Description
RP1-Serpin-A4 is a polyclonal antibody made to the serine proteinase inhibitor kallistatin (Serpin-A4). The antibody is made to a synthetic peptide based on the aminoterminal end of mature human serpin-A4. 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-A4, also known as Kallistatin and PI-4 was first described as kallikrein-binding protein (KBP), a protein found in complex with tissue kallikrein in plasma. The complex was seen as a 92 kDa heterodimer that was stable to heat and SDS denaturation, although 0.1% SDS would prevent the formation of the complex. Serpin A4 is a serpin of the A clade, the archetype of which is alpha-1 antitrypsin. Serpin-A4 levels were found to be 5-10 times lower in spontaneously hypertensive rats, and increasing the serpin-A4 in these rats returns them to a normotensive state. Upregulating serpin-A4 in wild type mice makes them hypotensive. Serpin-A4 has also been reported to be elevated in muscle damage, and decreased in diabetic retinopathy. Serpin-A4 is reportedly cleaved by cathepsin-D at the reactive center loop, the bait area that serpins have in common. Serpin-A4 works best against kallikrein-7, of the serine proteinases tested to date. Serpin-A4 is found at concentrations of approximately 13.5 ug/L of plasma, much less than the serpin A1 and serpin A3 concentrations. The mode of action of serpin A4 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A4 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. Heparin binds to serpin-A4 at two sites, and to the target serine proteinase, apparently stabilizing the complex. Serpin-A4 is increased by PDGF, estrogen, progesterone, growth hormone and thyroxin, and has been reported to increase vascular smooth muscle cell proliferation in culture. Serpin-A4 is also reported to decrease angiogenesis and tumor growth rate. The Serpin-A4 sequence codes for a 427 amino acid protein, with a predicted mass of 48.56 kDa and a pI of 7.59. Glycosylation makes serpin-A4 run at about 58 kDa on SDS PAGE gels, while bacterially produced recombinant serpin-A4 runs at about 40-43 kDa. Serpin-A4 is made by many tissues, including liver, stomach, pancreas, kidney, heart, colon, prostate and testis. 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-A4 is a polyclonal antibody made to the serine proteinase inhibitor kallistatin (Serpin-A4). The antibody is made to a synthetic peptide based on the Helix 4 to Helix 5 of human serpin-A4. 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-A4, also known as Kallistatin and PI-4 was first described as kallikrein-binding protein (KBP), a protein found in complex with tissue kallikrein in plasma. The complex was seen as a 92 kDa heterodimer that was stable to heat and SDS denaturation, although 0.1% SDS would prevent the formation of the complex. Serpin A4 is a serpin of the A clade, the archetype of which is alpha-1 antitrypsin. Serpin-A4 levels were found to be 5-10 times lower in spontaneously hypertensive rats, and increasing the serpin-A4 in these rats returns them to a normotensive state. Upregulating serpin-A4 in wild type mice makes them hypotensive. Serpin-A4 has also been reported to be elevated in muscle damage, and decreased in diabetic retinopathy. Serpin-A4 is reportedly cleaved by cathepsin-D at the reactive center loop, the bait area that serpins have in common. Serpin-A4 works best against kallikrein-7, of the serine proteinases tested to date. Serpin-A4 is found at concentrations of approximately 13.5 ug/L of plasma, much less than the serpin A1 and serpin A3 concentrations. The mode of action of serpin A4 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A4 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. Heparin binds to serpin-A4 at two sites, and to the target serine proteinase, apparently stabilizing the complex. Serpin-A4 is increased by PDGF, estrogen, progesterone, growth hormone and thyroxin, and has been reported to increase vascular smooth muscle cell proliferation in culture. Serpin-A4 is also reported to decrease angiogenesis and tumor growth rate. The Serpin-A4 sequence codes for a 427 amino acid protein, with a predicted mass of 48.56 kDa and a pI of 7.59. Glycosylation makes serpin-A4 run at about 58 kDa on SDS PAGE gels, while bacterially produced recombinant serpin-A4 runs at about 40-43 kDa. Serpin-A4 is made by many tissues, including liver, stomach, pancreas, kidney, heart, colon, prostate and testis. 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-A4 is a polyclonal antibody made to the serine proteinase inhibitor kallistatin (Serpin-A4). The antibody is made to a synthetic peptide based on the second heparin binding site of human serpin-A4. 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-A4, also known as Kallistatin and PI-4 was first described as kallikrein-binding protein (KBP), a protein found in complex with tissue kallikrein in plasma. The complex was seen as a 92 kDa heterodimer that was stable to heat and SDS denaturation, although 0.1% SDS would prevent the formation of the complex. Serpin A4 is a serpin of the A clade, the archetype of which is alpha-1 antitrypsin. Serpin-A4 levels were found to be 5-10 times lower in spontaneously hypertensive rats, and increasing the serpin-A4 in these rats returns them to a normotensive state. Upregulating serpin-A4 in wild type mice makes them hypotensive. Serpin-A4 has also been reported to be elevated in muscle damage, and decreased in diabetic retinopathy. Serpin-A4 is reportedly cleaved by cathepsin-D at the reactive center loop, the bait area that serpins have in common. Serpin-A4 works best against kallikrein-7, of the serine proteinases tested to date. Serpin-A4 is found at concentrations of approximately 13.5 ug/L of plasma, much less than the serpin A1 and serpin A3 concentrations. The mode of action of serpin A4 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A4 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. Heparin binds to serpin-A4 at two sites, and to the target serine proteinase, apparently stabilizing the complex. Serpin-A4 is increased by PDGF, estrogen, progesterone, growth hormone and thyroxin, and has been reported to increase vascular smooth muscle cell proliferation in culture. Serpin-A4 is also reported to decrease angiogenesis and tumor growth rate. The Serpin-A4 sequence codes for a 427 amino acid protein, with a predicted mass of 48.56 kDa and a pI of 7.59. Glycosylation makes serpin-A4 run at about 58 kDa on SDS PAGE gels, while bacterially produced recombinant serpin-A4 runs at about 40-43 kDa. Serpin-A4 is made by many tissues, including liver, stomach, pancreas, kidney, heart, colon, prostate and testis. 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.
