimetric substrates such as BCIP/NBT, and 1:5000 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-Serpin-A10 is a polyclonal antibody made to the serine proteinase inhibitor Protein Z-dependent protease inhibitor (Serpin-A10). The antibody is made to a synthetic peptide based on Helix 4 to Helix 5 of human serpin-A10. 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
Serpin-A10 is a serine proteinase inhibitor found in plasma at concentrations of approximately 3.8 ug/ml. In circulation Serpin-A10 is primarily bound to protein-Z, a vitamin-K-dependent catalytically inactive serine proteinase found at approximately 2.6 ug/ml in serum. The protein-Z binding acts as a cofactor for serpin-A10, and the combination of protein-Z, calcium and phospholipids makes serpin-A10 maximally active. Factor-Xa is thought to be the principle target of serpin-A10, but the inhibition is overturned by factor-Va. In addition to factor-Xa, serpin-A10 is thought to inhibit factor-IXa, and cleavage is stimulated by but not dependent on protein-Z. Serpin-A10 is an A-clade serpin, the archetype of which is alpha-1 antitrypsin. The mode of action of most A-clade serpins involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of A-clade serpins is in a stressed state, and cleavage converts the molecule to a relaxed, more energetically favorable state. The structural change traps the proteinase that cleaves the reactive center loop (RCL), like a mousetrap. Factor-Xa is also inhibited by serpin-C1 (antithrombin) in the typical mousetrap fashion. The inhibition of factor-Xa by serpin-A10 is not thought to form an irreversible complex, as is the case with serpin-C1. Rather, serpin-A10/Factor-Xa complexes are thought to be reversible, more like the cotisol and thyroxin-binding serpins, serpins A6 and A7. Several nonsense and stop-codon mutations have been reported for serpin-A10, and associations have been suggested for venous thrombosis. The full length serpin-A10 sequence codes for a 444 amino acid protein, with a predicted mass of 50.7 kDa and a pI of 8.4. The basic pI may explain the association with the plasma membrane, where serpin-A10 may be associated with GAGs. A longer sequence of 484 amino acids is reported, with a 44 amino acid extension on the aminoterminus, and if expressed this would have a predicted mass of 55.1 kDa, and a pI of 7.5. A recommended starting concentration for Western blots is 1:1000 when using colorimetric substrates such as BCIP/NBT, and 1:5000 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-Serpin-A10 is a polyclonal antibody made to the serine proteinase inhibitor Protein Z-dependent protease inhibitor (Serpin-A10). The antibody is made to a synthetic peptide based on Helix 7 to Helix 8 of human serpin-A10. 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
Serpin-A10 is a serine proteinase inhibitor found in plasma at concentrations of approximately 3.8 ug/ml. In circulation Serpin-A10 is primarily bound to protein-Z, a vitamin-K-dependent catalytically inactive serine proteinase found at approximately 2.6 ug/ml in serum. The protein-Z binding acts as a cofactor for serpin-A10, and the combination of protein-Z, calcium and phospholipids makes serpin-A10 maximally active. Factor-Xa is thought to be the principle target of serpin-A10, but the inhibition is overturned by factor-Va. In addition to factor-Xa, serpin-A10 is thought to inhibit factor-IXa, and cleavage is stimulated by but not dependent on protein-Z. Serpin-A10 is an A-clade serpin, the archetype of which is alpha-1 antitrypsin. The mode of action of most A-clade serpins involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of A-clade serpins is in a stressed state, and cleavage converts the molecule to a relaxed, more energetically favorable state. The structural change traps the proteinase that cleaves the reactive center loop (RCL), like a mousetrap. Factor-Xa is also inhibited by serpin-C1 (antithrombin) in the typical mousetrap fashion. The inhibition of factor-Xa by serpin-A10 is not thought to form an irreversible complex, as is the case with serpin-C1. Rather, serpin-A10/Factor-Xa complexes are thought to be reversible, more like the cotisol and thyroxin-binding serpins, serpins A6 and A7. Several nonsense and stop-codon mutations have been reported for serpin-A10, and associations have been suggested for venous thrombosis. The full length serpin-A10 sequence codes for a 444 amino acid protein, with a predicted mass of 50.7 kDa and a pI of 8.4. The basic pI may explain the association with the plasma membrane, where serpin-A10 may be associated with GAGs. A longer sequence of 484 amino acids is reported, with a 44 amino acid extension on the aminoterminus, and if expressed this would have a predicted mass of 55.1 kDa, and a pI of 7.5. A recommended starting concentration for Western blots is 1:1000 when using colorimetric substrates such as BCIP/NBT, and 1:5000 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.
