Description
RP1-Serpin-A8 is a polyclonal antibody made to the serine proteinase inhibitor thyroxine-binding globulin (Serpin-A8). The antibody is made to a synthetic peptide based on the aminoterminal end of mature human serpin-A8. 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-A8, also known as angiotensinogen (AGT) is a serpin of the A clade, the archetype of which is alpha-1 antitrypsin. Best known as angiotensinogen, serpin-A8 is produced principally by the liver, but has also been described in brain, heart, and other tissues. Serpin-A8 is the precursor form of angiotensin-I, produced by the renin cleavage of the 10 amino terminal residues of the mature protein. Angiotensin-I is further processed by proteolytic cleavage to shorter forms with differing effects. Angiotensin is a potent vasoconstrictor, and the renin-angiotensin system largely controls blood pressure, as well as many other physiological functions. Most of the research on serpin-A8 revolves around the aminotermional 10 residues following the signal sequence, and very little on the serpin activities. The RCL of Serpin-A8 differs somewhat from the other A-clade serpins, and is not thought to go through the dramatic 'stressed' to 'relaxed' change that the other A-clade serpins exhibit after RCL cleavage. 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. Although there is little evidence for serpin-A8 proteinase inhibition, serpin-A8 has been identified in a high molecular weight complex with pregnancy-associated protein and eosinophil basic protein, and the complex is significantly elevated during pregnancy. Mutations in serpin-A8 that lead to abnormal glycosylation, and altered turnover rates are described, as well as mutations that effect the rennin cleavage site, and decrease angiotensin production. Other mutations in the body of serpin-A8 also are reported to effect angiotensin production, although the mechanisms are less clear. The Serpin-A8 sequence codes for a 485 amino acid protein, with a predicted mass of 53.2 kDa and a pI of 5.8. The acidic pI is in contrast to the basic pI of the heparin-binding serpins, and in line with serum proteins found in circulation. 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 at -20C.
Description
RP2-Serpin-A8 is a polyclonal antibody made to the serine proteinase inhibitor thyroxine-binding globulin (Serpin-A8). The antibody is made to a synthetic peptide based on Helix 4 to Helix 5 of human serpin-A8. 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-A8, also known as angiotensinogen (AGT) is a serpin of the A clade, the archetype of which is alpha-1 antitrypsin. Best known as angiotensinogen, serpin-A8 is produced principally by the liver, but has also been described in brain, heart, and other tissues. Serpin-A8 is the precursor form of angiotensin-I, produced by the renin cleavage of the 10 amino terminal residues of the mature protein. Angiotensin-I is further processed by proteolytic cleavage to shorter forms with differing effects. Angiotensin is a potent vasoconstrictor, and the renin-angiotensin system largely controls blood pressure, as well as many other physiological functions. Most of the research on serpin-A8 revolves around the aminotermional 10 residues following the signal sequence, and very little on the serpin activities. The RCL of Serpin-A8 differs somewhat from the other A-clade serpins, and is not thought to go through the dramatic 'stressed' to 'relaxed' change that the other A-clade serpins exhibit after RCL cleavage. 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. Although there is little evidence for serpin-A8 proteinase inhibition, serpin-A8 has been identified in a high molecular weight complex with pregnancy-associated protein and eosinophil basic protein, and the complex is significantly elevated during pregnancy. Mutations in serpin-A8 that lead to abnormal glycosylation, and altered turnover rates are described, as well as mutations that effect the rennin cleavage site, and decrease angiotensin production. Other mutations in the body of serpin-A8 also are reported to effect angiotensin production, although the mechanisms are less clear. The Serpin-A8 sequence codes for a 485 amino acid protein, with a predicted mass of 53.2 kDa and a pI of 5.8. The acidic pI is in contrast to the basic pI of the heparin-binding serpins, and in line with serum proteins found in circulation. 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 at -20C.
Description
RP3-Serpin-A8 is a polyclonal antibody made to the serine proteinase inhibitor thyroxine-binding globulin (Serpin-A8). The antibody is made to a synthetic peptide based on Helix 7 to Helix 8 of human serpin-A8. 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-A8, also known as angiotensinogen (AGT) is a serpin of the A clade, the archetype of which is alpha-1 antitrypsin. Best known as angiotensinogen, serpin-A8 is produced principally by the liver, but has also been described in brain, heart, and other tissues. Serpin-A8 is the precursor form of angiotensin-I, produced by the renin cleavage of the 10 amino terminal residues of the mature protein. Angiotensin-I is further processed by proteolytic cleavage to shorter forms with differing effects. Angiotensin is a potent vasoconstrictor, and the renin-angiotensin system largely controls blood pressure, as well as many other physiological functions. Most of the research on serpin-A8 revolves around the aminotermional 10 residues following the signal sequence, and very little on the serpin activities. The RCL of Serpin-A8 differs somewhat from the other A-clade serpins, and is not thought to go through the dramatic 'stressed' to 'relaxed' change that the other A-clade serpins exhibit after RCL cleavage. 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. Although there is little evidence for serpin-A8 proteinase inhibition, serpin-A8 has been identified in a high molecular weight complex with pregnancy-associated protein and eosinophil basic protein, and the complex is significantly elevated during pregnancy. Mutations in serpin-A8 that lead to abnormal glycosylation, and altered turnover rates are described, as well as mutations that effect the rennin cleavage site, and decrease angiotensin production. Other mutations in the body of serpin-A8 also are reported to effect angiotensin production, although the mechanisms are less clear. The Serpin-A8 sequence codes for a 485 amino acid protein, with a predicted mass of 53.2 kDa and a pI of 5.8. The acidic pI is in contrast to the basic pI of the heparin-binding serpins, and in line with serum proteins found in circulation. 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 at -20C.
