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AB151924

Recombinant Human Bcl-XL protein

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Recombinant Human Bcl-XL protein is a Human Fragment protein, in the 1 to 212 aa range, expressed in Escherichia coli, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, HPLC.

View Alternative Names

BCL2L, BCLX, BCL2L1, Bcl-2-like protein 1, Bcl2-L-1, Apoptosis regulator Bcl-X

Key facts

Purity

>95% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

Escherichia coli

Tags

His tag C-Terminus

Applications

HPLC, SDS-PAGE

applications

Biologically active

No

Accession

Q07817

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 20% Glycerol (glycerin, glycerine), 0.48% HEPES, 0.37% Potassium chloride

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "HPLC": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNR","proteinLength":"Fragment","predictedMolecularWeight":"23.8 kDa","actualMolecularWeight":null,"aminoAcidEnd":212,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q07817","tags":[{"tag":"His","terminus":"C-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Bcl-XL also known as Bcl-xL or Bcl-Xl protein is a member of the Bcl-2 protein family playing an important role in regulating cell death. Bcl-XL inhibits apoptosis by binding to pro-apoptotic proteins preventing the release of cytochrome c from mitochondria. This protein has a molecular weight of approximately 30 kDa. Bcl-xL is widely expressed in tissues notably in the brain endothelial cells and hematopoietic tissues where it contributes to cell survival.
Biological function summary

This protein acts as an anti-apoptotic molecule within the mitochondria and is part of the Bcl-2 family complex. Bcl-XL modulates the balance between pro-apoptotic and anti-apoptotic signals impacting cell fate. By binding and sequestering pro-apoptotic members such as Bax and Bak Bcl-XL prevents mitochondrial outer membrane permeabilization important for avoiding programmed cell death. This function not only supports cellular longevity but also understanding cancer cell survival.

Pathways

The Bcl-XL protein holds a significant position in the apoptotic signaling pathways. It is particularly involved in the intrinsic pathway where its interactions with mitochondrial proteins Bax and Bak determine cell survival or death. It is interconnected with the PI3K/AKT pathway where AKT kinase activity can upregulate Bcl-XL expression demonstrating how survival signals are transmitted. These interactions highlight its pivotal role in balancing life and death at the cellular level.

Bcl-XL's overexpression often connects to the progression of cancers and resistance to chemotherapy. By inhibiting programmed cell death Bcl-XL allows cancer cells to evade traditional treatments. Furthermore research implicates Bcl-XL in neurodegenerative disorders where its interaction with Bcl-2 proteins disrupts normal apoptotic processes contributing to cellular dysfunction and disease. Understanding Bcl-XL's disease-related roles furthers the development of targeted therapies combating its protective effects in pathological contexts.
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Specifications

Form

Liquid

Additional notes

Purity is greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE.

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General info

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 F(1)F(0) 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.

Sequence similarities

Belongs to the Bcl-2 family.

Post-translational modifications

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.

Subcellular localisation

Mitochondrion inner membrane

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Product protocols

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Target data

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 F(1)F(0) 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.
See full target information BCL2L1
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