Render Target: STATIC
Render Timestamp: 2024-12-09T11:45:12.647Z
Commit: 224419269841c11382c4555dbee545259bf6c379
XML generation date: 2024-09-30 01:57:17.034
Product last modified at: 2024-12-05T13:15:20.114Z
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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 B (E5V2L) Rabbit mAb #44153

Filter:
  • WB
  • IHC
  • F

    Supporting Data

    REACTIVITY M
    SENSITIVITY Endogenous
    MW (kDa) 30
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IHC-Immunohistochemistry 
    • F-Flow Cytometry 
    Species Cross-Reactivity Key:
    • M-Mouse 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    IHC Leica Bond 1:50 - 1:200
    Immunohistochemistry (Paraffin) 1:50 - 1:200
    Flow Cytometry (Fixed/Permeabilized) 1:50 - 1:200

    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.

    For a carrier-free (BSA and azide) version of this product see product #87791.

    Protocol

    Specificity / Sensitivity

    Granzyme B (E5V2L) Rabbit mAb recognizes endogenous levels of total mouse Granzyme B protein. This antibody does not cross-react with human Granzyme B proteins. Non-specific staining was observed in mouse kidney.

    Species Reactivity:

    Mouse

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala197 of mouse Granzyme B 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).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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