Vaspin Human, His

Vaspin Human Recombinant, His Tag
Cat. No.
BT30727
Source
Escherichia Coli.
Synonyms
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.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Vaspin Human Recombinant produced in E.Coli is a single, non-glycosylated, His Tag, polypeptide chain containing 415 amino acids and having a molecular mass of 47 kDa.
The Vaspin is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Vaspin, short for visceral adipose-specific serine protease inhibitor, is a recently discovered adipokine belonging to the serine protease inhibitor family. This protein plays a unique role in enhancing insulin sensitivity, particularly in individuals struggling with obesity. Research suggests that the expression of human vaspin mRNA within adipose tissue is regulated in a way that is specific to the fat depot. This regulation appears to be linked to factors such as obesity, insulin resistance, and the body's ability to process glucose.
Description
Recombinant human Vaspin, produced in E. coli bacteria, is a single-chain polypeptide. It is not glycosylated and contains a His tag for purification. With a length of 415 amino acids, it has a molecular weight of 47 kDa. The purification process involves proprietary chromatographic techniques to ensure high purity.
Physical Appearance
A clear and colorless solution that has been sterilized by filtration.
Formulation
The Vaspin protein is supplied in a buffer consisting of 20mM Tris at pH 8, 0.2mM PMSF (phenylmethylsulfonyl fluoride), and 10% glycerol.
Stability
While liquid Vaspin remains stable for up to one week at 10°C, it is recommended to store it at temperatures below -18°C for optimal long-term preservation. To further enhance stability during prolonged storage, consider adding a carrier protein such as HSA (human serum albumin) or BSA (bovine serum albumin) to a final concentration of 0.1%. Avoid repeated freezing and thawing of the product.
Purity
The purity of Vaspin is determined using SDS-PAGE analysis and is consistently greater than 90.0%.
Synonyms
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.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLKPSFSPRN YKALSEVQGW KQRMAAKELA RQNMDLGFKL LKKLAFYNPG RNIFLSPLSI STAFSMLCLG AQDSTLDEIK QGFNFRKMPE KDLHEGFHYI IHELTQKTQD LKLSIGNTLF IDQRLQPQRK FLEDAKNFYS AETILTNFQN LEMAQKQIND FISQKTHGKI NNLIENIDPG TVMLLANYIF FRARWKHEFD PNVTKEEDFF LEKNSSVKVP MMFRSGIYQV GYDDKLSCTI LEIPYQKNIT AIFILPDEGK LKHLEKGLQV DTFSRWKTLL SRRVVDVSVP RLHMTGTFDL KKTLSYIGVS KIFEEHGDLT KIAPHRSLKV GEAVHKAELK MDERGTEGAA GTGAQTLPME TPLVVKIDKP YLLLIYSEKI PSVLFLGKIV NPIGK.

Product Science Overview

Introduction

Vaspin, also known as visceral adipose-specific serpin or SERPINA12, is a member of the serine protease inhibitor family. It is a newly identified adipokine, predominantly expressed in visceral white adipose tissues. Vaspin has garnered significant interest due to its unique role as an insulin-sensitizing adipocytokine, particularly in the context of obesity .

Structure and Characteristics

Human recombinant vaspin is produced in Escherichia coli and is a single, non-glycosylated polypeptide chain containing 415 amino acids. It has a molecular mass of approximately 47 kDa . The recombinant protein is tagged with a His (histidine) tag, which facilitates its purification through affinity chromatography techniques .

The amino acid sequence of human recombinant vaspin includes several distinctive structural features typical of the serpin family, such as three beta-sheets, nine alpha-helices, and one central loop . These structural elements are crucial for its function as a serine protease inhibitor.

Biological Function

Vaspin’s primary function is as a serine protease inhibitor, although its specific protease targets are still under investigation. It exhibits approximately 40.2% sequence identity with alpha1-antitrypsin, another well-known serpin . Vaspin’s expression in visceral fat is positively correlated with body mass index (BMI) and body fat percentage .

Role in Metabolism and Obesity

Vaspin plays a significant role in glucose metabolism and insulin sensitivity. Studies have shown that the administration of vaspin to obese mice improves glucose tolerance and insulin sensitivity, leading to normalized blood glucose levels . This makes vaspin a potential therapeutic target for metabolic disorders such as obesity and type 2 diabetes.

Production and Purification

The production of human recombinant vaspin involves the expression of the protein in Escherichia coli. The His tag attached to the protein allows for its purification using affinity chromatography, resulting in a highly purified product with a purity greater than 90% as determined by SDS-PAGE . The protein is typically formulated in a buffer containing 20mM Tris (pH 8), 0.2mM PMSF, and 10% glycerol .

Stability and Storage

Human recombinant vaspin is stable at 10°C for up to one week but should be stored below -18°C for long-term storage. To prevent degradation, it is recommended to add a carrier protein such as 0.1% human serum albumin (HSA) or bovine serum albumin (BSA) and to avoid freeze-thaw cycles .

Applications

Vaspin is primarily used in laboratory research to study its role in metabolism, obesity, and related metabolic disorders. It is also utilized in various assays, including Western blotting, ELISA, and functional assays, to investigate its biological functions and interactions .

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