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Granzyme B

Granzyme B is a serine protease primarily expressed in cytotoxic T lymphocytes and natural killer cells.
It plays a crucial role in inducing apoptosis in target cells during the immune response.
Granzyme B can trigger cell death through both caspase-dependent and caspase-independant pathways, making it an important effector molecule in cell-mediated cytoxicity.
Accurate and reproducbile protocols for studying Granzyme B are essential for advancing our understanding of its function in the immune system and its potential as a therapeutic target.

Most cited protocols related to «Granzyme B»

1
Luminex® Assays for Biomarker Profiling
Cited 14 times
Reagents for Luminex® assays were custom developed by R&D Systems. Thirteen biomarkers were selected and divided into 2 panels based on relative plasma abundance and assay dynamic range. Panel 1 included the following 5 high-abundance biomarkers tested at a dilution of 1:30: sVCAM-1, sICAM-1, sTNFR-1, CHI3L1, Cystatin C. Panel 2 included the following 8 low-abundance biomarkers tested at a dilution of 1:3: Angiopoeitin-2 (Ang-2), sFlt-1, IL-6, IP-10, Ang-1, IL-8, sTREM-1, Granzyme B. The 5 biomarkers that did not overlap between the platforms are presented in S1 Table. Unfiltered plasma was diluted using diluents supplied by the manufacturer. Each 96-well plate included 7-fold serial dilutions of standards tested in duplicate and 72 patient samples, 8 of which were tested in duplicate. A total of 6 batches of Luminex Panel 1 and 2 were necessary to complete analysis of 410 samples. Assays were performed according to manufacturer’s magnetic Luminex® screening assay protocol [34 ]. Briefly, a microparticle cocktail, diluted plasma, and biomarker standards were added to a 96-well plate. Following a 2-hour incubation, plates were washed and a biotin antibody cocktail was added. After a 1-hour incubation, plates were washed and streptavidin-Phycoerythrin (PE) was added for 30-min, followed by a final wash and resuspension in wash buffer. All incubations were done at room temperature on a microplate shaker at 800 rpm. Plates were read immediately on the MAGPIX® instrument and raw data were analyzed using the xPONENT® software. Values outside the lower limit of quantification were assigned a value of 1/3 of the lower limit of the standard curve.
Leligdowicz A., Conroy A.L., Hawkes M., Zhong K., Lebovic G., Matthay M.A, & Kain K.C. (2017). Validation of two multiplex platforms to quantify circulating markers of inflammation and endothelial injury in severe infection. PLoS ONE, 12(4), e0175130.
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Publication 2017
ANGPT1 protein, human Biological Assay Biological Markers Biotin Buffers Cell-Derived Microparticles Combined Antibody Therapeutics Granzyme B Patients Phycoerythrin Plasma Post-gamma-Globulin Streptavidin Technique, Dilution
2
Uniplex IF Staining for Immune Markers
Cited 13 times
After chromogen-based IHC analysis was used for all of the targets, each target was assessed by a uniplex IF assay to optimize the antibodies and to generate spectral libraries required for multiplex IF image analysis. Uniplex IF staining was performed manually by using the Opal 7 kit (catalogue #NEL797001KT; PerkinElmer, Waltham, MA), which uses individual tyramide signal amplification (TSA)-conjugated fluorophores to detect various targets within an IF assay. After deparaffinization, slides were placed in a plastic container filled with antigen retrieval (AR) buffer in Tris-EDTA buffer (for CD4, CD3, granzyme B, and CD57 analysis) or citrate buffer (for analysis of the remaining markers); microwave technology (EZ-RETRIEVER® system microwave from BioGenex) was used to bring the liquid to the boiling point (1 min) at 100 °C, and the sections were then microwaved for an additional 15 min at 75 °C. Slides were allowed to cool in the AR buffer for 15 min at room temperature and were then rinsed with deionized water and 1 × Tris-buffered saline with Tween 20 (TBST; Santa Cruz Biotechnology, Dallas, TX). To initiate protein stabilization and background reduction, Tris-HCl buffer containing 0.1% Tween (Dako, catalogue #S3022) was used for 10 min at room temperature. Slides were then incubated between 30 min and 2 h (depending on which antibody was used at room temperature) with the same primary antibodies used for IHC analysis against the immune markers at specific dilutions: AE1/AE3 (dilution 1:300), PD-L1 (dilution 1:3000), CD4 (dilution 1:80), CD8 (dilution 1:120), CD3 (dilution 1:100), PD-1 (dilution 1:250), granzyme B (dilution 1:1), CD57 (dilution 1:10), CD45RO (dilution 1:1), FOXP3 (dilution 1:50), and CD68 (dilution 1:450). Next, the slides were washed and incubated for 10 min at room temperature with anti-mouse or anti-rabbit secondary antibodies (Novocastra, Leica Biosystems) after successive washes in TBST.
