Bcl-2 Protein
Bcl-2 Protein - Related Videos
11:24
Direct Protein Delivery to Mammalian Cells Using Cell-permeable Cys2-His2 Zinc-finger Domains
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Cited by 14 •
2015
Zinc-finger domains are intrinsically cell-permeable and capable of mediating protein delivery into a broad range of mammalian cell types. Here, a detailed step-by-step protocol for implementing zinc-finger technology for intracellular protein delivery is presented.
08:23
2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes
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Cited by 10 •
2018
Protein-protein and protein-metabolite interactions are crucial for all cellular functions. Herein, we describe a protocol that allows parallel analysis of these interactions with a protein of choice. Our protocol was optimized for plant cell cultures and combines affinity purification with mass spectrometry-based protein and metabolite detection.
10:26
Photopatterning Proteins and Cells in Aqueous Environment Using TiO2 Photocatalysis
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Cited by 2 •
2015
We describe a protocol for modifying cell affinity of a scaffold surface in aqueous environment. The method takes advantage of titanium dioxide photocatalysis to decompose organic film in the photo-irradiated region. We show that it can be used to create microdomains of scaffolding proteins, both ex situ and in situ.
08:31
Total Protein Extraction and 2-D Gel Electrophoresis Methods for Burkholderia Species
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Cited by 2 •
2013
Members of the Burkholderia genus are pathogens of clinical importance. We describe a method for total bacterial protein extraction, using mechanical disruption, and 2-D gel electrophoresis for subsequent proteomic analysis.
![Protein Film Infrared Electrochemistry Demonstrated for Study of H<sub>2</sub> Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg%3Fv%3D2026-09-28%252016%253A08%253A49&w=750&q=75)
10:01
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
0 Views •
Cited by 10 •
2017
Here, we describe a technique, protein film infrared electrochemistry, which allows immobilized redox proteins to be studied spectroscopically under direct electrochemical control at a carbon electrode. Infrared spectra of a single protein sample can be recorded at a range of applied potentials and under a variety of solution conditions.
FAQs
Bcl-2 binds pro-apoptotic members of the Bcl-2 family at the mitochondrial outer membrane and inhibits their activity. This restraint limits mitochondrial membrane permeabilization, a key event that would otherwise allow cytochrome c to leave the mitochondria. By restricting cytochrome c release, Bcl-2 reduces activation of the caspases that execute programmed cell death.
Mitochondrial membrane permeabilization connects regulation by Bcl-2 family proteins to downstream apoptotic execution. When this membrane barrier remains intact, cytochrome c stays within the mitochondria and caspase activation is limited. Bcl-2 therefore acts at an early decision point, influencing whether intracellular death signaling progresses rather than merely affecting the final stages of cell disassembly.
Abnormally high or otherwise dysregulated Bcl-2 expression can suppress the pro-apoptotic signals that would normally eliminate damaged cells. Continued inhibition of mitochondrial membrane permeabilization reduces cytochrome c release and downstream caspase activation. In cancer biology, this survival advantage may allow malignant cells to remain viable despite signals that would ordinarily promote programmed cell death.
Bcl-2 serves as a biomarker because its expression provides information about the survival-apoptosis balance within cells. In a medical or cancer-biology context, detecting abnormal Bcl-2 expression can help identify a cellular state associated with reduced apoptotic signaling and persistence of damaged or malignant cells. Its value comes from linking molecular status with cell survival behavior.
Bcl-2 inhibitors are designed to counter the protein’s survival function rather than reinforce it. By reducing Bcl-2-mediated inhibition of pro-apoptotic family members, these drugs can help restore mitochondrial apoptotic signaling, including the pathway leading toward cytochrome c release and caspase activation. This approach is relevant to selected cancers in which abnormal survival signaling contributes to disease persistence.
Bcl-2 has dual clinical relevance when its abnormal expression is associated with cancer-cell survival. As a biomarker, it can indicate disruption of apoptotic regulation. As a therapeutic target, it identifies a survival function that drugs may inhibit to re-enable programmed cell death. Considering both roles connects molecular assessment with treatment strategies aimed at selected cancers.