Description
RP1-Serpin-A12 is a polyclonal antibody made to the serine proteinase inhibitor Serpin-A12. The antibody is made to a synthetic peptide based on the aminoterminal end of mature human serpin-A12. 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-A12, also known as Vaspin (Visceral adipose tissue-derived serine protease inhibitor) is an A-clade serpin, the archetype of which is alpha-1 antitrypsin. Serpin-A12 was first described from rat visceral adipose tissue, in the Otsuka Long-Evans Tokushima fatty rats (OLETF), which are used for models of obesity and diabetes. In humans serpin-A12 is thought to be differentially expressed in adipose tissues, with levels of expression very low in lean, glucose-tolerant subjects. Serpin-A12 is considered an adipose derived hormone, or an adiptokine (an adipose-derived cytokine), due to the distal effects it is thought to play on insulin resistance and glucose metabolism. Serum levels of serpin-A12 are slightly increased in males with type-II diabetes, relative to normal glucose-tolerant individuals. Serpin-A12 levels were found to be higher in normal glucose-tolerant females than in males, but the serpin-A12 levels dropped ion type-II diabetes females (relative to controls). Exercise was shown to elevate serum concentrations of serpin-A12, in both glucose-tolerant controls and in individuals with type-II diadetes. Serpin-A12 serum levels also increased with body-mass index (BMI). Administration of recombinant serpin-A12 to obese mice improved glucose tolerance and insulin sensitivity. In humans serpin-A12 gene polymorphisims have been implicated as possible risk factors in type-II diabetes. The mode of action of most A-clade serpins involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of A-clade serpins 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. Other serpins of the A-clade are well known as circulating inhibitors of serine proteinases, principally in the coagulation cascade, but little is known to date about serpin-A12 specificity, localization or function. Full length serpin-A12 sequence codes for a 414 amino acid protein, with a predicted mass of 47.2 kDa and a pI of 9.2. 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 months at -20C.
Description
RP2-Serpin-A12 is a polyclonal antibody made to the serine proteinase inhibitor Serpin-A12. The antibody is made to a synthetic peptide based on helix 5 to helix 6 of human serpin-A12. 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-A12, also known as Vaspin (Visceral adipose tissue-derived serine protease inhibitor) is an A-clade serpin, the archetype of which is alpha-1 antitrypsin. Serpin-A12 was first described from rat visceral adipose tissue, in the Otsuka Long-Evans Tokushima fatty rats (OLETF), which are used for models of obesity and diabetes. In humans serpin-A12 is thought to be differentially expressed in adipose tissues, with levels of expression very low in lean, glucose-tolerant subjects. Serpin-A12 is considered an adipose derived hormone, or an adiptokine (an adipose-derived cytokine), due to the distal effects it is thought to play on insulin resistance and glucose metabolism. Serum levels of serpin-A12 are slightly increased in males with type-II diabetes, relative to normal glucose-tolerant individuals. Serpin-A12 levels were found to be higher in normal glucose-tolerant females than in males, but the serpin-A12 levels dropped ion type-II diabetes females (relative to controls). Exercise was shown to elevate serum concentrations of serpin-A12, in both glucose-tolerant controls and in individuals with type-II diadetes. Serpin-A12 serum levels also increased with body-mass index (BMI). Administration of recombinant serpin-A12 to obese mice improved glucose tolerance and insulin sensitivity. In humans serpin-A12 gene polymorphisims have been implicated as possible risk factors in type-II diabetes. The mode of action of most A-clade serpins involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of A-clade serpins 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. Other serpins of the A-clade are well known as circulating inhibitors of serine proteinases, principally in the coagulation cascade, but little is known to date about serpin-A12 specificity, localization or function. Full length serpin-A12 sequence codes for a 414 amino acid protein, with a predicted mass of 47.2 kDa and a pI of 9.2. 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 months at -20C.
Description
RP3-Serpin-A12 is a polyclonal antibody made to the serine proteinase inhibitor Serpin-A12. The antibody is made to a synthetic peptide based on helix 7 to helix 8 of human serpin-A12. 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-A12, also known as Vaspin (Visceral adipose tissue-derived serine protease inhibitor) is an A-clade serpin, the archetype of which is alpha-1 antitrypsin. Serpin-A12 was first described from rat visceral adipose tissue, in the Otsuka Long-Evans Tokushima fatty rats (OLETF), which are used for models of obesity and diabetes. In humans serpin-A12 is thought to be differentially expressed in adipose tissues, with levels of expression very low in lean, glucose-tolerant subjects. Serpin-A12 is considered an adipose derived hormone, or an adiptokine (an adipose-derived cytokine), due to the distal effects it is thought to play on insulin resistance and glucose metabolism. Serum levels of serpin-A12 are slightly increased in males with type-II diabetes, relative to normal glucose-tolerant individuals. Serpin-A12 levels were found to be higher in normal glucose-tolerant females than in males, but the serpin-A12 levels dropped ion type-II diabetes females (relative to controls). Exercise was shown to elevate serum concentrations of serpin-A12, in both glucose-tolerant controls and in individuals with type-II diadetes. Serpin-A12 serum levels also increased with body-mass index (BMI). Administration of recombinant serpin-A12 to obese mice improved glucose tolerance and insulin sensitivity. In humans serpin-A12 gene polymorphisims have been implicated as possible risk factors in type-II diabetes. The mode of action of most A-clade serpins involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of A-clade serpins 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. Other serpins of the A-clade are well known as circulating inhibitors of serine proteinases, principally in the coagulation cascade, but little is known to date about serpin-A12 specificity, localization or function. Full length serpin-A12 sequence codes for a 414 amino acid protein, with a predicted mass of 47.2 kDa and a pI of 9.2. 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 months at -20C.
