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Caspase Antibodies

Antibody Image LS-B3341
Anti-Caspase-9 antibody LS-B3741

Caspases, or Cysteine Aspartate-specific Proteases, are enzymes involved in the signal transduction pathways of apoptosis and inflammation. Caspases are produced in cells as catalytically inactive zymogens which experience proteolytic processing at conserved aspartic residues. Upon cleavage, they produce a large and a small subunit that dimerize to form the active enzyme. The sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. There are two types of apoptotic caspases, initiator (apical) caspases and effector (executioner) caspases. Initiator caspases, such as Caspase-2, -8, -9, and -10, cleave inactive pro-forms of effector caspases, thereby activating them. Effector caspases, such as Caspase-3, -6, and -7, in turn cleave other protein substrates within the cell, to trigger the apoptotic process. The initiation of this cascade reaction is regulated by caspase inhibitors. Caspase-4 and Caspase-5, which are overexpressed in some cases of vitiligo and associated autoimmune diseases caused by NALP1 variants, are not currently classified as initiator or effector in MeSH, because they are inflammatory enzymes that, in concert with Caspase-1, are involved in T-cell maturation. Caspase-14 is not involved in apoptosis or inflammation, but instead is involved in skin cell development.

Caspase antibodies are available from LSBio for all 12 caspases that have been identified in humans. Caspase antibodies are used in many applications, particularly in immunohistochemistry to detect activation of Caspase-3 in apoptosis.

[More about Caspases]


Antibody Image LS-B112
Anti-Caspase-1 antibody LS-B112

Caspase-1 (CASP1)

Caspase-1, also called interleukin-1 beta converting enzyme, is a cysteine C14 endopeptidase able to process pro-interleukin-1 beta into its active form. Caspase-1 is identical to Caenorhabditis elegans cell death gene ced-3 and may be involved in apoptotic signaling. Inhibition of Caspase-1 in mice models extended survival and delayed appearance of neuronal inclusions and symptoms of Huntington's Disease.

[Caspase-1 Antibodies]

Antibody Image LS-B475
Anti-Caspase-2 antibody LS-B475

Caspase-2 (CASP2)

Although phylogenetically similar to members of the Caspase inflammatory subfamily, Caspase-2 is thought to be involved in stress-induced apoptosis. Caspase-2 has two major isoforms; overexpression on the long form results in apoptosis while that of the short form suppresses cell death.

[Caspase-2 Antibodies]

Antibody Image LS-B3404
Anti-Caspase-3 antibody LS-B3404

Caspase-3 (CASP3)

Caspase-3 is synthesized as an inactive proenzyme that undergoes proteolytic cleavage to produce 2 subunits, termed p20 and p11. These subunits dimerize to form the active enzyme. Caspase-3 proteolytically cleaves and activates other proteins. Caspase-3 has been associated with apoptosis.

[Caspase-3 Antibodies]

Antibody Image LS-B710
Anti-Caspase-4 antibody LS-B710

Caspase-4 (CASP4)

Caspase-4 is a member of the inflammatory subfamily of Caspases, and was initially identified as a homologous protein to Caspase-1 and the C. elegans Ced-3 which could induce apoptosis in transfected cells. More recent studies have shown that it can be activated by ER stress and has been suggested to be involved in multiple neuronal pathologies such as Alzheimer's disease.

[Caspase-4 Antibodies]

Antibody Image LS-B476
Anti-Caspase-5 antibody LS-B476

Caspase-5 (CASP5)

Caspase-5 is a member of the inflammatory subfamily of Caspases, and can interact with Caspase-1; both are constituents of the NALP1 inflammasome, a complex that can trigger the cleavage of pro-IL-1b. Expression of Caspase-5 can be regulated by lipopolysaccharide (LPS) and IFN-g.

[Caspase-5 Antibodies]

Antibody Image LS-B1345
Anti-Caspase-6 antibody LS-B1345

Caspase-6 (CASP6)

Caspase-6 is an executioner Caspase of the apoptotic subfamily of Caspases that was identified based on its homology with human Caspases-2 and -3, as well as the C. elegans cell death protein CED-3. It possesses two isoforms, of which only the longer form possesses protease activity. Caspase-6 is highly expressed in adult brain and may play a role in several neuronal pathologies.

