Recombinant Feline Serum Amyloid A1 Protein Summary
Description |
Recombinant cat serum amyloid A. Source:Feline Amino Acid Sequence:121 aa recombinant protein produced in a eukaryotic expression system, which includes a proprietary 10 aa tag at the N-terminus, UniProt P19707 |
Source |
E. coli |
Protein/Peptide Type |
Recombinant Protein |
Gene |
SAA1 |
Purity |
>95% |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
13.8 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 |
0.01 M HCl |
Preservative |
No Preservative |
Concentration |
LYOPH |
Purity |
>95% |
Reconstitution Instructions |
Reconstitute with 1.0 ml distilled water. Care should be taken during reconstitution as the protein may appear as a film at the bottom of the vial. Gently mix vial after reconstitution. |
Alternate Names for Recombinant Feline Serum Amyloid A1 Protein
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 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.
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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