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Recombinant Human Serum Amyloid A1 Protein

Novus Biologicals, part of Bio-Techne | Catalog # NBP2-61366

Novus Biologicals, part of Bio-Techne
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NBP2-61366-100ug
NBP2-61366-10ug
NBP2-61366-500ug

Key Product Details

Source

E. coli

Conjugate

Unconjugated

Product Specifications

Description

A single non-glycosylated polypeptide chain containing 104 amino acids corresponding to Recombinant Human Apolipoprotein-Serum Amyloid A

Source: E. coli

Uniprot ID: P0DJI8

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

Purity

>98%, by SDS-PAGE and HPLC

Predicted Molecular Mass

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.

Activity

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.

Protein / Peptide Type

Recombinant Protein

Formulation, Preparation and Storage

NBP2-61366
Formulation 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
Reconstitution Recommended to centrifuge prior to opening. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL. Apportion stock solutions into working aliquots and store at <-20C.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Store at -20 to -70C as supplied. After reconstitution, store at 2 to 8C for 1 month and at -20 to -70C for long term storage. Avoid repeated freeze-thaw cycles.

Background: Serum Amyloid A1

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 its 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 quot houekeeping quot 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.

Alternate Names

PIG4, SAA1

Gene Symbol

SAA1

Additional Serum Amyloid A1 Products

Product Documents for Recombinant Human Serum Amyloid A1 Protein

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Product Specific Notices for Recombinant Human Serum Amyloid A1 Protein

This product is for research use only and is not approved for use in humans or in clinical diagnosis. This product is guaranteed for 1 year from date of receipt.

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