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Can promote mitochondrial permeability transition and facilitate necrotic cell death under different types of stress conditions. Additionally we are shipping Heme Binding Protein 2 Antibodies (41) and and many more products for this protein.
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The gene copy numbers and mRNA levels for both ALG-2 and HEBP2 are significantly upregulated in breast and lung cancer. Coexpression of ALG-2 and HEBP2 markedly increases the cytoplasmic pool of ALG-2 and alters the subcellular distribution of HEBP2. Abnormalities in the ALG-2/HEBP2 interaction impairs spindle orientation and positioning during mitosis.
There are important structural differences in the BH3 domain in the intact SOUL molecule and the same sequence bound to Bcl-xL.
SOUL can be a novel member of the BH3 domain-only proteins that cannot induce cell death alone but can facilitate both outer and inner mitochondrial membrane permeabilization and predominantly necrotic cell death in oxidative stress.
SOUL promotes necrotic cell death by inducing mitochondrial permeability transition
preliminary X ray structure
Results provide a better understanding of the target recognition mechanism and conformational change of SOUL in the interaction with ALG-2.
The heme-binding properties and coordination structure of SOUL protein are distinct from those of mouse liver p22HBP, despite high sequence homology.
Can promote mitochondrial permeability transition and facilitate necrotic cell death under different types of stress conditions. Does not bind hemin (By similarity). May have low affinity for heme.
heme-binding protein 2
, heme binding protein 2
, heme-binding protein 2-like
, SOUL/heme-binding protein
, placental protein 23
, putative heme-binding protein