How does Bcl-xL work?

How does Bcl-xL work?

Bcl-xL inhibits the activation of Bax and Bak, preventing a loss of mitochondrial outer membrane (MOM) integrity and release of cytochrome c into the cytoplasm. Therefore, the Bcl-xL isoform is anti-apoptotic.

Where is Bcl-xL located?

mitochondrion
Bcl-2 is located at the mitochondrion, endoplasmic reticulum (ER) and the nuclear envelope [14, 15]. Bcl-XL resides in the nuclear envelope, extra-nuclear membranes, including the mitochondrion but also cytosol [16, 17].

Does BCL-xL inhibit apoptosis?

These data suggest that Bcl-xL may prevent or at least delay apoptosis in the presence of Fas-activated proteases. The ability of Bcl-xL to protect cells from death following a substantial amount of PARP cleavage was not unique to Jurkat T cells.

What does Bcl-xL stand for?

B-cell lymphoma-extra large
B-cell lymphoma-extra large (Bcl-xL), encoded by the BCL2-like 1 gene, is a transmembrane molecule in the mitochondria.

What is the intrinsic pathway of apoptosis?

The intrinsic apoptosis pathway is initiated by, for example, chemotherapy and/or radiotherapy. It is activated by a range of exogenous and endogenous stimuli, such as DNA damage, ischemia, and oxidative stress. Moreover, it plays an important function in development and in the elimination of damaged cells.

What is the Bcl-2 pathway?

BCL-2 family proteins are the regulators of apoptosis, but also have other functions. This family of interacting partners includes inhibitors and inducers of cell death. Together they regulate and mediate the process by which mitochondria contribute to cell death known as the intrinsic apoptosis pathway.

How Bcl-2 family proteins regulate the intrinsic pathway of apoptosis?

BCL2 prevents BAX/BAK oligomerization, which would otherwise lead to the release of several apoptogenic molecules from the mitochondrion. It is also known that BCL2 binds to and inactivates BAX and other pro-apoptotic proteins, thereby inhibiting apoptosis.

Is bad pro-apoptotic?

The BCL2 associated agonist of cell death (BAD) protein is a pro-apoptotic member of the Bcl-2 gene family which is involved in initiating apoptosis. BAD is a member of the BH3-only family, a subfamily of the Bcl-2 family.

How do you test for Bcl-xL (54h6)?

Resuspend cells in 200-500 µl of 1X PBS and analyze on flow cytometer. Bcl-xL (54H6) Rabbit mAb detects endogenous levels of total Bcl-xL protein. The antibody does not cross-react with other Bcl-2 family members.

What is the lysate control for Bcl-xL antibody?

Immunoprecipitation of Bcl-xL from Jurkat cell extracts, using Bcl-xL Antibody. Lane 1 is the lysate control; lane 2 is antibody alone and lane 3 is antibody plus lysate.

How does Bcl-xL prevent apoptosis?

Bcl-xL prevents apoptosis through two different mechanisms: heterodimerization with an apoptotic protein inhibits its apoptotic effect (1,2) and formation of mitochondrial outer membrane pores help maintain a normal membrane state under stressful conditions (3).

What is the difference between Bcl-xL (54h6) and α-tubulin (11h10) Mab?

The Bcl-xL (54H6) Rabbit mAb confirms silencing of Bcl-xL expression, while the α-Tubulin (11H10) Rabbit mAb is used as a loading control. Immunoprecipitation of Bcl-xL from Jurkat cell extracts, using Bcl-xL (54H6) Rabbit mAb.