Description
RP1-Serpin-A6 is a polyclonal antibody made to the serine proteinase inhibitor corticosteroid binding globulin (Serpin-A6). The antibody is made to a synthetic peptide based on the aminoterminal end of mature human serpin-A6. 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-A6, also known as corticosteroid binding globulin (CBG) and transcortin is a serpin of the A clade, the archetype of which is alpha-1 antitrypsin. Best known as corticosteroid binding globulin, serpin-A6 is produced principally by the liver. Serpin-A6 is the main carrier of cortisol in plasma, conveying about 90-95% of the total cortisol. About 60% of aldosterone in circulation is carried by serpin-A6, and smaller percentages of progesterone and testosterone are also transported by serpin-A6. The corticosteroid carrying capacity of seerpin-A6 is not passive; the bound steroid is held in an unreactive form, and cleavage of the serpin-A6 RCL allows release in an active form. This mechanism allows corticosteroids to be delivered and activated at the sites of inflammation and proteolysis. A family of loss-of-function mutations in serpin-A6 has been implicated in idiopathic chronic fatigue syndrome, thought to cause fatigue by reducing the amount of available cortisol, although there is some dispute about the mechanism. The mode of action of serpin A6 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A6 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-A6 sequence codes for a 405 amino acid protein, with a predicted mass of 45.1 kDa and a pI of 5.6. 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-A6 is a polyclonal antibody made to the serine proteinase inhibitor corticosteroid binding globulin (Serpin-A6). The antibody is made to a synthetic peptide based on Helix 4 to Helix 5 of human serpin-A6. 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-A6, also known as corticosteroid binding globulin (CBG) and transcortin is a serpin of the A clade, the archetype of which is alpha-1 antitrypsin. Best known as corticosteroid binding globulin, serpin-A6 is produced principally by the liver. Serpin-A6 is the main carrier of cortisol in plasma, conveying about 90-95% of the total cortisol. About 60% of aldosterone in circulation is carried by serpin-A6, and smaller percentages of progesterone and testosterone are also transported by serpin-A6. The corticosteroid carrying capacity of seerpin-A6 is not passive; the bound steroid is held in an unreactive form, and cleavage of the serpin-A6 RCL allows release in an active form. This mechanism allows corticosteroids to be delivered and activated at the sites of inflammation and proteolysis. A family of loss-of-function mutations in serpin-A6 has been implicated in idiopathic chronic fatigue syndrome, thought to cause fatigue by reducing the amount of available cortisol, although there is some dispute about the mechanism. The mode of action of serpin A6 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A6 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-A6 sequence codes for a 405 amino acid protein, with a predicted mass of 45.1 kDa and a pI of 5.6. 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-A6 is a polyclonal antibody made to the serine proteinase inhibitor corticosteroid binding globulin (Serpin-A6). The antibody is made to a synthetic peptide based on Helix 7 to Helix 8 of human serpin-A6. 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-A6, also known as corticosteroid binding globulin (CBG) and transcortin is a serpin of the A clade, the archetype of which is alpha-1 antitrypsin. Best known as corticosteroid binding globulin, serpin-A6 is produced principally by the liver. Serpin-A6 is the main carrier of cortisol in plasma, conveying about 90-95% of the total cortisol. About 60% of aldosterone in circulation is carried by serpin-A6, and smaller percentages of progesterone and testosterone are also transported by serpin-A6. The corticosteroid carrying capacity of seerpin-A6 is not passive; the bound steroid is held in an unreactive form, and cleavage of the serpin-A6 RCL allows release in an active form. This mechanism allows corticosteroids to be delivered and activated at the sites of inflammation and proteolysis. A family of loss-of-function mutations in serpin-A6 has been implicated in idiopathic chronic fatigue syndrome, thought to cause fatigue by reducing the amount of available cortisol, although there is some dispute about the mechanism. The mode of action of serpin A6 involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of serpin A6 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-A6 sequence codes for a 405 amino acid protein, with a predicted mass of 45.1 kDa and a pI of 5.6. 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.
