antibody

SAA-1 (Serum Amyloid A Protein, SAA, SAA1, SAA2)

S1002-51B

100 ug

monoclonal

mouse

nonconjugated

13A67 (Reu 86.5)

SAA-1 (Serum Amyloid A Protein, SAA, SAA1, SAA2)

mouse

Mab

Antibodies

100 ug

13A67 (Reu 86.5)

IgG1

The serum amyloid A (SAA) family comprises a number of differentially expressed apolipoproteins, acute-phase SAA1 and SAA2, the former being the major component in plasma, and constitutive SAAs (C-SAAs). Although the liver is the primary site of synthesis of both SAA types extrahepatic production has been reported. The in vivo concentrations increase by as much as 1000-fold during inflammation. Several studies have stressed 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. Recently, a broader view of SAA expression and function has been emerging. Expression studies show production of SAA proteins in histologically normal, atherosclerotic, Alzheimer, inflammatory, and tumor tissues. SAA has been found to have binding sites for high density lipoproteins, calcium, laminin, and heparin/heparan-sulfate. Also adhesion motifs were identified and new functions, affecting cell adhesion, migration, proliferation and aggregation discovered. These findings emphasize the importance of SAA in various physiological and pathological processes, including inflammation, atherosclerosis, thrombosis, AA- amyloidosis, rheumatoid arthritis, and neoplasia. SAA has also a number of immunomodulatory roles, it can induce chemotaxis and adhesion molecule expression, has cytokine-like properties and can promote the upregulation of metalloproteinases. It enhances the binding of high-density lipoprotein to macrophages and thus helps in the delivery of lipids to sites of injury for use in tissue repair. It is thus thought to be an integral part of the disease processes. In addition, recent experiments suggest that SAA may play a "housekeeping" role in normal human tissues. Elevated levels of SAA over time predispose to secondary amyloidosis, extracellular accumulation of amyloid fibrils, derived from a circulating precursor, in various tissue and organs. The most common form of amyloidosis occurs secondary to chronic inflammatory disease, particularly rheumatoid arthritis. The antibody is raised against human SAA and Helix Pomatia Haemocyanine. It reacts with SAA-1 type. Applications: Suitable for use in ELISA, Western Blot and Immunohistochemistry. Other applications not tested. Recommended Dilution: Western Blot: 1:10 Immunohistochemistry: Frozen or paraffin sections Optimal dilutions to be determined by the researcher. Storage and Stability: May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Hu Mo

Human SAA and Helix Pomatia Haemocyanine

Recognizes human SAA-1. Species Crossreactivity: mouse

Purified by Protein G affinity chromatography.

Supplied as a liquid in PBS, 0.1% BSA, 0.02% sodium azide.

~0.1mg/ml

Product Type: Mab Isotype: IgG1 Clone No: 13A67 (Reu 86.5) Host: mouse Source: human Concentration: ~0.1mg/ml Form: Supplied as a liquid in PBS, 0.1% BSA, 0.02% sodium azide. Purity: Purified by Protein G affinity chromatography. Immunogen: Human SAA and Helix Pomatia Haemocyanine Specificity: Recognizes human SAA-1. Species Crossreactivity: mouse Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.

E IHC WB

-20°C

1. Hazenberg, B et al; Immunohistochemical detection of Amyloid AA in formaline-fixed paraffin-embedded rectal biopsies with the monoclonal antibody anti-human SAA antibody Reu.86.2. Amyloid and Amyloidosis 1990, VIth International Symposium on Amyloidosis: 809. 2.Hazenberg, B et al; Monoclonal antibody based ELISA for human SAA. Amyloid and Amyloidosis, eds. LB Natvig et al, Kluwer Acad Publ 1990: 898. 3. Wilkins, J et al; Rapid automated enzyme immunoassays of Serum Amyloid A. Clin Chem 1994, 40: 1284. 4.Hazenberg, B et al; A quantitative method for detecting deposits of amyloid A protein in aspirated fat tissue of patients with arthritis. Ann Rheum Dis 1999, 58: 96.