The slides were then incubated at room temperature for 10 min with one of the following Alexa Fluor tyramides (PerkinElmer) included in the Opal 7 kit to detect antibody staining, prepared according to the manufacturer’s instructions: Opal 520, Opal 540, Opal 570, Opal 620, Opal 650, and Opal 690 (dilution 1:50). After three additional washes in deionized water, the slides were counterstained with DAPI for 5 min and mounted with VECTASHIELD Hard Set (Vector Labs, Burlingame, CA). Autofluorescence (negative control) slides were also included, using primary and secondary antibodies and omitting the fluor tyramides. As performed with the IHC staining, the correct titration in the uniplex IF slides was chosen carefully to obtain a uniform, specific, and correct staining pattern. Similar to IHC validation, positive and negative controls were used during each run staining.
Parra E.R., Uraoka N., Jiang M., Cook P., Gibbons D., Forget M.A., Bernatchez C., Haymaker C., Wistuba I.I, & Rodriguez-Canales J. (2017). Validation of multiplex immunofluorescence panels using multispectral microscopy for immune-profiling of formalin-fixed and paraffin-embedded human tumor tissues. Scientific Reports, 7, 13380.
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Publication 2017
Anti-Antibodies Antibodies Antigens azo rubin S Biological Assay Buffers CD45RO Antigens CD274 protein, human Citrates Cloning Vectors DAPI Edetic Acid Granzyme B Immunoglobulins Mus Proteins Rabbits Saline Solution Technique, Dilution Titrimetry Tromethamine Tween 20 Tweens VPDA protocol
3
Predictive Biomarkers for Pediatric Septic Shock
Cited 13 times
The 12 candidate biomarkers (gene symbols) included: C-C chemokine ligand 3 (CCL3), C-C chemokine ligand 4 (CCL4), neutrophil elastase 2 (ELA2), granzyme B (GZMB), heat shock protein 70 kDa 1B (HSPA1B), interleukin 1α (IL1A), interleukin 8 (IL8), lipocalin 2 (LCN2), lactotransferrin (LTF), matrix metalloproteinase 8 (MMP8), resistin (RETN), and thrombospondin 1 (THBS1). These were selected from 117 gene probes demonstrating outcome predictive strength in microarray-based studies involving children with septic shock [18 (link),19 (link)]. The serum concentrations of the candidate biomarkers were measured using a multiplex magnetic bead platform (MILLIPLEX™ MAP) designed for this project by the EMD Millipore Corporation (Billerica, MA, USA). Biomarker concentrations were measured in a Luminex® 100/200 System (Luminex Corporation, Austin, TX, USA), according to the manufacturers' specifications. Assay performance data are provided in Additional File 1.
Wong H.R., Salisbury S., Xiao Q., Cvijanovich N.Z., Hall M., Allen G.L., Thomas N.J., Freishtat R.J., Anas N., Meyer K., Checchia P.A., Lin R., Shanley T.P., Bigham M.T., Sen A., Nowak J., Quasney M., Henricksen J.W., Chopra A., Banschbach S., Beckman E., Harmon K., Lahni P, & Lindsell C.J. (2012). The pediatric sepsis biomarker risk model. Critical Care, 16(5), R174.