[Caspase-6 Antibodies]

Antibody Image LS-B3670
Anti-Caspase-7 antibody LS-B3670

Caspase-7 (CASP7)

Caspase-7 is an executioner Caspase of the apoptotic subfamily of Caspases that was identified based on its homology with Caspases -1 and -3, as well as the C. elegans cell death protein CED-3. Alternative splicing of Caspase-7 mRNA results in the production of 3 distinct isoforms. Caspase-7 activity can be directly inhibited by XIAP expression.

[Caspase-7 Antibodies]

Antibody Image LS-B3796
Anti-Caspase-8 antibody LS-B3796

Caspase-8 (CASP8)

Caspase-8 is an initiator Caspase of the apoptotic subfamily of Caspases that was identified as a member of the Fas/APO-1 death-inducing signaling complex. The adaptor molecule FADD couples procaspase-8 to the Fas receptor death domain; subsequent oligomerization promotes procaspase-8 autoactivation. FLIP, a catalytically inactive Caspase-8-like molecule inhibits these interactions and thus can inhibit apoptosis.

[Caspase-8 Antibodies]

Antibody Image LS-B3741
Anti-Caspase-9 antibody LS-B3741

Caspase-9 (CASP9)

Caspase-9 is a cysteine C14 endopeptidase that mediates oncogene and drug-induced apoptosis. It is activated upon binding to Apaf-1/cytochrome c and inhibited upon phosphorylation by the serine/ threonine kinase Akt. Activated caspase-9 cleaves downstream Caspases such as Caspase-3, -6 and -7 initiating the Caspase cascade. Like other Caspases, Caspase-9 plays a critical role in mediating apoptosis during normal brain development. Caspase-9 also cleaves amyloid beta-protein precursors, principal constituent of senile plaques, and is involved in neuronal death observed in Alzheimer disease.

[Caspase-9 Antibodies]

Antibody Image LS-C49364
Anti-Caspase-10 antibody LS-C49364

Caspase-10 (CASP10)

Caspase-10 cleaves and activates Caspases -3 and -7, and the protein itself is processed by Caspase-8. Mutations in this gene are associated with apoptosis defects seen in type II autoimmune lymphoproliferative syndrome. Three alternatively spliced transcript variants encoding different isoforms have been described for this gene.

[Caspase-10 Antibodies]

Antibody Image LS-B747
Anti-Caspase-12 antibody LS-747

Caspase-12 (CASP12)

Caspase-12 is involved in the apoptosis triggered by a stress on the endoplasmic reticulum. Caspase-12 is co-localized to the ER with several proteins that are involved in Alzheimer's disease including gamma-secretase presenilin and beta-amyloid precursor protein (APP). Caspase-12 mediates cytotoxicity induced by amyloid-beta. Caspase-12 activation results in cell death in the absence of the cytochrome c-dependent pathway. Recently Caspase-12 has been suggested to affect signaling pathways linking some G-protein coupled receptors to alphaIIbbeta3 activation. Caspase-12 is ubiquitously expressed in mouse tissues.

[Caspase-12 Antibodies]

Antibody Image LS-B474
Anti-Caspase-14 antibody LS-B474

Caspase 14 (CASP14)

Caspase-14 has been shown to be processed and activated by Caspase-8 and Caspase-10 in vitro, and by anti-Fas agonist antibody or TNF-related apoptosis inducing ligand in vivo. The expression and processing of this Caspase may be involved in keratinocyte terminal differentiation, which is important for the formation of the skin barrier.

[Caspase-14 Antibodies]


More about Caspases

Caspases, or Cysteine Aspartate-specific Proteases, are enzymes involved in the signal transduction pathways of apoptosis and inflammation. Caspases are produced in cells as catalytically inactive zymogens which experience proteolytic processing at conserved aspartic residues. Upon cleavage, they produce 2 subunits, large and small, that dimerize to form the active enzyme. The sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. There are more than 400 caspases so far identified, and they are divided into two major classes: effectors and initiators.

Effector Caspases:

Effector caspases, also known as executioner caspases, include Caspase-3, -6, and -7, and are responsible for cleaving downstream substrates. Both Caspase-3 and -7 play important roles in apoptosis, where they are activated and enhanced by initiator caspases and are responsible for proteolytic degradation and the eventual death of a cell.

