Granzyme B, a neutral serine protease, has been demonstrated to be a pivotal molecule for protective immunity against viral infection and cellular malignant transformation. Provided are single-chain Fv antibodies specific for granzyme B, as versatile alternatives and complementary reagents to currently available monoclonal antibodies. Owing to the availability of its DNA sequence and large scale production capability, Fv17 should be a superior reagent for monitoring granzyme B expression in natural killer cells and antigen specific CD8 T cell immunity.
Figure 1 Dot blot detection of purified granzyme B by scFvs.
Purified granzyme B (500 ng) in PBS (pH 7.4), or treated with SDS, or SDS/ -mercaptoethanol, respectively, was deposited onto nitrocellulose membranes.
Figure 2 Immunoprecipitation of granzyme B by scFv and antibodies.
Immunoprecipitation of granzyme B from whole cell lysates of YTS cells.
Figure 3 Sandwich ELISA analysis.
Fv17 was coated onto plastic wells with anti-thyroglobulin Fv as the control.
Figure 4 Intracellular staining of granzyme B.
Peripheral blood mononuclear cells either unstimulated (plot A) or stimulated with influenza virus (plot B) were stained with PE-Cy7-labeled anti-CD8 and subsequently with FITC-labeled Fv17 in combination with PE-labeled anti-perforin.
This is a product of Creative Biolabs' Hi-Affi™ recombinant antibody portfolio, which has several benefits including:
• Increased sensitivity
• Confirmed specificity
• High repeatability
• Excellent batch-to-batch consistency
• Sustainable supply
• Animal-free production
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