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Publication 2012
austin beta-Chemokines Biological Assay Biological Markers Child Genes Granzyme B Heat-Shock Proteins 70 IL1A protein, human Interleukin-8 Lactoferrin Ligands Lipocalin-2 Microarray Analysis Neutrophil Collagenase neutrophil elastase, human Resistin Septic Shock Thrombospondin 1
4
Comprehensive Tumor Microenvironment Profiling in NSCLC
Cited 10 times
To measure the IHC expression of the different markers and quantify the
inflammatory cells expressing the slides, containing whole-tumor sections or
immunohistochemically stained TMA sections, were digitally scanned at
×200 magnification using a ScanScope Aperio AT Turbo slide scanner
(Leica Microsystems). The images were visualized using the ImageScope software
program (Leica Microsystems) and analyzed using the Aperio Image Toolbox and
GENIE image analysis tool (Leica Microsystems). The pathologist who performed
the image analysis was blinded to patients’ outcome. After training, the
software by a pathologist (Supplementary Fig. S1), membranous PD-L1 expression in malignant
epithelial cells and macrophages was analyzed using a cell membrane staining
algorithm, and the staining intensity scored as 0 (no staining), 1+
(weak staining), 2+ (moderate staining), or 3+ (strong staining)
and extension (percentage) of expression were determined (Fig. 1). The PD-L1 H-scores for tumor
tissues were determined by multiplying the staining intensity and reactivity
extension values (range, 0–300). The densities of cells expressing CD3,
CD4, CD8, CD57, granzyme B, CD45RO, PD-1, and FOXP3 were evaluated using the
Aperio nuclear algorithm and CD68 using Aperio cytoplasmic algorithm (Fig. 2 and Supplementary Fig. S2) and counting
the cells positive for them in 5 random square areas (1 mm2 each) in
both intratumoral and peritumoral compartments. While 5 intratumoral regions
were available in all cases and 24 tumors did not have peritumoral regions for
analysis. Histologic assessment of each 1 mm2 was performed to ensure
that tumor tissue (at least 80% malignant cells and tumor stroma) was
included in the selected intratumoral region, and only non-malignant cells were
included in the peritumoral compartment. For this analysis, each area examined
was overlapped with the sequential IHC slides to quantify each marker at the
same location of the tumor specimens. The average total number of cells positive
for each marker in the 5 square areas was expressed in density per
mm2. Similar to PD-L1 H-score from 5
intratumoral areas, the TMA was scored as the median PD-L1
H-score average of all cores from each case. In addition, as
has been proposed by Teng and colleagues (24 (link)), 4 different types tumor microenvironment we were able to
identify based on the density of TILs and the expression of PD-L1, as follows:
type I (adaptive immune resistance), type II (immunologic ignorance), type III
(intrinsic induction), and type IV (tolerance). Combining PD-L1 expression in
malignant cells (>5% was considered positive) with the density of
cells expressing CD3 using 3 levels (tertile) divided on the basis of regular
values of distribution by the statistical software (moderate and severe density
were considered positive), we were able to identify the frequency of those four
subtypes of tumor’ microenvironment in our NSCLC cases.
Parra E.R., Behrens C., Rodriguez-Canales J., Lin H., Mino B., Blando J., Zhang J., Gibbons D.L., Heymach J.V., Sepesi B., Swisher S.G., Weissferdt A., Kalhor N., Izzo J., Kadara H., Moran C., Lee J.J, & Wistuba I.I. (2016). Image Analysis–based Assessment of PD-L1 and Tumor-Associated Immune Cells Density Supports Distinct Intratumoral Microenvironment Groups in Non–small Cell Lung Carcinoma Patients. Clinical cancer research : an official journal of the American Association for Cancer Research, 22(24), 6278-6289.
Publication 2016
Acclimatization CD45RO Antigens CD274 protein, human Cells Cytoplasm Debility Granzyme B Immune Tolerance Lymphocytes, Tumor-Infiltrating Macrophage Neoplasms Non-Small Cell Lung Carcinoma Pathologists Patients Plasma Membrane Tissues Tumor Markers Tumor Microenvironment
5
Urine-based Molecular Biomarkers for Kidney Transplant
Cited 9 times
After transplantation, urine was collected on days 3, 7, 15, and 30 and in months 2, 3, 4, 5, 6, 9, and 12; as well as at the time of each kidney-allograft biopsy and 2 weeks thereafter. Urine-cell pellets were prepared at the clinical sites, stored at −80°C, and shipped to the Gene Expression Monitoring (GEM) Core at Weill Cornell Medical College, New York.
