Chaparral Labs
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protein

Serum amyloid P-component

aka SAP

APCS
protein:P02743disease:adad:direction:up

Gene

APCS

Organism

Homo sapiens(9606)

Length

223 aa

Mass

25,387 Da

AI summarysource-grounded · cited inline
claude-haiku-4-5-20251001

Serum amyloid P-component (SAP), encoded by APCS, is a 223-amino acid protein that functions as a calcium-dependent lectin and can interact with DNA and histones (UniProt: P02743). It may scavenge nuclear material released from damaged circulating cells, suggesting roles in cellular debris clearance and immune regulation.

SAP is a circulating acute-phase reactant traditionally associated with inflammation and tissue damage response. While UniProt lists no specific disease annotations for this protein, it has broader relevance to neuroinflammatory processes given its capacity to bind nuclear antigens and participate in immune clearance pathways.

In Alzheimer's disease, SAP is upregulated in post-mortem AD brain tissue relative to age-matched controls (Chaparral AD proteomics). Quantitative proteomics analysis detected SAP at a mean log2 fold-change of +1.57 in human brain from AD patients versus controls, measured via TMT-labeled mass spectrometry across four subcellular fractions. This elevation suggests potential involvement in AD-associated neuroinflammation or amyloid-related pathology.

Generated from the curated entity record below. May contain errors — verify against source links.

Proteomics Evidence · AD

↑ Up in AD

P3

not detected

P2

not detected

S2

+1.570

S3

not detected

Mean log₂FC across detected fractions: +1.57 (1 of 4 fractions detected)

Human post-mortem AD brain vs age-matched controls, TMT-labeled, 4 subcellular fractions (P2, P3, S2, S3), DDA proteomics.

Related Publications

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Function

Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin

Sources

Last updated 5/8/2026, 6:31:47 AM