Description
RP1-Serpin-A2 is a polyclonal antibody made to the serine proteinase inhibitor Alpha-1-antitrypsin-related protein (Serpin-A2). The antibody is made to a synthetic peptide based on the amino end of mature human serpin-A2. 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-A2, also known as alpha-1-antitrypsin-related protein, is a serine proteinase inhibitor (SERPIN). Serpin -A2 was cloned in an analysis of the serpin A1 gene, to which the serpin A2 gene is linked. At first thought to be a pseudogene, the serpin A2 gene contains the same RNA splice sites as the serpin A1 sequence, and does not contain an internal stop codon. The sequence identity between human serpin A1 and A2 is 61% at the amino acid level, with 73% similarity, although there are key differences in the sequences. Perhaps most importantly, the P1 site of the reactive center loop is changed from methionine in serpin A1 to tryptophan in serpin A2. Other serpins contain different residues in the P1 position, and they confer different enzyme specificities, so it is likely that serpin A2 has a different inhibitory profile than serpin A1. Little is known about the serpin A2 protein. The mode of action of serpin A2 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A2 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. Assuming similar function as serpin A1, serpin A2 can also relieve the stress somewhat by polymerizing, and the homooligomers are inactivated, causing a protease imbalance and tissue damage. Three sequences are reported for serpin A2: a 583 amino acid form with a 275 residue extension at the amino end, a 421 amino acid form and a 420 amino acid form. The 583 amino acid form would be atypical for the serpin A clade, if expressed, and has a predicted mass of 64.8 kDa and a pI of 6.4. The two sequences most similar to serpin A1 have predicted mass of 47.7 kDa and pI of 6.8. 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-A2 is a polyclonal antibody made to the serine proteinase inhibitor Alpha-1-antitrypsin-related protein (Serpin-A2). The antibody is made to a synthetic peptide based on the Helix 4 to Helix 5 region of human serpin-A2. 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-A2, also known as alpha-1-antitrypsin-related protein, is a serine proteinase inhibitor (SERPIN). Serpin -A2 was cloned in an analysis of the serpin A1 gene, to which the serpin A2 gene is linked. At first thought to be a pseudogene, the serpin A2 gene contains the same RNA splice sites as the serpin A1 sequence, and does not contain an internal stop codon. The sequence identity between human serpin A1 and A2 is 61% at the amino acid level, with 73% similarity, although there are key differences in the sequences. Perhaps most importantly, the P1 site of the reactive center loop is changed from methionine in serpin A1 to tryptophan in serpin A2. Other serpins contain different residues in the P1 position, and they confer different enzyme specificities, so it is likely that serpin A2 has a different inhibitory profile than serpin A1. Little is known about the serpin A2 protein. The mode of action of serpin A2 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A2 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. Assuming similar function as serpin A1, serpin A2 can also relieve the stress somewhat by polymerizing, and the homooligomers are inactivated, causing a protease imbalance and tissue damage. Three sequences are reported for serpin A2: a 583 amino acid form with a 275 residue extension at the amino end, a 421 amino acid form and a 420 amino acid form. The 583 amino acid form would be atypical for the serpin A clade, if expressed, and has a predicted mass of 64.8 kDa and a pI of 6.4. The two sequences most similar to serpin A1 have predicted mass of 47.7 kDa and pI of 6.8. 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-A2 is a polyclonal antibody made to the serine proteinase inhibitor Alpha-1-antitrypsin-related protein (Serpin-A2). The antibody is made to a synthetic peptide based on the Helix 7to Helix 8 region of human serpin-A2. 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-A2, also known as alpha-1-antitrypsin-related protein, is a serine proteinase inhibitor (SERPIN). Serpin -A2 was cloned in an analysis of the serpin A1 gene, to which the serpin A2 gene is linked. At first thought to be a pseudogene, the serpin A2 gene contains the same RNA splice sites as the serpin A1 sequence, and does not contain an internal stop codon. The sequence identity between human serpin A1 and A2 is 61% at the amino acid level, with 73% similarity, although there are key differences in the sequences. Perhaps most importantly, the P1 site of the reactive center loop is changed from methionine in serpin A1 to tryptophan in serpin A2. Other serpins contain different residues in the P1 position, and they confer different enzyme specificities, so it is likely that serpin A2 has a different inhibitory profile than serpin A1. Little is known about the serpin A2 protein. The mode of action of serpin A2 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A2 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. Assuming similar function as serpin A1, serpin A2 can also relieve the stress somewhat by polymerizing, and the homooligomers are inactivated, causing a protease imbalance and tissue damage. Three sequences are reported for serpin A2: a 583 amino acid form with a 275 residue extension at the amino end, a 421 amino acid form and a 420 amino acid form. The 583 amino acid form would be atypical for the serpin A clade, if expressed, and has a predicted mass of 64.8 kDa and a pI of 6.4. The two sequences most similar to serpin A1 have predicted mass of 47.7 kDa and pI of 6.8. 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.
