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SIGLEC7 Protein (AA 19-353) (His tag)

SIGLEC7 Origin: Human Host: HEK-293 Cells Recombinant >95 % as determined by SDS-PAGE. Active
Catalog No. ABIN7013595
  • Target See all SIGLEC7 Proteins
    SIGLEC7 (Sialic Acid Binding Ig-Like Lectin 7 (SIGLEC7))
    Protein Type
    Recombinant
    Biological Activity
    Active
    Protein Characteristics
    AA 19-353
    Origin
    Human
    Source
    • 6
    • 3
    • 3
    • 2
    • 1
    HEK-293 Cells
    Purification tag / Conjugate
    This SIGLEC7 protein is labelled with His tag.
    Sequence
    AA 19-353
    Characteristics
    Biotinylated Human SIRP alphaV2 / CD172a Protein, His,Avitag™
    Purity
    >95 % as determined by SDS-PAGE.
    Endotoxin Level
    Less than 1.0 EU per μg by the LAL method.
    Top Product
    Discover our top product SIGLEC7 Protein
  • Application Notes
    MALS verified
    Restrictions
    For Research Use only
  • Format
    Lyophilized
    Buffer
    25 mM MES, 150 mM NaCl, pH 5.5
    Storage
    -20 °C
  • Target
    SIGLEC7 (Sialic Acid Binding Ig-Like Lectin 7 (SIGLEC7))
    Alternative Name
    Siglec-7 (SIGLEC7 Products)
    Synonyms
    SIGLEC7 Protein, AIRM1 Protein, CD328 Protein, CDw328 Protein, D-siglec Protein, QA79 Protein, SIGLEC-7 Protein, SIGLEC19P Protein, SIGLECP2 Protein, p75 Protein, p75/AIRM1 Protein, sialic acid-binding Ig-like lectin 7 Protein, sialic acid binding Ig like lectin 7 Protein, LOC468976 Protein, SIGLEC7 Protein
    Background
    Siglec-7 is a member of the human CD33-related Siglec receptor. The extracellular region of Siglec-7 is characterized by an N-terminal V-set Ig domain that can bind sialic acid and two C2-set Ig domains. The cytoplasmic tail of Siglec-7 has one immune-receptor tyrosine-based inhibitory motif (ITIM) and one ITIM-like motif. Siglec-7 is considered as a sialic acid-dependent immunoreceptor with inhibitory potential and expressed predominantly on human NK cells, monocytes and a small subset of CD8+ T cells.
    Molecular Weight
    38.8 kDa
    NCBI Accession
    NP_055200
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