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Mouse Anti-BCL2L1 Recombinant Antibody (2H12) (CBMAB-AP593LY)


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Published Data
Mouse Anti-BCL2L1 Recombinant Antibody (2H12) (CBMAB-AP593LY) in WB
Protein expression of cleaved PARP1, PARP1, BAK, and BCL-XL as examined by Western blot analysis. Values indicate means ± SEM. (n = 3, ** p ≤ 0.01, *** p ≤ 0.001). ...View More
Pham, C. H., Lee, J. E., Yu, J., Lee, S. H., Yu, K. R., Hong, J., ... & Yoo, H. M. (2021). Anticancer effects of propionic acid inducing cell death in cervical cancer cells. Molecules, 26(16), 4951.
Mouse Anti-BCL2L1 Recombinant Antibody (2H12) (CBMAB-AP593LY) in Immunoblot
IB showing the expression of BCL-2 and BCL-xL in sorted EGFP þ Ramos B cells transduced with the indicated vectors and stimulated with anti-IgM (25 mg ml-1) for 48 h. ...View More
Wu, J. L., Wu, H. Y., Tsai, D. Y., Chiang, M. F., Chen, Y. J., Gao, S., ... & Lin, K. I. (2016). Temporal regulation of Lsp1 O-GlcNAcylation and phosphorylation during apoptosis of activated B cells. Nature Communications, 7(1), 12526.
Mouse Anti-BCL2L1 Recombinant Antibody (2H12) (CBMAB-AP593LY) in WB
Depletion of TCERG1 decreases the level of Bcl-xL protein in cells upon staurosporine treatment. Cell extracts from control and TCERG1 knockdown (KD) Jurkat cells with (+STAU) or without treatment with 0.5 μM staurosporine (-STAU) for 1 h were analyzed by immunoblotting with specific antibodies against TCERG1, Bcl-x, Bcl-2, and β-actin. The quantification of the bands is shown below each panel. ...View More
Montes, M., Coiras, M., Becerra, S., Moreno-Castro, C., Mateos, E., Majuelos, J., ... & Suñé, C. (2015). Functional consequences for apoptosis by transcription elongation regulator 1 (TCERG1)-mediated Bcl-x and Fas/CD95 alternative splicing. PLoS One, 10(10), e0139812.
Mouse Anti-BCL2L1 Recombinant Antibody (2H12) (CBMAB-AP593LY) in WB
Bcl-2 and Bcl-xL are upregulated in docetaxel-resistant cell lines. Treatment with RU-486 (3 mM) reverses the elevated expression of Bcl-2 and Bcl-xL in docetaxel-resistant prostate cancer cells. ...View More
Kroon, J., Puhr, M., Buijs, J. T., Van Der Horst, G., Hemmer, D. M., Marijt, K. A., ... & Van Der Pluijm, G. (2016). Glucocorticoid receptor antagonism reverts docetaxel resistance in human prostate cancer. Endocrine-related cancer, 23(1), 35-45.

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
2H12
Antibody Isotype
IgG2a, κ
Application
WB, IP, IHC-P, IF

Basic Information

Immunogen
N-terminal peptide (amino acids 3-14) common to human and mouse Bcl-xL and Bcl-xS.
Host Species
Mouse
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)1:50-1:500
IHC-P1:50-1:500

