SAA1 Human

Serum Amyloid A (APO-SAA1) Human Recombinant
Cat. No.
BT22033
Source
Escherichia Coli.
Synonyms
Serum amyloid A protein, SAA, Amyloid protein A, Amyloid fibril protein AA, SAA1, SAA2, PIG4, TP53I4, MGC111216.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 97.0% 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.
Shipped with Ice Packs
In Stock

Description

SAA1 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.
The SAA1 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
SAA1 protein, primarily produced by hepatocytes in response to inflammatory cytokines, is an acute phase reactant. This apolipoprotein, mainly synthesized in the liver, circulates at low levels in the bloodstream. SAA1 appears to play a role in the immune system, with its levels rising in blood and tissues during inflammation. It may contribute to tissue repair, act as an antibacterial agent, and signal the migration of immune cells to infection sites. Additionally, SAA1 functions as an apolipoprotein within the HDL complex.
Elevated SAA1 levels can lead to secondary amyloidosis, a condition characterized by the extracellular accumulation of amyloid fibrils derived from a circulating precursor. This deposition occurs in various tissues and organs, primarily as a consequence of chronic inflammation, particularly rheumatoid arthritis. In individuals with chronic inflammatory diseases, a cleavage product of SAA1, known as amyloid protein A, deposits systemically as amyloid in vital organs like the liver, spleen, and kidneys. These deposits, highly insoluble and resistant to breakdown, disrupt tissue architecture and impair organ function.
Description
Recombinant human SAA1, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 104 amino acids. With a molecular weight of 11.7 kDa, it undergoes purification using proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation

The lyophilization of SAA1 was carried out from a 0.2 µm filtered solution concentrated at 20mM Tris-HCl, pH 9.0 and 150mM NaCl.

Solubility
To reconstitute lyophilized SAA1, it is recommended to dissolve it in sterile 18 MΩ-cm H2O at a concentration of at least 100 µg/ml. This solution can be further diluted in other aqueous solutions.
Stability
Lyophilized SAA1 remains stable at room temperature for up to 3 weeks. However, it is advisable to store it desiccated below -18°C. Upon reconstitution, SAA1 should be stored at 4°C for 2-7 days. For extended storage, freezing below -18°C is recommended. To preserve protein stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is suggested.
Repeated freeze-thaw cycles should be avoided.
Purity
Purity exceeds 97.0%, as determined by:
(a) RP-HPLC analysis.
(b) SDS-PAGE analysis.
Biological Activity
The biological activity, assessed using a chemoattract bioassay with human monocytes, falls within the concentration range of 10-100 ng/ml.
Synonyms
Serum amyloid A protein, SAA, Amyloid protein A, Amyloid fibril protein AA, SAA1, SAA2, PIG4, TP53I4, MGC111216.
Source
Escherichia Coli.
Amino Acid Sequence
RSFFSFLGEA FDGARDMWRA YSDMREANYI GSDKYFHARG NYDAAKRGPG GVWAAEAISD ARENIQRFFG HGAEDSLADQ 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. Among these, Serum Amyloid A1 (SAA1) is a major acute-phase reactant produced predominantly by hepatocytes in response to inflammatory cytokines. The recombinant form of this protein, known as APO-SAA1 (Human Recombinant), is widely used in research to study its biological functions and implications in various diseases.

Structure and Expression

SAA1 is a small protein consisting of 104 amino acids . It is encoded by the SAA1 gene in humans and is highly conserved across vertebrate species . The protein is primarily synthesized in the liver, although extrahepatic production has also been reported . Under normal physiological conditions, SAA1 is present in the blood at low concentrations (20-50 µg/ml) . However, during the acute-phase response (APR), its levels can increase dramatically, up to 1000-fold within 24 hours .

Biological Functions

SAA1 plays a crucial role in the body’s response to inflammation, infection, and trauma. It is involved in several physiological processes, including:

  • Lipid Metabolism: SAA1 is associated with HDL and plays a role in lipid transport and metabolism .
  • Cytokine-like Activity: SAA1 functions as a cytokine, participating in cell-cell communication and modulating inflammatory and immune responses .
  • Acute-Phase Response: SAA1 is a key component of the APR, contributing to the restoration of homeostasis following physiological perturbations .
Clinical Significance

Elevated levels of SAA1 are associated with various pathological conditions, including chronic inflammatory diseases, infections, and malignancies . It is particularly significant in the diagnosis and monitoring of these conditions, often rising earlier and more sharply than C-reactive protein (CRP), another acute-phase reactant . Additionally, SAA1 has been implicated in the formation of amyloid fibrils, which can accumulate and lead to secondary amyloidosis .

Recombinant SAA1

Recombinant human SAA1 (APO-SAA1) is produced using an expression system in E. coli, resulting in a protein with a molecular weight of approximately 11.7 kDa . This recombinant form is used extensively in research to study the protein’s structure, function, and role in disease processes. It is available in a lyophilized form and is highly purified, with a purity of ≥ 98% as determined by SDS-PAGE and HPLC analyses .

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