SLPI Human

Secretory Leukocyte Peptidase Inhibitor Human Recombinant
Cat. No.
BT16903
Source
Escherichia Coli.
Synonyms
Antileukoproteinase, ALK1, ALP, BLPI, HUSI, HUSI-I, MPI, WAP4, WFDC4, WAP four-disulfide core domain protein 4, Protease inhibitor WAP4, Seminal proteinase inhibitor, Mucus proteinase inhibitor.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 80.0% 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

SLPI Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (26-132 a.a.) and having a molecular mass of 14 kDa. The SLPI is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Secretory leukocyte protease inhibitor (SLPI) is a secreted protein that protects epithelial tissues from damage by serine proteases. It is found in various secretions, including seminal plasma, cervical mucus, and bronchial secretions. SLPI exhibits a strong affinity for trypsin, leukocyte elastase, and cathepsin G, effectively inhibiting their activity. This inhibitory action contributes to the immune response by safeguarding epithelial surfaces from damage caused by these enzymes. SLPI also demonstrates broad-spectrum antibiotic properties. As an acid-stable protease inhibitor, SLPI effectively neutralizes trypsin, chymotrypsin, elastase, and cathepsin G, preventing elastase-induced harm to oral and mucosal tissues.
Description
This recombinant SLPI protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 128 amino acids (specifically, amino acids 26-132). It has a molecular weight of 14 kDa. A 21 amino acid His-Tag is fused to the N-terminus of the SLPI protein to facilitate purification, which is achieved using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The SLPI human solution is provided in a buffer consisting of 20mM Tris-HCl (pH 8.0), 2mM DTT, 0.1M NaCl, and 20% glycerol.
Stability
For short-term storage (2-4 weeks), the solution should be kept at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. To maintain protein integrity, avoid repeated cycles of freezing and thawing.
Purity
The purity of SLPI is greater than 80%, as determined by SDS-PAGE analysis.
Synonyms
Antileukoproteinase, ALK1, ALP, BLPI, HUSI, HUSI-I, MPI, WAP4, WFDC4, WAP four-disulfide core domain protein 4, Protease inhibitor WAP4, Seminal proteinase inhibitor, Mucus proteinase inhibitor.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSGKSFKAGV CPPKKSAQCL RYKKPECQSD WQCPGKKRCC PDTCGIKCLD PVDTPNPTRR KPGKCPVTYG QCLMLNPPNF CEMDGQCKRD LKCCMGMCGK SCVSPVKA.

Product Science Overview

Structure and Function

SLPI consists of two homologous domains of 53 and 54 amino acids . The C-terminal domain exhibits anti-protease activity, while the N-terminal domain’s function remains unknown . SLPI is known to inhibit several proteases, including human leukocyte elastase, cathepsin G, trypsin, neutrophil elastase, and mast cell chymase .

Biological Role

SLPI plays a crucial role in protecting epithelial tissues from serine proteases . It contributes to the immune response by safeguarding epithelial surfaces from endogenous proteolytic enzymes . Additionally, SLPI has broad-spectrum antibiotic activity, providing antibacterial, antifungal, and antiviral protection .

Clinical Significance

SLPI’s inhibitory effect on proteases makes it a significant player in modulating inflammatory and immune responses . It has been implicated in various diseases, including diabetic kidney disease (DKD), where its potential as a diagnostic and prognostic biomarker is being evaluated .

Historical Context

SLPI was first described by Robert Thompson and Kjell Ohlsson in 1986 during a study aimed at identifying novel leukocyte protease inhibitors in human saliva . Since then, extensive research has been conducted to understand its structure, function, and clinical applications.

Applications in Biotechnology

Recombinant SLPI is produced using biotechnological methods to study its therapeutic potential. Its ability to inhibit proteases and modulate immune responses makes it a promising candidate for treating inflammatory diseases and infections.

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