Granzyme B (GZMB) (AA 17-247) (Active) Protein

Details for Product No. ABIN2666524, Supplier: Log in to see
Protein Name
Protein Characteristics
AA 17-247
5
2
2
2
2
1
1
1
1
1
1
1
Origin
Mouse (Murine)
16
13
1
1
1
Source
HEK-293
8
7
4
3
2
2
1
1
1
1
1
Protein Type
Recombinant
Biological Activity
Active
Application
Flow Cytometry (FACS)
Options
Supplier
Log in to see
Supplier Product No.
Log in to see
Purity > 95 % , as determined by Coomassie stained SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level

Less than 1.0 EU per μg of protein as determine by the LAL method.

Background Granzyme B is a serine protease expressed by cytotoxic T cells (CTL) and NK cells. Its main function is to induce cell death to eliminate harmful targets such as allogeneic, virally infected, and tumorous cells. This is evident by the fact that CTLs from mice deficient of granzyme B exhibit a profound defect in inducing rapid DNA fragmentation and apoptosis in target cells. Following receptor-mediated conjugate formation between CTL or NK and their target cell, granzyme B enters the target via endocytosis, and subsequently activates multiple protein substrates to induce apoptosis. Most circulating CD56+ CD8- NK cells, and approximately half of circulating CD8+ T cells, coexpress both granzyme A and B. In contrast, few circulating CD4+ T cells express granzymes A or B. Activation of CD8+ and CD4+ T cells induces substantial expression of granzyme B, but not granzyme A. Besides CTL and NK, evidence has shown that the distribution of human granzyme B has a broader spectrum of cells including CD34+ hematopoietic progenitor cells, keratinocytes, basophils, mast cells, plasmacytoid dendritic cells, and B cells. Although its role in cytotoxic lymphocyte-mediated apoptosis is well established, granzyme B can also degrade extracellular matrix proteins and alter inflammation if present in the extracellular milieu. These findings suggest that granzyme B can function as an activation molecule with potentially important immunoregulatory functions. In addition, it was shown that expression of granzyme B is elevated in acute coronary syndrome and acute myocardia infarction, indicating that granzyme B could be a factor involved in cardiovascular diseases.
Molecular Weight This 246 amino acid recombinant protein has a predicted molecular mass of approximately 27.5 kDa. The protein migrates at approximately 37 kDa in DTT-reducing conditions and approximately 37 kDa in non-reducing conditions by SDS-PAGE. The predicted N-term
Research Area Immunology, Innate Immunity, Adaptive Immunity, Apoptosis/Necrosis, Inflammation, Enzymes, Metabolism
Application Notes Optimal working dilution should be determined by the investigator.
Comment

Biological activity: Recombinant mouse Granzyme B supplied in its inactive form. Once the mouse Granzyme B is activated by active mouse Capthepsin C/DPPI, it is able to cleave the peptide substrate t-Butyloxycaronyl-Ala-Ala-ThioBenzyl ester (Boc-AAD-SBzl) in the presence of 5,5'Dithio-bis (2-nitrobenzoic acid) (DTNB)1,2, with an activity > 3000 pmol/min/μg.

Restrictions For Research Use only
Format Liquid
Reconstitution For maximum results, quick spin vial prior to opening. The recombinant protein could be aliquoted and stored at -20 °C in a sterile buffer (20 mM Tris, 150 mM NaCl, and pH 7.5).
Concentration 200 μg/mL
Buffer 0.22 μm filtered protein solution is in 20 mM Tris, 150 mM NaCl, and pH 7.5.
Handling Advice Avoid repeated freeze/thaw cycles.
Storage -20 °C
Storage Comment Unopened vial can be stored at -70°C for six months.
Supplier Images
ELISA image for Granzyme B (GZMB) (AA 17-247) (Active) protein (ABIN2666524) Granzyme B (GZMB) (AA 17-247) (Active) protein
Background publications Hiebert, Granville: "Granzyme B in injury, inflammation, and repair." in: Trends in molecular medicine, Vol. 18, Issue 12, pp. 732-41, 2012 (PubMed).

Saito, Kondo, Hojo: "Granzyme B as a novel factor involved in cardiovascular diseases." in: Journal of cardiology, Vol. 57, Issue 2, pp. 141-7, 2011 (PubMed).

Grossman, Verbsky, Tollefsen, Kemper, Atkinson, Ley: "Differential expression of granzymes A and B in human cytotoxic lymphocyte subsets and T regulatory cells." in: Blood, Vol. 104, Issue 9, pp. 2840-8, 2004 (PubMed).

Edwards, Kam, Powers, Trapani: "The human cytotoxic T cell granule serine protease granzyme H has chymotrypsin-like (chymase) activity and is taken up into cytoplasmic vesicles reminiscent of granzyme B-containing endosomes." in: The Journal of biological chemistry, Vol. 274, Issue 43, pp. 30468-73, 1999 (PubMed).

Smyth, McGuire, Thia: "Expression of recombinant human granzyme B. A processing and activation role for dipeptidyl peptidase I." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 154, Issue 12, pp. 6299-305, 1995 (PubMed).

Heusel, Wesselschmidt, Shresta, Russell, Ley: "Cytotoxic lymphocytes require granzyme B for the rapid induction of DNA fragmentation and apoptosis in allogeneic target cells." in: Cell, Vol. 76, Issue 6, pp. 977-87, 1994 (PubMed).

Trapani, Klein, White, Dupont: "Molecular cloning of an inducible serine esterase gene from human cytotoxic lymphocytes." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 85, Issue 18, pp. 6924-8, 1988 (PubMed).

Schmid, Weissmann: "Induction of mRNA for a serine protease and a beta-thromboglobulin-like protein in mitogen-stimulated human leukocytes." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 139, Issue 1, pp. 250-6, 1987 (PubMed).

Did you look for something else?