The staff at GEM Core isolated RNA from the pellets and assessed RNA quantity and purity (Table S3 in the Supplementary Appendix). Absolute levels of the mRNAs prespecified in the study protocol (CD3ε, perforin, granzyme B, proteinase inhibitor 9, CD103, IP-10, CXCR3, and transforming growth factor β1 [TGF-β1]) and 18S ribosomal RNA (rRNA) were quantified in preamplification-enhanced real-time quantitative polymerase-chain-reaction (PCR) assays with the use of oligonucleotide primers and TaqMan probes (Table S4 in the Supplementary Appendix) designed by the GEM Core, and the results (mRNA copies per microgram of total RNA and 18S rRNA copies [×10−6] per microgram of total RNA) were reported to the statistical analysis and clinical coordinating center. The staff members at GEM Core were unaware of the clinical information, including the results of kidney-allograft biopsies, before transfer of the mRNA data set to the statistical analysis and clinical coordinating center.
Urine specimens were classified as passing quality control if the 18S rRNA copy number was greater than or equal to 5×107 per microgram of total RNA isolated from the urine pellet and if the TGF-β1 mRNA copy number was greater than or equal to 100 copies per microgram of total RNA isolated from the urine pellet. If either threshold was not met, the specimen was classified as failing quality control.
Suthanthiran M., Schwartz J.E., Ding R., Abecassis M., Dadhania D., Samstein B., Knechtle S.J., Friedewald J., Becker Y.T., Sharma V.K., Williams N.M., Chang C.S., Hoang C., Muthukumar T., August P., Keslar K.S., Fairchild R.L., Hricik D.E., Heeger P.S., Han L., Liu J., Riggs M., Ikle D.N., Bridges N.D, & Shaked A. (2013). Urinary-Cell mRNA Profile and Acute Cellular Rejection in Kidney Allografts. The New England journal of medicine, 369(1), 20-31.
Publication 2013
Allografts alpha HML-1 Biological Assay Biopsy CD3E protein, human Cells CXCR3 protein, human Granzyme B Kidney Oligonucleotide Primers Pellets, Drug Perforin Protease Inhibitors Real-Time Polymerase Chain Reaction RNA, Messenger RNA, Ribosomal, 18S TGF-beta1 Transplantation Urine

Most recents protocols related to «Granzyme B»

1
Isolation and Analysis of Tumor-Infiltrating Lymphocytes
Tumors were treated as above and harvested at the indicated time points. For isolation of tumor-infiltrating lymphocytes, tumors were excised, then minced, and digested in wash media (RPMI 1640 supplemented with 5% fetal calf serum, Hepes, GlutaMAX, and Pen/Strep) with collagenase A (1 mg/ml) and deoxyribonuclease I (0.5 μg/ml) in a shaking incubator for up to 45 min at 37°C to achieve a single-cell suspension. Once a single-cell suspension was achieved, samples were washed and then either restimulated or stained for flow cytometry analysis. For cytokine staining and ex vivo restimulation with PMA and ionomycin, aliquots of tumor homogenates were incubated for 3 hours at 37°C in 10% complete RPMI (as above) with PMA (50 ng/ml), ionomycin (500 ng/ml), and brefeldin A (1 μg/ml) before flow cytometry staining. For cytokine staining and ex vivo restimulation with A20 idiotype peptide, aliquots of tumor homogenates were incubated for 5 hours at 37°C in 10% complete RPMI (as above) with the A20 idiotype peptide (DYWGQGTEL; 1 μg/ml) and brefeldin A (1 μg/ml) before staining for flow cytometry. Live/dead staining was performed via Ghost Dye Red 780 labeling (Tonbo Biosciences), as per the manufacturer’s protocol. Cells were then stained for flow cytometry, with intracellular staining performed using the Tonbo Foxp3/Transcription Factor Staining Buffer Kit per the manufacturer’s instructions. Antibodies used were anti-CD45 (clone 30-F11, BioLegend), NK1.1 (clone PD136, BD Biosciences), CD3e (clone 145-2C11, Tonbo Biosciences), TCRβ (clone H57-597, BD Biosciences), CD4 (clone RM4-5, BD Biosciences), CD8 (clone 53-6.7, Tonbo Biosciences), Foxp3 (clone FJK-16s, Thermo Fisher Scientific), CXCR6 (clone SA051D1, BioLegend), Granzyme-B (clone QA16A02, BioLegend), Ki-67 (clone SolA15, Thermo Fisher Scientific), IFN-γ (clone XMG1.2, Tonbo Biosciences), B220 (clone RA3-6B2, BD Biosciences), CD11c (clone N418, Tonbo Biosciences), Ly6G (clone 1A8, Tonbo Biosciences), CD11b (clone M1/70, Tonbo Biosciences), MHC-II (clone M5/114.15.2, Tonbo Biosciences), and CD103 (clone 2E7, BioLegend).
