Recombinant Human Serum Amyloid A1 Protein

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Concentration
LYOPH

Order Details

Recombinant Human Serum Amyloid A1 Protein Summary

Description
A single non-glycosylated polypeptide chain containing 104 amino acids.

Source: Escherichia coli.

Amino Acid Sequence:
RSFFSFLGEA FDGARDMWRA YSDMREANYI GSDKYFHARG NYDAAKRGPG GVWAAEAISN ARENIQRFFG RGAEDSLADQ AANEWGRSGK DPNHFRPAGL PEKY

Details of Functionality
Fully biologically active when compared to standard. The biological activity determined by its ability to down-regulate lipid biosynthesis in aortic smooth muscle cells. The effective concentration was found to be 4 uM.
Source
E. coli
Protein/Peptide Type
Recombinant Protein
Gene
SAA1
Purity
>98%, by HPLC

Applications/Dilutions

Theoretical MW
11.7 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

Storage
Store at -20C. Avoid freeze-thaw cycles.
Buffer
Lyophilized from a 0.2 um filtered concentrated solution in 20 mM Tris-HCl, pH 9.0, 150 mM NaCl.
Preservative
No Preservative
Concentration
LYOPH
Purity
>98%, by HPLC
Reconstitution Instructions
Reconstitute with sterilized distilled water or 0.1% BSA aqueous buffer to a final concentration of 0.1 - 1.0 mg/ml.

Alternate Names for Recombinant Human Serum Amyloid A1 Protein

  • MGC111216
  • PIG4
  • SAA
  • SAA1
  • SAA2
  • serum amyloid A protein
  • Serum Amyloid A1
  • TP53I4
  • tumor protein p53 inducible protein 4

Background

The serum amyloid A (SAA) family comprises a number of differentially expressed lipoproteins, acute phase SAA1 and SAA2, the former being a major component in plasma, and constitutive SAA's (C-SAAs). Although the liver is the primary site of synthesis of both SAA types, extrhepatic production has been reported. The in vivo concentrations increase by as much as 1000 fold during inflammation. Several studies have expressed it's importance in the diagnosis and monitoring of various diseases. Pathological SAA values are often detected in association with normal CRP concentrations. SAA rises earlier and more sharply than CRP. SAA enhances the binding of HDL's to macrophages and thus helps the delivery of lipid to sites of injury for use in tissue repair. It is thus thought to be an integral part of the disease process. In addition, recent experiments suggest that SAA may play a "houekeeping" role in normal human tissues. Elevated levels of SAA over time predispose secondary amyloidosis, extracellular accumulation of amyloid fibrils, derived from a circulating precursor, in various tissues and organs. The most common form of amyloidosis occurs secondary to chronic inflammatory disease, particularly rheumatoid artheritis. Amyloidosis is a heterogeneous group of disorders characterized by extracellular deposition of abnormal protein fibrils, which are derived from different proteins. Almost all patients with amyloidosis have some level of renal disorders. The immunoperoxidase technique has the advantage of being able to detect amyloid in formalin-fixed paraffin embedded tissues and is a very specific method for identifying amyloid fibril proteins. Small and minute amounts of amyloid can be detected with both Amyloid P (ab688) and Amyloid A antibodies, and thus could allow earlier treatment before organ damage has occurred.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.

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Bioinformatics

Gene Symbol SAA1
Entrez