SAA Equine

Serum Amyloid A (APO-SAA) Equine Recombinant
Cat. No.
BT21853
Source
Escherichia Coli.
Synonyms
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity

Greater than 95.0% 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

SAA Equine produced in E.coli is a single, non-glycosylated polypeptide chain (1-110 a.a) containing 120 a.a and having a molecular mass of 13,580 Dalton. SAA s fused with a 10 amino acids affinity tag at N-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Description
SAA Equine, produced in E. coli, is a single, non-glycosylated polypeptide chain (amino acids 1-110) containing 120 amino acids and having a molecular mass of 13,580 Daltons. SAA is fused with a 10 amino acid affinity tag at the N-terminus and purified by proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
SAA was lyophilized from 0.01M HCl (pH 2.0).
Solubility
It is recommended to reconstitute the lyophilized SAA in 0.01M HCl (pH 2.0) at a concentration not less than 100 µg/ml. This solution can then be further diluted into other aqueous solutions.
Stability
Lyophilized SAA, although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution, Serum Amyloid A (APO-SAA) should be stored at 4°C for between 2-7 days. For future use, it should be stored below -18°C. For long-term storage, it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Source
Escherichia Coli.

Product Science Overview

Structure and Production

The recombinant SAA protein is typically produced in Escherichia coli (E. coli). It is a single, non-glycosylated polypeptide chain consisting of 110 amino acids, with a molecular mass of approximately 13,580 Daltons . The protein is often fused with an affinity tag at the N-terminus to facilitate purification through chromatographic techniques .

Function and Importance

SAA serves as a sensitive marker for various inflammatory disorders, including infections, autoimmune diseases, and cancer . Elevated levels of SAA are indicative of an acute-phase response, making it invaluable in clinical diagnostics for disease monitoring and treatment evaluation . In horses, SAA concentrations can range from nearly undetectable levels in healthy individuals to several thousand mg/L in those with severe inflammation .

Clinical Applications

The recombinant form of SAA is used extensively in research and diagnostic applications. It aids in the development of assays to measure SAA levels in blood samples, providing critical information about the inflammatory status of the animal . These assays are particularly useful in veterinary medicine, where rapid and accurate detection of inflammation is essential for effective treatment.

Stability and Storage

The lyophilized (freeze-dried) form of recombinant SAA is stable at room temperature for up to three weeks but should be stored desiccated below -18°C for long-term preservation . Upon reconstitution, it is recommended to store the protein at 4°C for short-term use and below -18°C for extended periods, with the addition of a carrier protein to prevent freeze-thaw cycles .

Research and Therapeutic Potential

Research into SAA continues to uncover its complex roles in inflammation, immune regulation, and lipid metabolism . Understanding these roles opens up potential therapeutic strategies for conditions characterized by excessive inflammation. By modulating SAA activities, scientists hope to develop novel interventions that could transform clinical practice and improve outcomes for various inflammatory diseases .

In summary, Serum Amyloid A (APO-SAA) Equine Recombinant is a vital tool in both research and clinical diagnostics, offering insights into the inflammatory processes and potential therapeutic avenues for managing inflammation in horses.

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