Human alpha 1 Antitrypsin intron 1 ChIP Primer and Probe Set (ab85777)

Overview

  • Product nameHuman alpha 1 Antitrypsin intron 1 ChIP Primer and Probe Set
    See all alpha 1 Antitrypsin kits
  • Product overview

    Accession number: NM_000295.
    The HsSERPINA1 primers and probe can be used to quantify a control locus in chromatin immunoprecipitation (ChIP) assays with chromatin prepared from human cells.

    SERPINA1 (Alpha 1-Antitrypsin protease) is expressed in liver but inactive in most other cell types. The primers and probe are located in intron 1. In most cell types SERPINA1 is enriched with histone modifications associated with silencing (e.g. Histone H3 K27 di methylation, see image with ab24684). Whereas it shows low levels of histone modifications associated with active gene transcription such as Histone H3 K9 acetylation (see image with ab4441).

Properties

  • FunctionInhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.
    Short peptide from AAT: reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE).
  • Tissue specificityUbiquitous. Expressed in leukocytes and plasma.
  • Involvement in diseaseAlpha-1-antitrypsin deficiency
  • Sequence similaritiesBelongs to the serpin family.
  • DomainThe reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.
  • Post-translational
    modifications
    N-glycosylated. Differential glycosylation produces a number of isoforms. N-linked glycan at Asn-107 is alternatively di-antennary, tri-antennary or tetra-antennary. The glycan at Asn-70 is di-antennary with trace amounts of tri-antennary. Glycan at Asn-271 is exclusively di-antennary. Structure of glycans at Asn-70 and Asn-271 is Hex5HexNAc4. The structure of the antennae is Neu5Ac(alpha1-6)Gal(beta1-4)GlcNAc attached to the core structure Man(alpha1-6)[Man(alpha1-3)]Man(beta1-4)GlcNAc(beta1-4)GlcNAc. Some antennae are fucosylated, which forms a Lewis-X determinant.
    Proteolytic processing may yield the truncated form that ranges from Asp-30 to Lys-418.
  • Cellular localizationSecreted. Endoplasmic reticulum. The S and Z allele are not secreted effectively and accumulate intracellularly in the endoplasmic reticulum and Secreted, extracellular space, extracellular matrix.
  • Information by UniProt
  • Alternative names
    • A1A
    • A1AT
    • A1AT_HUMAN
    • AAT
    • Alpha 1 antiproteinase
    • Alpha 1 antitrypsin
    • Alpha 1 antitrypsin null
    • Alpha 1 protease inhibitor
    • Alpha-1 protease inhibitor
    • Alpha-1-antiproteinase
    • alpha1 proteinase inhibitor
    • Alpha1AT
    • Dom1
    • PI
    • PI1
    • PRO2275
    • Serine (or cysteine) proteinase inhibitor clade A member 1
    • Serine protease inhibitor 1-1
    • Serine protease inhibitor A1a
    • Serpin A1
    • Serpin A1a
    • Serpin peptidase inhibitor clade A member 1
    • Serpina1
    • Short peptide from AAT
    • SPAAT
    • Spi1-1
    see all

References for Human alpha 1 Antitrypsin intron 1 ChIP Primer and Probe Set (ab85777)

ab85777 has not yet been referenced specifically in any publications.

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