Savage T.M., Vincent R.L., Rae S.S., Huang L.H., Ahn A., Pu K., Li F., de los Santos-Alexis K., Coker C., Danino T, & Arpaia N. (2023). Chemokines expressed by engineered bacteria recruit and orchestrate antitumor immunity. Science Advances, 9(10), eadc9436.
Publication 2023
alpha HML-1 Antibodies Antigen T Cell Receptor, beta Chain Brefeldin A Buffers Cells Clone Cells collagenase 1 Cytokine Deoxyribonuclease I Fetal Bovine Serum Flow Cytometry Granzyme B HEPES Immunoglobulin Idiotypes Interferon Type II Ionomycin isolation ITGAM protein, human Lymphocytes, Tumor-Infiltrating Neoplasms Peptides Protoplasm Red Cell Ghost Streptococcal Infections Transcription Factor
2
Granzyme B Cleaves MSI-H Neoantigens
The ability of Granzyme B to cleave shared neoantigens present in MSI-H tumors was analyzed by the PROSPERous online tool (35 (link)). Briefly, shared neoantigens which are developed as frameshift peptides due to repeated mismatch repair deficiency provoking an immune response in independent patients with MSI-H tumors were selected based on the prior study of Ruodko et al. (7 (link)). The amino acid sequences of the selected neoantigens were subjected to the PROSPERous prediction algorithm using the P4-P2’ cleavage site and logistic regression options.
Grolmusz V.K., Nagy P., Likó I., Butz H., Pócza T., Bozsik A., Papp J., Oláh E, & Patócs A. (2023). A common genetic variation in GZMB may associate with cancer risk in patients with Lynch syndrome. Frontiers in Oncology, 13, 1005066.
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Publication 2023
Amino Acid Sequence Cytokinesis Frameshift Mutation Granzyme B Neoplasms Patients Peptides Response, Immune Turcot syndrome
3
Quantification of Immune Markers in Pancreatic Tumors
Panc02 tumors were extracted from sacrificed mice. Tumor tissue was placed in a 1.5 mL tube containing RIPA buffer (5 M NaCl, 0.5 M EDTA pH = 8, 1 M Tris pH = 8, 1% NP-40, 10% sodium deoxycholate, 10% SDS) and protease inhibitor cocktail (1:100, Sigma-Aldrich, St Louis, Missouri, USA). Stainless steel beads (SSB14B, Next Advance, New York, USA) were added and tumor tissue was homogenized using the Bullet Blender Tissue Homogenizer (Next Advance, Troy, NY) according to the manufacturer’s protocol. The homogenate was centrifuged and supernatant was collected. The protein concentration of the tumor lysates was determined using Protein Assay Dye Reagent Concentrate (Bio-Rad, California, USA). The quantification of Granzyme B, CXCL16 and CCL5 was carried out by a specific enzyme-linked immunosorbent assay (ELISA) kit (R&D Systems) in accordance with the manufacturers’ instructions. All experiments were performed using at least three biological repeats.
Vorontsova A., Cooper T.J., Haj-Shomaly J., Benguigui M., Levin S., Manobla B., Menachem R., Timaner M., Raviv Z, & Shaked Y. (2023). Chemotherapy-induced tumor immunogenicity is mediated in part by megakaryocyte-erythroid progenitors. Oncogene, 42(10), 771-781.
