Description
RP1-Serpin-A1 is a polyclonal antibody made to the serine proteinase inhibitor Alpha-1-antitrypsin (Serpin-A1). The antibody is made to a synthetic peptide based on the aminoterminal end of mature human serpin-A1. 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-A1, also known as alpha-1-antitrypsin (alpha-1-antitrypsin, alpha-1 protease inhibitor, alpha-1-antiproteinase, AAT, PI) is a serine proteinase inhibitor (SERPIN), and the archetype of the A-clade of structurally related serpins. Serpin A1 is produced by the liver, and is abundant in plasma; usually found at 1-2 mg/ml. Serpin A1 is an acute phase protein, and plasma concentrations for serpin A1 are elevated several fold in acute phase reactions. Serpin A1 is found throughout the body, but the principle organ of action is the lung, where it acts to reign in neutrophil elastase. A number of point mutations lead to decreased activity or expression of serpin A1, and have been associated with emphysemas and liver cirrhosis. Hereditary alpha-1-antitrypsin deficiency affects approximately 1:2,500 in northern Europe, and considered one of the most common hereditary disorders globally. Clinical evaluation of sera from hereditary alpha-1-antitrypsin deficiency patients was initially done by acid starch gel electrophoresis, and the different isoforms classified by their relative mobility: F (fast), M (medium), S (slow) and Z (most cathodal). The mode of action of serpin A1 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A1 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. Serpin A1 can also relieve the stress somewhat by polymerizing, and the homooligomers are inactivated, causing a protease imbalance and tissue damage. The methionine in the RCL is in the P1 position, and oxidation of the methionine by tobacco smoking has been linked to emphysema. The full length serpin-A1 sequence encodes a 418 amino acid protein, with a predicted mass of 46.7 kDa, and a pI of 5.24. 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 at -20C.
Description
RP2-Serpin-A1 is a polyclonal antibody made to the serine proteinase inhibitor Alpha-1-antitrypsin (Serpin-A1). The antibody is made to a synthetic peptide based on the region from the end of helix 4 to the beginning of helix 5 of human serpin-A1. 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-A1, also known as alpha-1-antitrypsin (alpha-1-antitrypsin, alpha-1 protease inhibitor, alpha-1-antiproteinase, AAT, PI) is a serine proteinase inhibitor (SERPIN), and the archetype of the A-clade of structurally related serpins. Serpin A1 is produced by the liver, and is abundant in plasma; usually found at 1-2 mg/ml. Serpin A1 is an acute phase protein, and plasma concentrations for serpin A1 are elevated several fold in acute phase reactions. Serpin A1 is found throughout the body, but the principle organ of action is the lung, where it acts to reign in neutrophil elastase. A number of point mutations lead to decreased activity or expression of serpin A1, and have been associated with emphysemas and liver cirrhosis. Hereditary alpha-1-antitrypsin deficiency affects approximately 1:2,500 in northern Europe, and considered one of the most common hereditary disorders globally. Clinical evaluation of sera from hereditary alpha-1-antitrypsin deficiency patients was initially done by acid starch gel electrophoresis, and the different isoforms classified by their relative mobility: F (fast), M (medium), S (slow) and Z (most cathodal). The mode of action of serpin A1 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A1 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. Serpin A1 can also relieve the stress somewhat by polymerizing, and the homooligomers are inactivated, causing a protease imbalance and tissue damage. The methionine in the RCL is in the P1 position, and oxidation of the methionine by tobacco smoking has been linked to emphysema. The full length serpin-A1 sequence encodes a 418 amino acid protein, with a predicted mass of 46.7 kDa, and a pI of 5.24. 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 at -20C.
Description
RP3-Serpin-A1 is a polyclonal antibody made to the serine proteinase inhibitor Alpha-1-antitrypsin (Serpin-A1). The antibody is made to a synthetic peptide based on the region from the start of helix 7 through helix 8 of human serpin-A1. 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-A1, also known as alpha-1-antitrypsin (alpha-1-antitrypsin, alpha-1 protease inhibitor, alpha-1-antiproteinase, AAT, PI) is a serine proteinase inhibitor (SERPIN), and the archetype of the A-clade of structurally related serpins. Serpin A1 is produced by the liver, and is abundant in plasma; usually found at 1-2 mg/ml. Serpin A1 is an acute phase protein, and plasma concentrations for serpin A1 are elevated several fold in acute phase reactions. Serpin A1 is found throughout the body, but the principle organ of action is the lung, where it acts to reign in neutrophil elastase. A number of point mutations lead to decreased activity or expression of serpin A1, and have been associated with emphysemas and liver cirrhosis. Hereditary alpha-1-antitrypsin deficiency affects approximately 1:2,500 in northern Europe, and considered one of the most common hereditary disorders globally. Clinical evaluation of sera from hereditary alpha-1-antitrypsin deficiency patients was initially done by acid starch gel electrophoresis, and the different isoforms classified by their relative mobility: F (fast), M (medium), S (slow) and Z (most cathodal). The mode of action of serpin A1 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A1 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. Serpin A1 can also relieve the stress somewhat by polymerizing, and the homooligomers are inactivated, causing a protease imbalance and tissue damage. The methionine in the RCL is in the P1 position, and oxidation of the methionine by tobacco smoking has been linked to emphysema. The full length serpin-A1 sequence encodes a 418 amino acid protein, with a predicted mass of 46.7 kDa, and a pI of 5.24. 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 at -20C.
