• NatureRecombinant
  • SourceEscherichia coli
  • Amino Acid Sequence
    • SpeciesHuman
    • SequenceAmino acid sequencing indicates that the N-terminal methionine is removed during expression in Escherichia coli.
    • Amino acids1 to 172


Our Abpromise guarantee covers the use of ab58944 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    Functional Studies


  • Purity> 95 % SDS-PAGE.
    This protein was expressed in Escherichia coli then purified from the soluble fraction of disrupted cells. Detergents were not used in the purification process.
  • FormLiquid
  • Additional notesNo change in EC50 or dimerization has been observed in recombinant human Bcl2L2 that is stored at -20 °C.
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.

    Preservative: None
    Constituents: 10% Glycerol, 0.1M Potassium chloride, 25mM HEPES, pH 7.5

General Info

  • Alternative names
    • Apoptosis regulator BCL W
    • Apoptosis regulator Bcl-W
    • B2CL2_HUMAN
    • BCL 2 Like 2
    • Bcl 2 like 2 protein
    • Bcl 2L2
    • BCL W
    • Bcl-2-like protein 2
    • Bcl2 L2
    • BCL2 like 2
    • BCL2 like 2 protein
    • Bcl2-L-2
    • Bcl2l2
    • BCLW
    • KIAA0271
    • PPP1R51
    • Protein phosphatase 1 regulatory subunit 51
    see all
  • FunctionPromotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX.
  • Tissue specificityExpressed (at protein level) in a wide range of tissues with highest levels in brain, spinal cord, testis, pancreas, heart, spleen and mammary glands. Moderate levels found in thymus, ovary and small intestine. Not detected in salivary gland, muscle or liver. Also expressed in cell lines of myeloid, fibroblast and epithelial origin. Not detected in most lymphoid cell lines.
  • Sequence similaritiesBelongs to the Bcl-2 family.
  • DomainThe BH4 motif seems to be involved in the anti-apoptotic function.
    The BH1 and BH2 motifs form a hydrophobic groove which acts as a docking site for the BH3 domain of some pro-apoptotic proteins. The C-terminal residues of BCL2L2 fold into the BH3-binding cleft and modulate pro-survival activity by regulating ligand access. When BH3 domain-containing proteins bind, they displace the C-terminus, allowing its insertion into the membrane and neutralizing the pro-survival activity of BCL2L2.
  • Cellular localizationMitochondrion membrane. Loosely associated with the mitochondrial membrane in healthy cells. During apoptosis, tightly bound to the membrane.
  • Information by UniProt

References for Recombinant Human Bcl2L2 protein (ab58944)

ab58944 has not yet been referenced specifically in any publications.

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