Description
RP1-Serpin-A3 is a polyclonal antibody made to the serine proteinase inhibitor Alpha-1-antichymotrypsin (Serpin-A3). The antibody is made to a synthetic peptide based on the aminoterminal end of mature human serpin-A3. 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-A3, also known as alpha-1-antichymotrypsin (alpha-1-antichymotrypsin, growth inhibiting protein 24) is a serine proteinase inhibitor (SERPIN). Serpin A3 is produced by the liver, and is abundant in plasma; usually found at around 0.5 mg/ml. Serpin A3 is an acute phase protein, and plasma concentrations for serpin A3 are elevated several fold in acute phase reactions. Interleukin-1 is known to stimulate serpin-A3 production, and in astrocytes serpin A3 production is thought to require activator protein-1. The production of serpin A3 by glial cells is considered a source of neurological damage in some cases, leading to Tau hyperphosphorylation, neurofibrillary tangles, resulting in Alzheimer's disease. Different reports suggest that serpin A3 actually neutralizes fibrillar aggregation and cytotoxicity of the Abeta-peptide. Most references term serpin A3 an inflammatory player, in line with the status as an acute phase protein. Other 'serphinopathogies' are caused by serpin misfolding, and point mutations that allow oligimers of serpins to form. Glycosylation patterns on serpin A3 are reportedly altered in ovarian cancer, and serpin A3 levels are thought to be elevated in prostate cancer. Serpin A3 has also been reported to be required for the regulation of leukocyte protease release during inflammatory response. A polymorphism in serpin A3 is proposed to be a risk factor in some populations, although it has been ruled out in others. In skin wound healing, serpin A3 is thought to inhibit the proteolytic activation of MMP-9, but not inhibited by serpin A1. Serpin A3 is found throughout the body, but the principle organ of action is the lung, where it acts to reign in cathepsin G. In addition, serpin A3 binds to prostate specific antigen (PSA), and the dominant PSA-inhibitor complex found in sera is the PSA-serpin A3 complex. The mode of action of serpin A3 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A3 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 A3 can also relieve the stress somewhat by polymerizing, and the homooligomers are inactivated, causing a protease imbalance and tissue damage. The full length serpin-A3 sequence encodes a 423 amino acid protein, with a predicted mass of 47.7 kDa, and a pI of 5.2. 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-A3 is a polyclonal antibody made to the serine proteinase inhibitor Alpha-1-antichymotrypsin (Serpin-A3). The antibody is made to a synthetic peptide based on the helix 4 to helix 5 region of human serpin-A3. 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-A3, also known as alpha-1-antichymotrypsin (alpha-1-antichymotrypsin, growth inhibiting protein 24) is a serine proteinase inhibitor (SERPIN). Serpin A3 is produced by the liver, and is abundant in plasma; usually found at around 0.5 mg/ml. Serpin A3 is an acute phase protein, and plasma concentrations for serpin A3 are elevated several fold in acute phase reactions. Interleukin-1 is known to stimulate serpin-A3 production, and in astrocytes serpin A3 production is thought to require activator protein-1. The production of serpin A3 by glial cells is considered a source of neurological damage in some cases, leading to Tau hyperphosphorylation, neurofibrillary tangles, resulting in Alzheimer's disease. Different reports suggest that serpin A3 actually neutralizes fibrillar aggregation and cytotoxicity of the Abeta-peptide. Most references term serpin A3 an inflammatory player, in line with the status as an acute phase protein. Other 'serphinopathogies' are caused by serpin misfolding, and point mutations that allow oligimers of serpins to form. Glycosylation patterns on serpin A3 are reportedly altered in ovarian cancer, and serpin A3 levels are thought to be elevated in prostate cancer. Serpin A3 has also been reported to be required for the regulation of leukocyte protease release during inflammatory response. A polymorphism in serpin A3 is proposed to be a risk factor in some populations, although it has been ruled out in others. In skin wound healing, serpin A3 is thought to inhibit the proteolytic activation of MMP-9, but not inhibited by serpin A1. Serpin A3 is found throughout the body, but the principle organ of action is the lung, where it acts to reign in cathepsin G. In addition, serpin A3 binds to prostate specific antigen (PSA), and the dominant PSA-inhibitor complex found in sera is the PSA-serpin A3 complex. The mode of action of serpin A3 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A3 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 A3 can also relieve the stress somewhat by polymerizing, and the homooligomers are inactivated, causing a protease imbalance and tissue damage. The full length serpin-A3 sequence encodes a 423 amino acid protein, with a predicted mass of 47.7 kDa, and a pI of 5.2. 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-A3 is a polyclonal antibody made to the serine proteinase inhibitor Alpha-1-antichymotrypsin (Serpin-A3). The antibody is made to a synthetic peptide based on the helix 7 to helix 8 region of human serpin-A3. 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-A3, also known as alpha-1-antichymotrypsin (alpha-1-antichymotrypsin, growth inhibiting protein 24) is a serine proteinase inhibitor (SERPIN). Serpin A3 is produced by the liver, and is abundant in plasma; usually found at around 0.5 mg/ml. Serpin A3 is an acute phase protein, and plasma concentrations for serpin A3 are elevated several fold in acute phase reactions. Interleukin-1 is known to stimulate serpin-A3 production, and in astrocytes serpin A3 production is thought to require activator protein-1. The production of serpin A3 by glial cells is considered a source of neurological damage in some cases, leading to Tau hyperphosphorylation, neurofibrillary tangles, resulting in Alzheimer's disease. Different reports suggest that serpin A3 actually neutralizes fibrillar aggregation and cytotoxicity of the Abeta-peptide. Most references term serpin A3 an inflammatory player, in line with the status as an acute phase protein. Other 'serphinopathogies' are caused by serpin misfolding, and point mutations that allow oligimers of serpins to form. Glycosylation patterns on serpin A3 are reportedly altered in ovarian cancer, and serpin A3 levels are thought to be elevated in prostate cancer. Serpin A3 has also been reported to be required for the regulation of leukocyte protease release during inflammatory response. A polymorphism in serpin A3 is proposed to be a risk factor in some populations, although it has been ruled out in others. In skin wound healing, serpin A3 is thought to inhibit the proteolytic activation of MMP-9, but not inhibited by serpin A1. Serpin A3 is found throughout the body, but the principle organ of action is the lung, where it acts to reign in cathepsin G. In addition, serpin A3 binds to prostate specific antigen (PSA), and the dominant PSA-inhibitor complex found in sera is the PSA-serpin A3 complex. The mode of action of serpin A3 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A3 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 A3 can also relieve the stress somewhat by polymerizing, and the homooligomers are inactivated, causing a protease imbalance and tissue damage. The full length serpin-A3 sequence encodes a 423 amino acid protein, with a predicted mass of 47.7 kDa, and a pI of 5.2. 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.
