Description
RP1-Serpin-A7 is a polyclonal antibody made to the serine proteinase inhibitor thyroxine-binding globulin (Serpin-A7). The antibody is made to a synthetic peptide based on the aminoterminal end of mature human serpin-A7. 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-A7, also known as thyroxine-binding globulin (TBG) is a serpin of the A clade, the archetype of which is alpha-1 antitrypsin. Best known as thyroxine-binding globulin, serpin-A7 is produced principally by the liver. Serpin-A7 is the main carrier of T4 and T3 in plasma, conveying about 75% of circulating T4 and 70% of circulating T3. Approximately 20% of serpin-A7 is found in the bound form with T4 and T3, the balance is in a free form. Serum concentrations of serpin-A7 are about 20 mg/L. Like serpin-A6, the corticosteroid-binding globulin, the bound thyroxine is held in an unreactive form, and cleavage of the serpin-A7 RCL allows release in an active form. This mechanism allows thyroxine to be delivered and activated at the sites of inflammation and proteolysis. Serpin-A7 differs somewhat from serpin-A6 and the other A-clade serpins in having a proline in the P8 position of the RCL, which abrogates hydrogen bonding, and limits loop insertion into the A-sheet. This is thought to allow some reversible binding of thyroxine, whereas the cleavage of the RCL is an irreversible reaction. A family of loss-of-function mutations in serpin-A7 have been identified, as well as excess serpin-A7 produced by gene duplication. The loss of function and null mutations lead to decreased levels of thyroxine in plasma. The mode of action of serpin-A7 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A7 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 Serpin-A7 sequence codes for a 415 amino acid protein, with a predicted mass of 46.3 kDa and a pI of 5.8. The acidic pI is in contrast to the basic pI of the heparin-binding serpins, and in line with serum proteins found in circulation. 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-A7 is a polyclonal antibody made to the serine proteinase inhibitor thyroxine-binding globulin (Serpin-A7). The antibody is made to a synthetic peptide based on Helix 4 to Helix 5 of human serpin-A7. 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-A7, also known as thyroxine-binding globulin (TBG) is a serpin of the A clade, the archetype of which is alpha-1 antitrypsin. Best known as thyroxine-binding globulin, serpin-A7 is produced principally by the liver. Serpin-A7 is the main carrier of T4 and T3 in plasma, conveying about 75% of circulating T4 and 70% of circulating T3. Approximately 20% of serpin-A7 is found in the bound form with T4 and T3, the balance is in a free form. Serum concentrations of serpin-A7 are about 20 mg/L. Like serpin-A6, the corticosteroid-binding globulin, the bound thyroxine is held in an unreactive form, and cleavage of the serpin-A7 RCL allows release in an active form. This mechanism allows thyroxine to be delivered and activated at the sites of inflammation and proteolysis. Serpin-A7 differs somewhat from serpin-A6 and the other A-clade serpins in having a proline in the P8 position of the RCL, which abrogates hydrogen bonding, and limits loop insertion into the A-sheet. This is thought to allow some reversible binding of thyroxine, whereas the cleavage of the RCL is an irreversible reaction. A family of loss-of-function mutations in serpin-A7 have been identified, as well as excess serpin-A7 produced by gene duplication. The loss of function and null mutations lead to decreased levels of thyroxine in plasma. The mode of action of serpin-A7 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A7 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 Serpin-A7 sequence codes for a 415 amino acid protein, with a predicted mass of 46.3 kDa and a pI of 5.8. The acidic pI is in contrast to the basic pI of the heparin-binding serpins, and in line with serum proteins found in circulation. 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-A7 is a polyclonal antibody made to the serine proteinase inhibitor thyroxine-binding globulin (Serpin-A7). The antibody is made to a synthetic peptide based on Helix 7 to Helix 8 of human serpin-A7. 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-A7, also known as thyroxine-binding globulin (TBG) is a serpin of the A clade, the archetype of which is alpha-1 antitrypsin. Best known as thyroxine-binding globulin, serpin-A7 is produced principally by the liver. Serpin-A7 is the main carrier of T4 and T3 in plasma, conveying about 75% of circulating T4 and 70% of circulating T3. Approximately 20% of serpin-A7 is found in the bound form with T4 and T3, the balance is in a free form. Serum concentrations of serpin-A7 are about 20 mg/L. Like serpin-A6, the corticosteroid-binding globulin, the bound thyroxine is held in an unreactive form, and cleavage of the serpin-A7 RCL allows release in an active form. This mechanism allows thyroxine to be delivered and activated at the sites of inflammation and proteolysis. Serpin-A7 differs somewhat from serpin-A6 and the other A-clade serpins in having a proline in the P8 position of the RCL, which abrogates hydrogen bonding, and limits loop insertion into the A-sheet. This is thought to allow some reversible binding of thyroxine, whereas the cleavage of the RCL is an irreversible reaction. A family of loss-of-function mutations in serpin-A7 have been identified, as well as excess serpin-A7 produced by gene duplication. The loss of function and null mutations lead to decreased levels of thyroxine in plasma. The mode of action of serpin-A7 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A7 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 Serpin-A7 sequence codes for a 415 amino acid protein, with a predicted mass of 46.3 kDa and a pI of 5.8. The acidic pI is in contrast to the basic pI of the heparin-binding serpins, and in line with serum proteins found in circulation. 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.