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Publication 2023
Biological Assay Biopharmaceuticals Buffers CCL5 protein, human Deoxycholic Acid, Monosodium Salt Edetic Acid Enzyme-Linked Immunosorbent Assay Granzyme B Mus Neoplasm Proteins Neoplasms Nonidet P-40 Protease Inhibitors Proteins Radioimmunoprecipitation Assay Sodium Chloride Stainless Steel Tissues Tromethamine
4
Comprehensive IHC Staining Protocol for Tissue Analysis
IHC staining was performed on 4 μm formalin-fixed paraffin-embedded tissue sections, which were incubated at 60 °C for 1 h and deparaffinized and rehydrated with xylene and graded alcohol. For antigen retrieval, the sections were performed with EDTA (pH 8.0) or citrate buffer (pH 6.0) at high temperature and pressure for 3 min and cooled down to room temperature. Tissue sections were blocked with 3% hydrogen peroxide methanol solution for 30 min at 37 °C to inactivate the endogenous peroxidase and then added with animal nonimmune serum for 30 min in a humid chamber at 37 °C, followed by incubation with the primary antibodies overnight at 4 °C, including anti-ATAD3A (NBP2-14881, Novus Biologicals), anti-PD-L1 (clone 28-8, Abcam; D5V3B, Cell Signaling Technology), anti-CD8a (D4W2Z, Cell Signaling Technology), anti-CD8 (clone C8/144B, MXB Biotechnologies), anti-granzyme B (D6E9W, Cell Signaling Technology), anti-Ki67 (clone SP6, Abcam). After washing with PBS three times, the sections were incubated with secondary antibody (Dako) for 30 min in a humid chamber at 37 °C. The sections were washed with PBS for three times and performed with Dako Real™ Envison kit for staining. IHC score was quantified using Image-Pro Plus software 6.0, determined by integrated optical density (IOD) value/area, three to five fields per section.
Xie X.Q., Yang Y., Wang Q., Liu H.F., Fang X.Y., Li C.L., Jiang Y.Z., Wang S., Zhao H.Y., Miao J.Y., Ding S.S., Liu X.D., Yao X.H., Yang W.T., Jiang J., Shao Z.M., Jin G, & Bian X.W. (2023). Targeting ATAD3A-PINK1-mitophagy axis overcomes chemoimmunotherapy resistance by redirecting PD-L1 to mitochondria. Cell Research, 33(3), 215-228.
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Publication 2023
Animals Antibodies Antigens Biological Factors Buffers CD274 protein, human Citrates Clone Cells Edetic Acid Ethanol Fever Formalin Granzyme B Immunoglobulins Methanol Novus Paraffin Embedding Peroxidase Peroxides Pressure Serum Tissues Tritium Vision Xylene
5
Multiparameter Flow Cytometry Analysis
Cells were labeled with fluorochrome-conjugated monoclonal Abs to the following antigens: anti–human CD3–PE (OKT3, Tonbo, Cytek Biosciences), CD4–PE–Cyanine7 (SK3, Tonbo, Cytek Biosciences), CD8–APC (Hit8a, Tonbo, Cytek Biosciences), CD34–Alexa Fluor 647 (581, BioLegend), CD69–PerCP–Cyanine5.5 (FN50, BioLegend), CD137–PE (4B4-1, Miltenyi Biotec), PD-1–BV650 (EH12.2H7, BioLegend), HLA-II–APC (Tü39, BioLegend), and anti–mouse TCRβ-APC (H57-597, Tonbo, Cytek Biosciences). Dead cells were stained with either DAPI or LIVE/DEAD Fixable Aqua (Invitrogen, Thermo Fisher Scientific). E629-38–HLA-A*02:01–PE tetramer was assembled and labeled by the NIH Tetramer Core Facility. Cells were stained with 1 μg/mL tetramer for 1 hour on ice. Ab staining for surface antigens was performed for 15 minutes on ice. For intracellular cytokine staining (ICS), T cells were cocultured with peptide-pulsed APCs for 4–6 hours in the presence of Brefeldin A. Cells were permeabilized and stained for intracellular cytokines with the Cytofix/Cytoperm Kit (BD Biosciences) after surface staining, according to manufacturer’s instructions. The following fluorochrome-conjugated Abs were used for cytokine staining: IFN-γ–APC (4S.B3, BioLegend), IL-2–FITC (MQ1-17H12, BioLegend), TNF-α–BV785 (Mab11, BioLegend), and Granzyme B–PE (QA16A02, BioLegend). Data were acquired with a FACSCelesta flow cytometer (BD Biosciences) and analyzed with FlowJo v10.7 software.
Brightman S.E., Naradikian M.S., Thota R.R., Becker A., Montero L., Bahmanof M., Premlal A.L., Greenbaum J.A., Peters B., Cohen E.E., Miller A.M, & Schoenberger S.P. (2023). Tumor cells fail to present MHC-II–restricted epitopes derived from oncogenes to CD4+ T cells. JCI Insight, 8(2), e165570.
