Mouse Bcl-XL / BCL2L1(aa 1-212) Protein (His Tag)

BCL2-like 1 Protein Datasheet

BCL2L1(aa 1-212) / Bcl-XL Protein Product Information

• Synonym: RP23-106A3.4, Bcl(X)L, Bcl-XL, Bcl-Xs, Bcl2l, BclX, MGC113803, MGC99998, bcl-x
• Protein Construction: A DNA sequence encoding the mouse BCL2L1 (Q64373-1) (Met 1- Arg 212 ) was expressed, with a C-terminal polyhistidine tag.
• Source: Mouse
• Expression Host: E.coli

BCL2L1(aa 1-212) / Bcl-XL Protein QC Testing

• Purity: > 95 % as determined by SDS-PAGE.
• Bio-activity: 1. Measured by its binding ability in a functional ELISA.
  2. Immobilized human BID at 10 μg/mL (100 μl/well) can bind biotinylated mouse BCL2L1, The EC50 of biotinylated mouse BCL2L1 is 5.6 ng/mL.
  3. Immobilized mouse BID at 10 μg/mL (100 μl/well) can bind biotinylated mouse BCL2L1, The EC50 of biotinylated mouse BCL2L1 is 7.1 ng/mL.
• Endotoxin: Please contact us for more information.
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Met 1
• Molecular Mass: The recombinant mouse BCL2L1 comprises 222 amino acids and has a calculated molecular mass of 25.2 kDa. It migrates as an approximately 33 kDa band in SDS-PAGE under reducing conditions.
• Formulation: Lyophilized from 0.2μm filtered solution of PBS, pH7.5
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: BCL2L1(aa 1-212) / Bcl-XL protein

BCL2L1(aa 1-212) / Bcl-XL Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

BCL2L1(aa 1-212) / Bcl-XL Protein Description

The crystal and solution structures of a Bcl-2 family member, Bcl-xL is like this: The structures consist of two central, primarily hydrophobic α-helices, which are surrounded by amphipathic helices. A 60-residue loop connecting helices αl and α2 was found to be flexible and non-essential for anti-apoptotic activity. Bcl-xL is chareacterized as important factors in autophagy, inhibiting Beclin 1-mediated autophagy by binding to Beclin 1. In addition, Beclin 1, Bcl-2 and Bcl-xL can cooperate with Atg5 or Ca²⁺ to regulate both autophagy and apoptosis. Thus, Bcl-2 and Bcl-xL represent a molecular link between autophagy and apoptosis. Bcl-xL is also implicated in anoxia induced cell death. Key regulators of apoptosis during anoxia are the Bcl-2 family of proteins. The pathway is initiated by the loss of function of the prosurvival Bcl-2 family members Mcl-1 and Bcl-2/Bcl-XL, resulting in Bax- or Bak-dependent release of cytochrome c and subsequent caspase-9-dependent cell death. Thus, Bcl-xL, the well-characterized apoptosis guards, appears to be an inhibitor in cell death.

References

1. Muchmore SW. et al., 1996, Nature. 381: 335-41.
2. Shroff EH. et al., 2007, Antioxid Redox Signal. 9 (9) :1405-9.
3. Zhou F. et al., 2011, FEBS J. 278 (3): 403-13.