SAA Human

Serum Amyloid A (APO-SAA) Human Recombinant
Cat. No.
BT21979
Source
Escherichia Coli.
Synonyms
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis 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.
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Description

APO-SAA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 104 amino acids and having a molecular mass of 11.7kDa. Recombinant Apo-SAA is a consensus SAA molecule corresponding to human Apo-SAA1a, except for the presence of an N-terminal methionine, the substitution of asparagine for aspartic acid at position 60, and arginine for histidine at position 71 (the latter two substituted residues are present in Apo-SAA2b).
The Human APO-SAA is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Serum amyloid A protein (SAA), a member of the SAA family, is encoded by the SAA gene in humans. Primarily produced by the liver, SAA is secreted into the bloodstream and acts as the main acute phase reactant and an apolipoprotein component of the HDL complex. Notably, elevated levels of serum SAA protein have been linked to an increased risk of lung cancer. Under normal conditions, the concentration of Apo-SAA in plasma ranges from 1 to 5 µg/ml. However, within 24 hours of an inflammatory stimulus, Apo-SAA levels can surge dramatically, increasing 500-1000 fold, making it the most abundant HDL Apolipoprotein during inflammatory responses.
Description
Recombinant Human APO-SAA, produced in E. coli, is a single-chain polypeptide. This non-glycosylated protein comprises 104 amino acids with a molecular weight of 11.7 kDa. It is important to note that while this Recombinant Apo-SAA represents a consensus SAA molecule corresponding to human Apo-SAA1a, there are slight variations. These include an N-terminal methionine residue, an asparagine substitution for aspartic acid at position 60, and arginine replacing histidine at position 71. It's worth noting that the latter two substitutions are naturally found in the Apo-SAA2b isoform. The purification of Human APO-SAA is achieved using proprietary chromatographic techniques, ensuring a high degree of purity.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The lyophilization of Human SAA was performed from a concentrated solution (1 mg/ml) in a buffer consisting of 20 mM Tris-HCl at pH 9.0 and 150 mM NaCl.
Solubility
To reconstitute the lyophilized Human SAA, it is recommended to dissolve it in sterile 18 MΩ·cm H₂O to a concentration of at least 100 µg/ml. This solution can be further diluted as needed in other aqueous solutions.
Stability
Lyophilized Human SAA demonstrates stability at room temperature for a period of 3 weeks. However, for long-term storage, it is recommended to store the lyophilized product desiccated at temperatures below -18°C. Upon reconstitution, Human SAA should be stored at 4°C for a maximum of 2-7 days. For extended storage beyond this period, it is advisable to store the reconstituted protein at -18°C. To maintain protein integrity and activity, it is crucial to avoid repeated freeze-thaw cycles.
Purity
Purity of the protein is greater than 98.0%, as determined by the following methods: (a) Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) analysis and (b) Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis.
Biological Activity
The biological activity of Human SAA is assessed based on its ability to downregulate lipid biosynthesis in aortic smooth muscle cells. The effective concentration for this activity was determined to be 4 µM.
Source
Escherichia Coli.
Amino Acid Sequence
RSFFSFLGEA FDGARDMWRA YSDMREANYI GSDKYFHARG NYDAAKRGPG GVWAAEAISN ARENIQRFFG RGAEDSLADQ AANEWGRSGK DPNHFRPAGL PEKY.

Product Science Overview

Introduction

Serum Amyloid A (SAA) proteins are a family of apolipoproteins associated with high-density lipoprotein (HDL) in plasma. These proteins are encoded by the SAA gene in humans and are primarily synthesized in the liver. SAA proteins play a crucial role in the acute phase response, a rapid inflammatory response to trauma, infection, or other stressors.

Structure and Composition

Human recombinant Serum Amyloid A (APO-SAA) is a non-glycosylated polypeptide chain consisting of 104 amino acids with a molecular mass of approximately 11.7 kDa . The recombinant form is produced in Escherichia coli and is purified using proprietary chromatographic techniques . The amino acid sequence of APO-SAA includes several key residues that are critical for its function and stability.

Biological Function

SAA proteins are involved in various physiological processes, including lipid metabolism, immune response, and inflammation. During an acute phase response, the concentration of SAA in the serum can increase up to 1000-fold within 24 hours . This dramatic increase is primarily due to de novo synthesis in the liver. SAA proteins act as cytokine-like molecules, facilitating cell-cell communication and modulating inflammatory and immune responses .

Clinical Significance

Elevated levels of SAA are associated with several pathological conditions, including chronic inflammatory diseases, infections, and malignancies . SAA proteins can form amyloid fibrils, which accumulate in tissues and contribute to amyloidosis, a condition characterized by the deposition of insoluble protein aggregates. Additionally, SAA has been linked to atherosclerosis and other cardiovascular diseases due to its role in lipid transport and metabolism .

Applications in Research and Medicine

Recombinant human APO-SAA is widely used in research to study its biological functions and mechanisms of action. It is also utilized in the development of diagnostic assays and therapeutic interventions for diseases associated with abnormal SAA levels. The recombinant form provides a consistent and reliable source of the protein for experimental and clinical applications .

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