Granzyme B antibody | GB11
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Mouse anti Granzyme B
- Product Type
- Monoclonal Antibody
- Granzyme B
|Mouse anti Granzyme B antibody, clone GB11 recognizes the serine protease Granzyme B, important in the induction of apoptosis in target cells by cytolytic lymphocytes (CTLs).
Granzyme B plays a key role in the induction of apoptosis by CTLs. After delivery to the target cell, Granzyme B activates the cascade of caspases that finally results in cell death.
Mouse anti Granzyme B antibody, clone GB11 is suitable for the detection of Granzyme B expressing cells by flow cytometry. In normal peripheral blood approximately 20% of CD8+ve T cells have been found to express Granzyme B.
- Target Species
- Species Cross-Reactivity
Target Species Cross Reactivity Chimpanzee Monkey Rhesus Monkey
- N.B. Antibody reactivity and working conditions may vary between species.
- Product Form
- Purified IgG - liquid
- Purified IgG prepared by affinity chromatography on Protein A from tissue culture supernatant
- Buffer Solution
- Tris buffered saline
- Preservative Stabilisers
- 0.09% sodium azide (NaN3)
- Purified human Granzyme B.
- Approx. Protein Concentrations
- IgG concentration 1.0 mg/ml
- Fusion Partners
- Spleen cells from immunised Balb/c mice were fused with cells of the mouse SP2/0 myeloma cell line.
- For research purposes only
- 12 months from date of despatch
Avoid repeated freezing and thawing as this may denature the antibody. Storage in frost-free freezers is not recommended.
|Application Name||Verified||Min Dilution||Max Dilution|
|Flow Cytometry 1||1/10||1/100|
|Immunohistology - Frozen|
- 1 Membrane permeabilization is required for this application. The use of Leucoperm (Product Code BUF09) is recommended for this purpose.
- Flow Cytometry
- Use 10μl of the suggested working dilution to label 106 cells or 100μl whole blood
- Mouse anti Human granzyme B antibody, clone GB11 may be used as a capture reagent in sandwich ELISA assays for soluble Granzyme B in conjunction with biotin conjugated clone GB10 (MCA2119B) as a detection reagent.
References for Granzyme B antibody
Spaeny-Dekking, E.H. et al. (1998) Extracellular granzymes A and B in humans: detection of native species during CTL responses in vitro and in vivo.
J Immunol. 160 (7): 3610-6.
Tschopp, C.M. (2006) Granzyme B, a novel mediator of allergic inflammation: its induction and release in blood basophils and human asthma.
Wever, D. C. et al. (1998) The CD8+ Granzyme B+ T cell subset in peripheral blood from healthy individuals contains activated and apoptosis-prone cells.
Immunol. 93: 383
Hsi, B.L. & Yeh, C.J. (1986) Monoclonal antibodies to human amnion.
J Reprod Immunol. 9 (1): 11-21.
Mahrus, S. & Craik, C.S. (2005) Selective chemical functional probes of granzymes A and B reveal granzyme B is a major effector of natural killer cell-mediated lysis of target cells.
Chem Biol. 12: 567-77.
Davis, C.C. et al. (2010) Interleukin-7 permits Th1/Tc1 maturation and promotes ex vivo expansion of cord blood T cells: a critical step toward adoptive immunotherapy after cord blood transplantation.
Cancer Res. 70: 5249-58.
Hallermalm, K. et al. (2008) Modulation of the tumor cell phenotype by IFN-gamma results in resistance of uveal melanoma cells to granule-mediated lysis by cytotoxic lymphocytes.
J Immunol. 180: 3766-74.
Hufner, K. et al. (2009) Fewer latent herpes simplex virus type 1 and cytotoxic T cells occur in the ophthalmic division than in the maxillary and mandibular divisions of the human trigeminal ganglion and nerve.
J Virol. 83: 3696-703.
View The Latest Product References
Kumar, D. et al. (2009) JNK MAPK pathway regulates constitutive transcription of CCL5 by human NK cells through SP1.
J Immunol. 182: 1011-20.
Clayton, A. et al. (2008) Human tumor-derived exosomes down-modulate NKG2D expression.
J Immunol. 180: 7249-58.
Schleypen, J.S. et al. (2006) Cytotoxic markers and frequency predict functional capacity of natural killer cells infiltrating renal cell carcinoma.
Clin Cancer Res. 12: 718-25.
Hodge, S. et al. (2015) Increased CD8 T-cell granzyme B in COPD is suppressed by treatment with low-dose azithromycin.
Respirology. 20 (1): 95-100.
Kumagai-Takei, N. et al. (2016) The Suppressed Induction of Human Mature Cytotoxic T Lymphocytes Caused by Asbestos Is Not due to Interleukin-2 Insufficiency.
J Immunol Res. 2016: 7484872.
Kumagai-Takei, N. et al. (2021) Effect of IL-15 addition on asbestos-induced suppression of human cytotoxic T lymphocyte induction.
Environ Health Prev Med. 26 (1): 50.
Jimenez, O. et al. (2019) M1-like macrophage polarization prevails in young children with classic Hodgkin Lymphoma from Argentina.
Sci Rep. 9 (1): 12687.
- Entrez Gene
- GO Terms
- GO:0005515 protein binding
- GO:0001772 immunological synapse
- GO:0004252 serine-type endopeptidase activity
- GO:0005829 cytosol
- GO:0005634 nucleus
- GO:0006922 cleavage of lamin
- GO:0019835 cytolysis
- GO:0008629 induction of apoptosis by intracellular signals
- GO:0008633 activation of pro-apoptotic gene products
- View More GO Terms
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