SERPINA12 Protein (His tag)
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- Target See all SERPINA12 Proteins
- SERPINA12 (serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 12 (SERPINA12))
- Protein Type
- Recombinant
- Biological Activity
- Active
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Origin
- Human
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Source
- HEK-293 Cells
- Purification tag / Conjugate
- This SERPINA12 protein is labelled with His tag.
- Purpose
- Recombinant Human Vaspin/SerpinA12 Protein (His Tag)(Active)
- Sequence
- Met 1-Lys 414
- Characteristics
- A DNA sequence encoding the human SERPINA12 (NP_776249.1) (Met 1-Lys 414) was expressed, with a polyhistidine tag at the C-terminus.
- Purity
- > 97 % as determined by reducing SDS-PAGE.
- Endotoxin Level
- < 1.0 EU per μg as determined by the LAL method.
- Biological Activity Comment
- Measured by its ability to inhibit KLK7 cleavage the fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2 (Catalog # ES002). The IC50 is <75 nM.
- Top Product
- Discover our top product SERPINA12 Protein
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serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 12 (SERPINA12) (AA 1-414) protein (GST tag)
SERPINA12 Origin: Human Host: Wheat germ Recombinant WB, ELISA, AP, AA
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- Restrictions
- For Research Use only
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- Format
- Lyophilized
- Reconstitution
- Please refer to the printed manual for detailed information.
- Buffer
- Lyophilized from sterile PBS, pH 7.4
- Storage
- 4 °C,-20 °C,-80 °C
- Storage Comment
- Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
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- Target
- SERPINA12 (serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 12 (SERPINA12))
- Alternative Name
- Vaspin/SerpinA12 (SERPINA12 Products)
- Synonyms
- SERPINA12 Protein, 4632419J12Rik Protein, OL-64 Protein, Ol-64 Protein, Ol64 Protein, serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 12 Protein, serpin family A member 12 Protein, serine (or cysteine) peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 12 Protein, serpin A12 Protein, SERPINA12 Protein, Serpina12 Protein, LOC612386 Protein
- Background
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Background: Serpins are the largest and most diverse family of protease inhibitors. Most serpins control proteolytic cascades, certain serpins do not inhibit enzymes, but instead perform diverse functions such as storage (ovalbumin, in egg white), hormone carriage proteins (thyroxine-binding globulin, cortisol-binding globulin) and tumor suppressor genes (maspin). Most inhibitory serpins target chymotrypsin-like serine proteases. These enzymes are defined by the presence of a nucleophilic serine residue in their catalytic site. Some serpins inhibit other classes of protease. A number of such serpins have been shown to target cysteine proteases. These enzymes differ from serine proteases in that they are defined by the presence of a nucleophilic cysteine residue, rather than a serine residue, in their catalytic site. SerpinA12, also known as OL-64, Visceral adipose tissue-derived serine protease inhibitor, Vaspin, Visceral adipose-specific serpin and SERPINA12, is a secreted protein which belongs to the serpin family. SerpinA12 / Vaspin is expressed in visceral adipose tissues. It may modulates insulin action conceivably only in the presence of its yet undefined target proteases in white adipose tissues. SerpinA12 / Vaspin may be the compensatory molecule in the pathogenesis of metabolic syndrome and SerpinA12 / Vaspin recombinant protein or vaspin-mimicking agents such as vaspin analogs, antibodies or small molecule agents may be the link to drug discovery and development.
Synonym: Serpin A12; OL-64; Visceral Adipose Tissue-Derived Serine Protease Inhibitor; Vaspin; Visceral Adipose-Specific Serpin; SERPINA12
- Molecular Weight
- 46.5 kDa
- NCBI Accession
- NP_776249
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