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SRP4324

Sigma-Aldrich

Apo-SAA human

recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC)

Synonym(s):

Amyloid fibril protein AA, Amyloid protein A, SAA, SAA1, SAA2, Serum amyloid A protein

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About This Item

MDL number:
UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in E. coli

Assay

≥98% (HPLC)
≥98% (SDS-PAGE)

form

lyophilized

mol wt

~11.5 kDa

packaging

pkg of 50 μg

storage condition

avoid repeated freeze/thaw cycles

technique(s)

protein expression: suitable

impurities

endotoxin, tested

NCBI accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... SAA1(6288)

Related Categories

General description

Human apo-SAA is a 104 amino acid polypeptide that circulates primarily in association with high-density lipoproteins (HDL). The level of apo-SAA, normally 1-5 μg/ml in plasma, increases 500-1000 fold within 24 hours of an inflammatory stimulus and, under these conditions, is the most abundant HDL apo-lipoprotein. The human SAA gene codes for a 122 amino acid polypeptide, which contains an 18 amino acid N-terminal signal sequence.
Research Area: IMMUNO AND CKS
Serum amyloid A (SAA) proteins are a group of apolipoproteins produced in response to cytokines released by activated monocytes/macrophages. SAA is a highly conserved acute-phase protein primarily synthesized by the liver.

Application

Apo-SAA human has been used to culture and stimulate RAW264.7 macrophages to study its effects on visfatin expression.
Apo-serum amyloid A has been used to study its effect on the expression of Visfatin in macrophages.

Biochem/physiol Actions

Serum amyloid A (SAA) is an equally sensitive marker for the acute phase as C-reactive protein (CRP). It is the most sensitive non-invasive biochemical indicator for allograft rejection. The function of SAA as a cytokine-like protein has been acknowledged in cell-cell communication and as a feedback mechanism in inflammatory, immunologic, neoplastic, and protective pathways. SAA plays a crucial role in the regulation and potentially the spread of the initial acute phase response.
Serum amyloid A (SAA) is found normally at concentrations of 0.1μM in blood. However, its concentration increases up to 1000-fold under stress. It has been associated with several chronic inflammatory diseases, such as atherosclerosis. It is found to participate in the inflammatory response by facilitating chemotaxis, migration, and adhesion of inflammatory cells, particularly monocytes/macrophages. SAA is also found to induce the synthesis and secretion of multiple kinds of inflammatory cytokines, such as TNF-α (tumor necrosis factor-α), IL-1β (interleukin-1β), MCP-1 (monocyte chemoattractant protein-1), and Lp-PLA2 (lipoprotein-associated phospholipase A2).

Physical form

Sterile filtered and Lyophilized without additives.

Reconstitution

Centrifuge the vial prior to opening. Avoid freeze-thaw cycles.
Reconstitute in 0.1% acetic acid to a concentration of 1 μg/ul. This solution can then be diluted into other aqueous buffers.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Human serum amyloid A (SAA) protein: a prominent acute-phase reactant for clinical practice
Malle, EDBF and De Beer, FC
European Journal of Clinical Investigation, 26(6), 427-435 (1996)
Immune functions of serum amyloid A
Eklund KK, et al.
Critical Reviews in Immunology, 32(4) (2012)
Serum Amyloid a Promotes Visfatin Expression in Macrophages.
Wang S
BioMed Research International (2016)
Qian Yan et al.
Cellular signalling, 26(9), 1783-1791 (2014-04-08)
Serum amyloid A (SAA), a major acute-phase protein, has potent cytokine-like activities in isolated phagocytes and synovial fibroblasts. SAA-induced proinflammatory cytokine gene expression requires transcription factors such as NF-κB; however, the associated epigenetic regulatory mechanism remains unclear. Here we report
Serum amyloid A-a review
Sack Jr, George H
Molecular Medicine, 46-46 (2018)

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