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Alpha 1 Antichymotrypsin [141176-92-3]

16-16-012400
Athens Research
Protein IDP01011
Product group Proteins / Signaling Molecules
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Overview

  • Supplier
    Athens Research
  • Product Name
    Alpha 1 Antichymotrypsin [141176-92-3]
  • Delivery Days Customer
    9
  • Applications Supplier
    Proteolytic Inhibition studies, Alzheimers research, Prostate Cancer Research. In Vitro Diagnostics, Antisera Production
  • CAS Number
    141176-92-3
  • Certification
    Research Use Only
  • Estimated Purity
    ≥95% by SDS-PAGE
  • Protein IDP01011
  • Protein Name
    Alpha-1-antichymotrypsin
  • Scientific Description
    Alpha 1-antichymotrypsin (ACT) is an acute-phase plasma glycoprotein encoded by the SERPINA3 gene, primarily produced in the liver. As a member of the serpin superfamily, ACT functions by inhibiting chymotrypsin-like serine proteases, including neutrophil cathepsin G and mast cell chymases. This protective mechanism prevents tissue damage from proteolytic enzymes, particularly in the lower respiratory tract. Normal serum levels range from 25-40mg/dL. During inflammatory processes, ACT concentration increases proportionally to the extent of tissue damage, with levels declining as inflammation resolves. ACT is significantly involved in Alzheimer's disease pathology, where it's overexpressed in astrocytes surrounding amyloid plaques, enhancing amyloid-beta fibrillization and inducing tau hyperphosphorylation. It's also elevated in rheumatoid arthritis, Crohn's disease, ulcerative colitis, and following burn injuries. Clinically, the PSA-ACT complex serves as a valuable biomarker for prostate cancer, indicating tumor mass and clinical staging.
  • Shelf life instruction
    more then 1 year
  • Source
    Source human plasma non-reactive for HBsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.
  • Storage Instruction
    ≤ -20°C
  • UNSPSC
    41116100

References

  • Laberge, A., et al., (2019) 'alfa‐2‐Macroglobulin induces the shedding of microvesicles from cutaneous wound myofibroblasts', J Cell Physiol., 234: pp 11369–11379.
    Read this paper
  • Domain, R., et al., (2024) 'Pharmacological inhibition of cathepsin S and of NSPs-AAP-1 (a novel, alternative protease driving the activation of neutrophil serine proteases)', Biochemical Pharmacology, 229: pp 116114.
    Read this paper