Initiator Caspases:

Initiator caspases, also known as apical caspases, include Caspase-1, -2, -4, -5, -8, -9, -10, and -12, and both interact with and are activated by upstream adaptor molecules through Caspase Activation Recruitment Domains and Death Effector Domains, both of which are protein-protein interaction domains. Initiator caspases activate downstream effector caspases in a "cascade" during the cell death process of apoptosis.

Apoptosis:

Caspases play a vital role in programmed cell death, apoptosis. Apoptosis is carried out by a "Caspase cascade" that is activated by two pathways, the Intrinsic (mitochondrial) pathway and the Extrinsic (death receptor) pathway:

The Intrinsic Pathway:

The intrinsic pathway primarily involves mitochondrial outer membrane permeabilization, and its purpose is to initiate apoptosis upon reception of cellular stress signals (e.g. in the case of damage to DNA). The mitochondrion plays a role as an intracellular death receptor by receiving a number of proapoptotic signals which trigger oligomerization of proapoptotic proteins. When the stability of a mitochondrial membrane is disturbed, these proteins, namely Bax and Bak, are released, leading to the activation of initiator caspases to begin the caspase cascade. Bax is a Bcl-2-associated protein, while Bak is a Bcl-2-antagonist killer, and they cause membrane permeabilization through destabilization of the lipid bilayer. This process leads to the release of cytochrome c into the cytoplasm, a signal for the formation of Apaf1-containing apoptosomes, which bind and activate initiator procaspase-9. Caspase-9, upon maturation, is still bound to this apoptosome, now a holo-enzyme complex that in turn activates downstream effector Caspases -3 and -7. The intra-chain cleavage of the effector Caspase-3 or -7 by initiator Caspase-9 greatly enhances the effectors' catalytic activity, leading to cell degredation and death.

The Extrinsic Pathway:

The cell death (extrinsic) pathway is characterized by the elimination of unwanted cells during development. In this pathway, the ligand for death receptor Fas triggers the Death-Inducing Signaling Complex (DISC) at the cell membrane. This complex is responsible for the recruitment of initiator Caspase-8, which is consequently cleaved in procaspase form and directly activates Caspase-3 and other caspases in the cascade. These effector caspases then carry out cell death. Caspase-8 can also cause apoptosome formation and cytrochrome c release by cleaving a proapoptotic member of the Bcl-2 family, Bid. Effector caspases (Caspase-3, -6 and -7) are activated by both the intrinsic and extrinsic pathways, and are responsible for the dismantling of various cell structures by cleaving specific substrate, such as PARP and kinase MST1.

Inflammation:

Outside of involvement with apoptosis, a subset of caspases, including Caspase-1, -4, and -5 in humans (Caspase-1 and -12 in mice), are known as inflammatory caspases and are involved in cytokine maturation. They are activated by multiprotein complex inflammasomes, and are initiator caspases with Caspase Activation Recruitment Domains at the N-terminus. While no specific substrates for human Caspase-4 or -5 have yet been identified, two human Caspase-1 substrates have been discovered, proIL-1ß and proIL-18. These cytokines are vital participants in inflammation, and have multiple functions. Some of proIL-18's functions are to induce adhesion molecule upregulation, activation of natural killer cell activity, and pro-inflammatory cytokines. IL-1ß is responsible for initiating and increasing many of the effects of host response and immunity to tissue damage and microbial invasion, and it is a major inflammation mediator.

Bibliography:

GeneCards: The Human Gene Compendium. Aliases and Descriptions for CASP3 gene. "Caspase 3, apoptosis-related cysteine peptidase." Weizmann Institute of Science.
RefSeq. NCBI Gene Summary. "CASP1 caspase, apoptosis-related cysteine peptidase (interleukin 1, beta, convertase) [Homo sapiens]." NCBI, NIH.
Shi, Yigong. "Activation of Initiator Caspases: History, Hypotheses, and Perspectives," Journal of Cancer Molecules 1(1): 9-18, 2005.
D'Amelio, M. et. al. "Neuronal capase-3 signaling: not only cell death," Cell Death and Differentiation (2010) 17, 1104-1114, 2010.
Los, Marek (MD.) and Henning Walczak. Caspases: Their Role in Cell Death and Cell Survival. Molecular Biology Intelligence Unit, Springer, p. 74. 2003.
Martinon, F. and J. Tschopp. "Inflammatory caspases and inflammasomes: master switches of inflammation," Cell Death and Differentiation (2007) 14, 10-22, 2007.

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