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Publication 2023
Alexa Fluor 647 Antigens Antigen T Cell Receptor, beta Chain Atrial Premature Complexes Brefeldin A Cells Cytokine DAPI Fluorescein-5-isothiocyanate Fluorescent Dyes Granzyme B Homo sapiens Interferon Type II Muromonab-CD3 Mus Peptides Protoplasm Surface Antigens T-Lymphocyte Tetrameres TNFRSF9 protein, human Tumor Necrosis Factor-alpha

Top products related to «Granzyme B»

1
Foxp3 transcription factor staining buffer set by Thermo Fisher Scientific
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The Foxp3/Transcription Factor Staining Buffer Set is a laboratory product designed for the detection and analysis of intracellular transcription factors, such as Foxp3, using flow cytometry. The set includes the necessary buffers and reagents to facilitate the fixation, permeabilization, and staining of cells for the purpose of intracellular protein detection and quantification.
2
Cytofix cytoperm kit by BD
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The Cytofix/Cytoperm kit is a laboratory product designed for fixing and permeabilizing cells. It provides the necessary solutions for the preparation of samples prior to intracellular staining and flow cytometric analysis.
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Ionomycin is a laboratory reagent used in cell biology research. It functions as a calcium ionophore, facilitating the transport of calcium ions across cell membranes. Ionomycin is commonly used to study calcium-dependent signaling pathways and cellular processes.
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The LSRFortessa is a flow cytometer designed for multiparameter analysis of cells and other particles. It features a compact design and offers a range of configurations to meet various research needs. The LSRFortessa provides high-resolution data acquisition and analysis capabilities.
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GolgiStop is a cell culture reagent that inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus, thereby preventing the secretion of newly synthesized proteins. It is a useful tool for investigating protein trafficking and localization in cells.
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Cytofix cytoperm by BD
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Cytofix/Cytoperm is a fixation and permeabilization solution developed by BD for use in flow cytometry and immunohistochemistry applications. It is designed to facilitate the intracellular staining of proteins and other cellular components while preserving cellular structure and antigenicity.
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Phorbol myristate acetate (pma) by Merck Group
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The PMA is a versatile laboratory equipment designed for precision measurement and analysis. It functions as a sensitive pressure transducer, accurately measuring and monitoring pressure levels in various applications. The PMA provides reliable and consistent data for research and testing purposes.
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Facscalibur by BD
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The FACSCalibur is a flow cytometry system designed for multi-parameter analysis of cells and other particles. It features a blue (488 nm) and a red (635 nm) laser for excitation of fluorescent dyes. The instrument is capable of detecting forward scatter, side scatter, and up to four fluorescent parameters simultaneously.
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Lsrii flow cytometer by BD
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The BD LSRII flow cytometer is a multi-parameter instrument designed for advanced flow cytometry applications. It features a modular design that allows for customization to meet specific research needs. The LSRII utilizes laser excitation and sensitive detectors to analyze the physical and fluorescent properties of individual cells or particles passing through a fluid stream.

More about "Granzyme B"

Granzyme B (GzmB) is a serine protease primarily expressed in cytotoxic T lymphocytes (CTLs) and natural killer (NK) cells.
It plays a crucial role in inducing apoptosis (programmed cell death) in target cells during the immune response.
GzmB can trigger cell death through both caspase-dependent and caspase-independent pathways, making it an important effector molecule in cell-mediated cytotoxicity.
Accurate and reproducible protocols for studying GzmB are essential for advancing our understanding of its function in the immune system and its potential as a therapeutic target.
The Foxp3/Transcription Factor Staining Buffer Set and Cytofix/Cytoperm kit are commonly used to detect and analyze GzmB-expressing cells.
Ionomycin and phorbol 12-myristate 13-acetate (PMA) can be used to stimulate and activate CTLs and NK cells, leading to the upregulation of GzmB.
Flow cytometry, using instruments like the LSRFortessa or FACSCalibur, is a widely used technique to quantify and characterize GzmB-positive cells.
The GolgiStop and GolgiPlug reagents can be employed to inhibit the secretion of GzmB, allowing for its intracellular detection.
By leveraging the insights gained from the MeSH term description and the Metadescription, researchers can optimize their GzmB studies using AI-driven platforms like PubCompare.ai.
This tool can help locate the most reproducible and accurate protocols from literature, preprints, and patents, and facilitate seamless research through AI-powered comparisons of different protocols and products.
With the right tools and techniques, researchers can deepen their understanding of GzmB's role in the immune system and explore its potential as a therapeutic target.