Render Target: SSR
Render Timestamp: 2024-11-14T22:47:01.475Z
Commit: 3c1f305a63297e594ac8d7bb5424007d592d68be
XML generation date: 2024-09-30 01:57:31.149
Product last modified at: 2024-09-30T08:01:50.737Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Granzyme H (E4T2E) Rabbit mAb #18268

Filter:
  • WB

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 25-35
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Granzyme H (E4T2E) Rabbit mAb recognizes endogenous levels of total Granzyme H protein. This antibody does not cross-react with human Granzyme A, B, K, or M proteins.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gln195 of human Granzyme H protein.

    Background

    Granzymes are a family of serine proteases expressed by cytotoxic T lymphocytes and natural killer (NK) cells and are key components of immune responses to pathogens and transformed cells (1). Granzymes are synthesized as zymogens and are processed into mature enzymes by cleavage of a leader sequence. They are released by exocytosis in lysosome-like granules containing perforin, a membrane pore-forming protein. Granzyme B has the strongest apoptotic activity of all the granzymes as a result of its caspase-like ability to cleave substrates at aspartic acid residues thereby activating procaspases directly and cleaving downstream caspase substrates (2,3).
    Granzyme H has chymotrypsin-like thioester activity with a preference for hydrophobic, aromatic amino acid residues, such as phenylalanine, tyrosine, or methionine, at the P1 site (4,5). Granzyme H is predominantly expressed at high levels in NK cells, but not in T lymphocytes, and has also been described in mast cells (6-8). After perforin-mediated entry into a target cell, Granzyme H induces many hallmarks of programmed cell death, such as mitochondrial depolarization, generation of reactive oxygen species, DNA degradation, and chromatin condensation (9,10).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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