Vaspin Human
Escherichia Coli.
Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.
Sterile Filtered White lyophilized (freeze-dried) powder.
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Description
Vaspin Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 394 amino acids and having a molecular mass of 45.1kDa.
Vaspin is purified by proprietary chromatographic techniques.
Product Specs
Vaspin, short for visceral adipose-specific SERPIN, is an adipokine belonging to the serine protease inhibitor family. This recently discovered protein has been shown to improve insulin sensitivity, particularly in individuals struggling with obesity. Studies indicate that the expression of the human vaspin gene in adipose tissue is influenced by the specific type of fat tissue and may be linked to factors such as body mass, insulin resistance, and the body's ability to process glucose.
Recombinant Human Vaspin, produced in E. coli bacteria, is a single-chain polypeptide consisting of 394 amino acids. This non-glycosylated protein has a molecular weight of 45.1 kDa. The purification process of Vaspin involves advanced chromatographic techniques to ensure its high purity.
Sterile Filtered White lyophilized powder.
The product is provided as a lyophilized powder, obtained by freeze-drying a 0.2µm filtered solution. The solution used for lyophilization contains 20mM Tris-HCl buffer with a pH of 8.0, 150mM NaCl (sodium chloride), and 0.02% Tween-20.
To reconstitute the lyophilized Vaspin, it is recommended to dissolve it in sterile 18 MΩ-cm H2O (water) at a concentration of at least 100 µg/ml. This solution can be further diluted with other aqueous solutions as needed.
While the lyophilized Vaspin remains stable at room temperature for up to 3 weeks, it is recommended to store it desiccated at a temperature below -18°C for long-term preservation. After reconstitution, the Vaspin solution should be stored at 4°C and is stable for 2-7 days. For extended storage, it is advisable to store the reconstituted solution below -18°C. It is important to avoid repeated cycles of freezing and thawing to maintain protein stability.
The purity of Vaspin is greater than 98.0%, as confirmed by the following analytical methods:
(a) High-Performance Liquid Chromatography (RP-HPLC) analysis.
(b) Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis.
Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.
Escherichia Coli.
LKPSFSPRNY KALSEVQGWK QRMAAKELAR QNMDLGFKLL KKLAFYNPGR NIFLSPLSIS TAFSMLCLGA QDSTLDEIKQ GFNFRKMPEK DLHEGFHYII HELTQKTQDL KLSIGNTLFI DQRLQPQRKF LEDAKNFYSA ETILTNFQNL EMAQKQINDF ISQKTHGKIN NLIENIDPGT VMLLANYIFF RARWKHEFDP NVTKEEDFFL EKNSSVKVPM MFRSGIYQVG YDDKLSCTIL EIPYQKNITA IFILPDEGKL KHLEKGLQVD TFSRWKTLLS RRVVDVSVPR LHMTGTFDLK KTLSYIGVSK IFEEHGDLTK IAPHRSLKVG EAVHKAELKM DERGTEGAAG TGAQTLPMET PLVVKIDKPY LLLIYSEKIP SVLFLGKIVN PIGK.
Product Science Overview
Vaspin is a protein consisting of 395 amino acid residues, with a molecular weight of approximately 45.2 kDa . The protein structure of vaspin includes three beta-sheets, nine alpha-helices, and one central loop, which are characteristic features of serpin family members . These structural elements are crucial for its function as a serine protease inhibitor.
Vaspin is known to play a role in various biological processes, including:
Despite its structural similarity to other serpins, the specific protease inhibitory activity of vaspin remains unknown . However, it has been observed that vaspin mRNA expression in visceral fat is positively correlated with body mass index (BMI) and the percentage of body fat .
Administration of vaspin to obese mice has shown promising results, including improved glucose tolerance and insulin sensitivity, which is reflected by normalized blood glucose levels . This suggests that vaspin may have potential therapeutic applications in the treatment of metabolic disorders such as obesity and type 2 diabetes.
Recombinant human vaspin is produced using Escherichia coli expression systems . The recombinant protein is typically purified to a high degree of purity (≥ 98%) using SDS-PAGE gel and HPLC analyses . It is available in lyophilized form and can be reconstituted for various laboratory applications, including Western blot, ELISA, and functional assays .
