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Manufactured by BioVendor

Granzyme B Murine Baculovirus

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:Baculovirus
  • Other names:Granzyme 2, Fragmentin 2, Human lymphocyte protein, Granzyme-B, GrB, GZMB, C11, CTLA-1, Cathepsin G-like 1, CTSGL1, Cytotoxic T-lymphocyte proteinase 2, Lymphocyte protease, HLP, SECT, T-cell serine protease 1-3E
  • Species:Murine
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Cat. No. Size Price

RBG20076002 2 µg
RBG20076010 10 µg
RBG20076100 100 μg
PubMed Product Details
Technical Data


Recombinant protein


Granzyme B is a cysteine protease found in the cytoplasmic granules of cytolytic T lymphocytes (CTL) and natural killer (NK) cells. Granzyme B is required for the induction of target cell lysis, which occurs as part of cell-mediated immune responses, and can activate apoptosis in target cells by both caspase-dependent and caspase-independent mechanisms. Proteolytic cleavage of substrates by Granzyme B takes place primarily after aspartic acid residues. Recombinant Murine Granzyme B is a glycosylated 227 amino acid protein, comprising the mature active portion of the murine Granzyme B precursor. The apparent molecular weight is 28.9 kDa by mass spectrometry.

Amino Acid Sequence






Biological Activity

Determined by its ability to cleave a synthetic chromogentic Granzyme B substrate. The expected specific activity, when using the Ac-IEPD-pNA substrate at 25οC, is greater than 750 nM/min per μg of enzyme.


Endotoxin level is <0.1 ng/μg of protein (<1EU/μg).


Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1–1.0 mg/ml. Do not vortex. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at –20°C to –80°C




Research topic

Apoptosis, Extracellular matrix, Immune Response, Infection and Inflammation, Transplantation, Animal studies


Granzymes are exogenous serine proteinases (enzymes) that are released from cytoplasmic granules of cytotoxic lymphocytes (CTLs) and NK cells. The name “granzymes” is derived from: granules + enzymes. These granules contain next to granzymes other proteins including a pore-forming protein (Perforin). Upon binding of the CTL to a target cell (by CTL-receptor and antigen-presenting MHC molecules on the target cell) the contents of the granules are released in the intercellular space where after perforine will “perforate” the target cell membrane by forming transmembrane pores. Through these pores the granzymes can now enter the cytosol of the target cell. Granzyme B activates the intracellular cascade of caspases finally resulting in the killing of the target cells. Also Granzyme A is able to induce apoptosis in the target cell but the molecular mechanisms of the pathway involved need to be clarified. Percentages of the Granzyme A and B positive CTLs can be determined by flow cytometry and immunocytochemical methods for many disorders. Not all granzymes enter the target cell, part of them also “leak” in to the peripheral blood and other biological fluids. Detectable amounts of granzymes have been found to circulate in healthy volunteers. These soluble granzymes can be measured by ELISAs. Viral infections: Increased levels of soluble granzymes have been found with patients suspected of an increased NK cell and CTL-response caused by systemic viral infections such as EBV, HIV, CMV, hepatitis A and Dengue fever. Lymphomas and carcinomas: It is shown that the presence of a high percentage of Granzyme B positive CTLs in glands of patients suffering from Hodgkin’s disease correlate with a severe prognosis. Rheumatoid arthritis: Soluble Granzyme A and B is increased in synovial fluid from rheumatoid arthritis and significantly higher than levels in patients with osteoarthrosis. Transplantation: Granzymes are likely involved in the acute rejection of kidney-transplants, as infiltrating lymphocytes in the rejected kidney strongly express granzymes. Increasing plasma levels of soluble granzymes in patients with a kidney transplants suggest a systemic viral infection, in particular an infection by CMV.

Summary References (10)

References to Granzyme B

  • Boivin WA, Cooper DM, Hiebert PR, Granville DJ. Intracellular versus extracellular granzyme B in immunity and disease: challenging the dogma. Lab Invest. 2009 Nov;89(11):1195-220. doi: 10.1038/labinvest.2009.91. Epub 2009 Sep 21. PMID: 19770840; PMCID: PMC7102238. See more on PubMed
  • Buzza MS, Zamurs L, Sun J, Bird CH, Smith AI, Trapani JA, Froelich CJ, Nice EC, Bird PI. Extracellular matrix remodeling by human granzyme B via cleavage of vitronectin, fibronectin, and laminin. J Biol Chem. 2005 Jun 24;280(25):23549-58. doi: 10.1074/jbc.M412001200. Epub 2005 Apr 19. PMID: 15843372. See more on PubMed
  • Hiebert PR, Boivin WA, Abraham T, Pazooki S, Zhao H, Granville DJ. Granzyme B contributes to extracellular matrix remodeling and skin aging in apolipoprotein E knockout mice. Exp Gerontol. 2011 Jun;46(6):489-99. doi: 10.1016/j.exger.2011.02.004. Epub 2011 Feb 18. PMID: 21316440. See more on PubMed
  • Hiebert PR, Wu D, Granville DJ. Granzyme B degrades extracellular matrix and contributes to delayed wound closure in apolipoprotein E knockout mice. Cell Death Differ. 2013 Oct;20(10):1404-14. doi: 10.1038/cdd.2013.96. Epub 2013 Aug 2. PMID: 23912712; PMCID: PMC3770318. See more on PubMed
  • Kurschus FC, Jenne DE. Delivery and therapeutic potential of human granzyme B. Immunol Rev. 2010 May;235(1):159-71. doi: 10.1111/j.0105-2896.2010.00894.x. PMID: 20536562. See more on PubMed
  • Lord SJ, Rajotte RV, Korbutt GS, Bleackley RC. Granzyme B: a natural born killer. Immunol Rev. 2003 Jun;193:31-8. doi: 10.1034/j.1600-065x.2003.00044.x. PMID: 12752668. See more on PubMed
  • Parkinson LG, Toro A, Zhao H, Brown K, Tebbutt SJ, Granville DJ. Granzyme B mediates both direct and indirect cleavage of extracellular matrix in skin after chronic low-dose ultraviolet light irradiation. Aging Cell. 2015 Feb;14(1):67-77. doi: 10.1111/acel.12298. Epub 2014 Dec 11. PMID: 25495009; PMCID: PMC4326907. See more on PubMed
  • Rousalova I, Krepela E. Granzyme B-induced apoptosis in cancer cells and its regulation (review). Int J Oncol. 2010 Dec;37(6):1361-78. doi: 10.3892/ijo_00000788. PMID: 21042704. See more on PubMed
  • Shi L, Yang X, Froelich CJ, Greenberg AH. Purification and use of granzyme B. Methods Enzymol. 2000;322:125-43. doi: 10.1016/s0076-6879(00)22013-2. PMID: 10914010. See more on PubMed
  • Trapani JA, Sutton VR. Granzyme B: pro-apoptotic, antiviral and antitumor functions. Curr Opin Immunol. 2003 Oct;15(5):533-43. doi: 10.1016/s0952-7915(03)00107-9. PMID: 14499262. See more on PubMed
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