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.05% BSA
Preservative
0.05% sodium azide
Concentration
0.2 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
BCL2 Like 1
Introduction
The protein encoded by this gene belongs to the BCL-2 protein family. BCL-2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. The proteins encoded by this gene are located at the outer mitochondrial membrane, and have been shown to regulate outer mitochondrial membrane channel (VDAC) opening. VDAC regulates mitochondrial membrane potential, and thus controls the production of reactive oxygen species and release of cytochrome C by mitochondria, both of which are the potent inducers of cell apoptosis. Alternative splicing results in multiple transcript variants encoding two different isoforms. The longer isoform acts as an apoptotic inhibitor and the shorter isoform acts as an apoptotic activator. [provided by RefSeq, Dec 2015]
Entrez Gene ID
397536
UniProt ID
Q9N1A2
Alternative Names
BCL2 Like 1; Protein Phosphatase 1, Regulatory Subunit 52; Apoptosis Regulator Bcl-X; BCL2L; BCLX; Bcl-2-Like Protein 1;
Function
Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis.
Isoform Bcl-X(L) also regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F1F0 activity and regulates endocytic vesicle retrieval in hippocampal neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles. May attenuate inflammation impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (PubMed:17418785).
Isoform Bcl-X(S) promotes apoptosis.
Biological Process
Apoptotic mitochondrial changes Source: ProtInc
Cytokine-mediated signaling pathway Source: Reactome
Defense response to virus Source: DIBU
Endocytosis Source: UniProtKB-KW
Extrinsic apoptotic signaling pathway in absence of ligand Source: GO_Central
Intrinsic apoptotic signaling pathway in response to DNA damage Source: GO_Central
MAPK cascade Source: Reactome
Mitotic cell cycle checkpoint Source: UniProtKB
Negative regulation of anoikis Source: UniProtKB
Negative regulation of apoptotic process Source: UniProtKB
Negative regulation of autophagy Source: UniProtKB
Negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Source: UniProtKB
Negative regulation of execution phase of apoptosis Source: UniProtKB
Negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
Negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: MGI
Negative regulation of intrinsic apoptotic signaling pathway Source: BHF-UCL
Negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage Source: BHF-UCL
Negative regulation of protein localization to plasma membrane Source: BHF-UCL
Negative regulation of release of cytochrome c from mitochondria Source: BHF-UCL
Positive regulation of intrinsic apoptotic signaling pathway Source: Reactome
Regulation of cytokinesis Source: UniProtKB
Regulation of mitochondrial membrane permeability Source: HGNC-UCL
Regulation of mitochondrial membrane potential Source: HGNC-UCL
Release of cytochrome c from mitochondria Source: HGNC-UCL
Response to cytokine Source: MGI
Suppression by virus of host apoptotic process Source: MGI
Cellular Location
Isoform Bcl-X(L): Centrosome; Mitochondrion inner membrane; Mitochondrion outer membrane; Mitochondrion matrix; Cytosol; Nucleus membrane; Synaptic vesicle membrane. After neuronal stimulation, translocates from cytosol to synaptic vesicle and mitochondrion membrane in a calmodulin-dependent manner (By similarity). Localizes to the centrosome when phosphorylated at Ser-49.
Topology
Helical: 210-226 aa
PTM
Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity.
Phosphorylated on Ser-62 by CDK1. This phosphorylation is partial in normal mitotic cells, but complete in G2-arrested cells upon DNA-damage, thus promoting subsequent apoptosis probably by triggering caspases-mediated proteolysis. Phosphorylated by PLK3, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Phosphorylation at Ser-49 appears during the S phase and G2, disappears rapidly in early mitosis during prometaphase, metaphase and early anaphase, and re-appears during telophase and cytokinesis.
Ubiquitinated by RNF183 during prolonged ER stress, leading to degradation by the proteosome.
More Infomation

Yang, Z., An, Y., Wang, N., Dong, X., & Kang, H. (2020). LINC02595 promotes tumor progression in colorectal cancer by inhibiting miR‐203b‐3p activity and facilitating BCL2L1 expression. Journal of cellular physiology, 235(10), 7449-7464.

Lizárraga-Verdugo, E., Ruiz-García, E., Lopez-Camarillo, C., Bermúdez, M., Avendaño-Félix, M., Ramos-Payán, R., ... & Aguilar-Medina, M. (2020). Cell survival is regulated via SOX9/BCL2L1 Axis in HCT-116 colorectal cancer cell line. Journal of oncology, 2020.

O'Hara, S. P., Splinter, P. L., Trussoni, C. E., Guicciardi, M. E., Splinter, N. P., Al Suraih, M. S., ... & LaRusso, N. F. (2019). The transcription factor ETS1 promotes apoptosis resistance of senescent cholangiocytes by epigenetically up-regulating the apoptosis suppressor BCL2L1. Journal of Biological Chemistry, 294(49), 18698-18713.

Duan, S., Yu, S., Yuan, T., Yao, S., & Zhang, L. (2019). Exogenous let-7a-5p induces A549 lung cancer cell death through BCL2L1-mediated PI3Kγ signaling pathway. Frontiers in oncology, 9, 808.

Zhang, H., Zong, Y., Qiu, G., Jia, R., Xu, X., Wang, F., & Wu, D. (2018). Silencing Lin28 promotes apoptosis in colorectal cancer cells by upregulating let‑7c targeting of antiapoptotic BCL2L1. Molecular medicine reports, 17(4), 5143-5149.

Cai, J., Liu, T., Jiang, X., Guo, C., Liu, A., & Xiao, X. (2017). Downregulation of USP18 inhibits growth and induces apoptosis in hepatitis B virus-related hepatocellular carcinoma cells by suppressing BCL2L1. Experimental cell research, 358(2), 315-322.

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For research use only. Not intended for any clinical use.

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