CASP12 Research Reagents

Inactive caspase-12 is a protein in humans that is encoded by CASP12 gene. Has no protease activity. May reduce cytokine release in response to bacterial lipopolysaccharide during infections. Reduces activation of NF-kappa-B in response to TNF.

The following CASP12 reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.

CASP12 Antibodies

CASP12 Antibodies for Homo sapiens (Human)

CASP12 Antibodies for Mus musculus (Mouse)

CASP12 Proteins

CASP12 Proteins for Mus musculus (Mouse)

CASP12 Proteins for Homo sapiens (Human)

CASP12 Proteins for Rattus norvegicus (Rat)

CASP12 Background

The CASP12 encodes caspase-12, which is one of the inflammatory group caspases [1]. Caspase-12 is localized on the cytoplasmic side of the ER (endoplasmic-reticulum) membrane and is involved in the ER stress-induced apoptosis [2]. Crystal structure analysis found that a caspase-associated recruitment domain (CARD), two catalytic domains, p20, and p10 in caspase-12. In humans, the caspase-12 gene has a single nucleotide polymorphism that facilitates the synthesis of either a truncated or full-length caspase-12 protein [3]. When exposed to ER stresses, cytosolic calcium levels are increased, inducing the activation of m-calpain. Activated m-calpain cleaves Bcl-XL and proteolytically activates caspase-12 [4]. Takunari Yoneda et al. found that ER stress led to the dissociation of procaspase-12 from TRAF2 of the stable complex formed in unstressed cells and simultaneous dimerization (or oligomerization) of procaspase-12 [6]. Active caspase-12 translocates from the ER to the cytosol and activates caspase-9 independent of Apaf-1, followed by activation of caspase-3 [5]. The activation of executioner caspase-3 promotes the cleavage and degradation of downstream target molecules that are important for cellular survival, thus leading to apoptosis. Mice deficient in caspase-12 are resistant to ER stress-induced apoptosis, but their cells undergo apoptosis in response to other death stimuli. In addition to the essential role in apoptosis, caspase-12 also exerts roles in the inflammation. In humans, a caspase-12 isozyme functions as a dominant-negative regulator of the pro-inflammatory signaling pathway [7]. Because it inhibits the activation of caspase-1 in inflammasome complexes, blocks the production of the pro-inflammatory cytokines IL-1β and IL-18, and disturbs the overall response to sepsis.

[1] Martinon, F. and Tschopp, J. Inflammatory caspases: linking an intracellular innate immune system to autoinflammatory diseases [J]. Cell, 2004, 117, 561-574.
[2]Nakagawa, T., Zhu, H., et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta [J]. Nature, 2000, 403, 98-136-21842.
[3] Saleh, M., Vaillancourt, et al. Differential modulation of endotoxin responsiveness by human caspase-12 polymorphisms [J]. Nature, 2004, 429, 75-79.
[4]Nakagawa, T. and Yuan, J. Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis [J]. J. Cell Biol. 2000, 150, 887-894.7-894.
[5] Rao, R. V., Castro-Obregon, S., et al. Coupling endoplasmic reticulum stress to the cell death program. An Apaf-1-independent intrinsic pathway [J]. J. Biol. Chem. 2002, 277, 21836-21842.
[6] Takunari Yoneda,‖, Kazunori Imaizumi, et al. Activation of Caspase-12, an Endoplasmic Reticulum (ER) Resident Caspase, through Tumor Necrosis Factor Receptor-associated Factor 2-dependent Mechanism in Response to the ER Stress [J]. The Journal of Biological Chemistry, 2001,276, 13935-13940.
[7] Saleh, M., Vaillancourt, J. P., et al. Differential modulation of endotoxin responsiveness by human caspase-12 polymorphisms [J]. Nature, 2002, 429, 75-79.


Get all the latest information on Events, Sales and Offers. Sign up for newsletter today.

© 2007-2021 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1