Description
RP1-Serpin-A5 is a polyclonal antibody made to the serine proteinase inhibitor protein C-inhibitor (Serpin-A5). The antibody is made to a synthetic peptide based on the aminoterminal end of mature human serpin-A5. 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-A5, also known as Protein-C Inhibitor, PCI, Plasminogen Activator Inhibitor-3, PAI-3 and Acrosomal Serine Protease Inhibitor is a serpin of the A clade, the archetype of which is alpha-1 antitrypsin. Best known as PCI, serpin-A5 is produced principally by the liver, and by the kidney, skin keratinocytes, and a number of other tissues. In the mouse serpin-A5 production is limited to genital tract tissues, indicating a more limited role in fertilization. In humans, serpin-A5 is found in serum, urine, tears and seminal fluid. The seminal plasma higher concentration is much higher than other bodily fluids, and serpin-A5 is thought to disable damaged sperm and help control local proteolysis. Inactivation of serpin-A5 leads to decreased fertility. Serpin-A5 forms a complex with kallikrein-3 in seminal plasma, but the chief target there is thought to be acrosin, although kallikrein-2 is also found in seminal fluid, and serpin-A5 was identified as a chief substrate by phage display. Heparin and other polyanion binding increases the serpin-A5 efficacy against acrosin approximately 100-fold and calcium binding is required for maximal inhibition. The heparin binding also increases serpin-A5 efficacy against activated protein C, chymotrypsin, Factor Xa, Plasma Kallikrein, thrombin and uPA, although it decreases efficacy against kallikrein-1. The thrombin inhibition is greatly increased when thrombomodulin binds to thrombin. Serpin-A5 has also been shown to inhibit matriptase-3, and over expression of serpin-A5 increases cell adhesion and motility of MDA-MB-435 breast cancer cells in culture. Hepatocyte Growth Factor Activator (HGFA) is also reported to be inhibited by serpin-A5 and inhibition was increased by heparin. The mode of action of serpin A5 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A5 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. The wide range of enzyme targets for serpin-A5 is thought to be due to the relatively long and flexible RCL. Heparin binds to serpin-A5 at two sites, and to the target serine proteinase, apparently stabilizing the complex. The Serpin-A5 sequence codes for a 406 amino acid protein, with a predicted mass of 45.7 kDa and a pI of 9.3. The basic pI helps drive the interaction with heparin and glycosamino glycans (GAGs). 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-A5 is a polyclonal antibody made to the serine proteinase inhibitor protein C-inhibitor (Serpin-A5). The antibody is made to a synthetic peptide based on Helix 4 to Helix 5 of human serpin-A5. 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-A5, also known as Protein-C Inhibitor, PCI, Plasminogen Activator Inhibitor-3, PAI-3 and Acrosomal Serine Protease Inhibitor is a serpin of the A clade, the archetype of which is alpha-1 antitrypsin. Best known as PCI, serpin-A5 is produced principally by the liver, and by the kidney, skin keratinocytes, and a number of other tissues. In the mouse serpin-A5 production is limited to genital tract tissues, indicating a more limited role in fertilization. In humans, serpin-A5 is found in serum, urine, tears and seminal fluid. The seminal plasma higher concentration is much higher than other bodily fluids, and serpin-A5 is thought to disable damaged sperm and help control local proteolysis. Inactivation of serpin-A5 leads to decreased fertility. Serpin-A5 forms a complex with kallikrein-3 in seminal plasma, but the chief target there is thought to be acrosin, although kallikrein-2 is also found in seminal fluid, and serpin-A5 was identified as a chief substrate by phage display. Heparin and other polyanion binding increases the serpin-A5 efficacy against acrosin approximately 100-fold and calcium binding is required for maximal inhibition. The heparin binding also increases serpin-A5 efficacy against activated protein C, chymotrypsin, Factor Xa, Plasma Kallikrein, thrombin and uPA, although it decreases efficacy against kallikrein-1. The thrombin inhibition is greatly increased when thrombomodulin binds to thrombin. Serpin-A5 has also been shown to inhibit matriptase-3, and over expression of serpin-A5 increases cell adhesion and motility of MDA-MB-435 breast cancer cells in culture. Hepatocyte Growth Factor Activator (HGFA) is also reported to be inhibited by serpin-A5 and inhibition was increased by heparin. The mode of action of serpin A5 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A5 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. The wide range of enzyme targets for serpin-A5 is thought to be due to the relatively long and flexible RCL. Heparin binds to serpin-A5 at two sites, and to the target serine proteinase, apparently stabilizing the complex. The Serpin-A5 sequence codes for a 406 amino acid protein, with a predicted mass of 45.7 kDa and a pI of 9.3. The basic pI helps drive the interaction with heparin and glycosamino glycans (GAGs). 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-A5 is a polyclonal antibody made to the serine proteinase inhibitor protein C-inhibitor (Serpin-A5). The antibody is made to a synthetic peptide based on the second heparin binding site of human serpin-A5. 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-A5, also known as Protein-C Inhibitor, PCI, Plasminogen Activator Inhibitor-3, PAI-3 and Acrosomal Serine Protease Inhibitor is a serpin of the A clade, the archetype of which is alpha-1 antitrypsin. Best known as PCI, serpin-A5 is produced principally by the liver, and by the kidney, skin keratinocytes, and a number of other tissues. In the mouse serpin-A5 production is limited to genital tract tissues, indicating a more limited role in fertilization. In humans, serpin-A5 is found in serum, urine, tears and seminal fluid. The seminal plasma higher concentration is much higher than other bodily fluids, and serpin-A5 is thought to disable damaged sperm and help control local proteolysis. Inactivation of serpin-A5 leads to decreased fertility. Serpin-A5 forms a complex with kallikrein-3 in seminal plasma, but the chief target there is thought to be acrosin, although kallikrein-2 is also found in seminal fluid, and serpin-A5 was identified as a chief substrate by phage display. Heparin and other polyanion binding increases the serpin-A5 efficacy against acrosin approximately 100-fold and calcium binding is required for maximal inhibition. The heparin binding also increases serpin-A5 efficacy against activated protein C, chymotrypsin, Factor Xa, Plasma Kallikrein, thrombin and uPA, although it decreases efficacy against kallikrein-1. The thrombin inhibition is greatly increased when thrombomodulin binds to thrombin. Serpin-A5 has also been shown to inhibit matriptase-3, and over expression of serpin-A5 increases cell adhesion and motility of MDA-MB-435 breast cancer cells in culture. Hepatocyte Growth Factor Activator (HGFA) is also reported to be inhibited by serpin-A5 and inhibition was increased by heparin. The mode of action of serpin A5 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A5 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. The wide range of enzyme targets for serpin-A5 is thought to be due to the relatively long and flexible RCL. Heparin binds to serpin-A5 at two sites, and to the target serine proteinase, apparently stabilizing the complex. The Serpin-A5 sequence codes for a 406 amino acid protein, with a predicted mass of 45.7 kDa and a pI of 9.3. The basic pI helps drive the interaction with heparin and glycosamino glycans (GAGs). 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.
