抗Caspase-3 (CPP32 4-1-18)抗体 | Anti-Caspase-3 (CPP32 4-1-18) Antibody

• 価格
• Image
• Background

価格

目次に戻る

Image

	Western Blot: Caspase-3 Antibody (CPP32 4-1-18) [NB500-210] - Western blot detection of Caspase (19 and 35 kDa) from HEK293 cell extract using NB500-210. Lanes 1 and 2 contain inactive and active Caspase, respectively.
	Immunohistochemistry-Paraffin: Caspase-3 Antibody (CPP32 4-1-18) [NB500-210] - IHC analysis of a formalin fixed and paraffin embedded human spleen section using 1:200 dilution of Caspase-3 antibody (clone CPP32 4-1-18). The staining was developed using HRP conjugated anti-mouse secondary antibody and DAB reagent. This Caspase 3 antibody generated a specific staining in the cytoplasm of various spleenocytes.
	Immunohistochemistry-Paraffin: Caspase-3 Antibody (CPP32 4-1-18) [NB500-210] - Rat epithelial cells of the tongue base. Antigen retrieval method: Citrate buffer.
	Immunohistochemistry-Paraffin: Caspase-3 Antibody (CPP32 4-1-18) [NB500-210] - Caspase-3 was detected in immersion fixed paraffin-embedded sections of human bladder 1:300 dilution of mouse anti-Caspase-3 monoclonal (NB500-210, Novus Biologicals), for 1 hour at room temperature followed by anti-mouse IgG VisUCyte HRP polymer(VC001). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue).
	Simple Western: Caspase-3 Antibody (CPP32 4-1-18) [NB500-210] - Simple Western lane view shows a specific band for Caspase 3 in 0.5 mg/ml of Hek293 lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.

目次に戻る

Background

Caspase-3 is a cytoplasmic heterotetrameric cysteine protease involved in activating caspases cascade which is responsible for execution of apoptosis. It contains two anti-parallel arranged heterodimers (each one formed by a 17 kD nd a 12 kD subunit) and is involved in the cleavage/activation of caspases cascade (caspase-6, -7 and -9) responsible for apoptosis execution. Caspase-3's cleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits. Caspase-3 undergoes S-nitrosylization on its catalytic site cysteine in unstimulated cells where as it gets denitrosylated upon activation of the Fas apoptotic pathway, associated with an increased intracellular caspase activity. Moreover, at the onset of apoptosis, caspase-3 proteolytically cleaves PARP at a '216-Asp-|-Gly-217' bond, and also cleaves/activates SREBPs between bHLH zipper domain and the membrane attachment domain. It interacts with BIRC6/bruce also and is involved in the cleavage of huntingtin and triggers cell adhesion in sympathetic neurons through RET cleavage. Caspase-3 is an important marker of apoptosis which is implicated in several physiological and pathological processes.

目次に戻る