Anti-Caspase-4 (Human) mAb

  • Applications
    • WB
  • Target Caspase 4
  • Host Species Mouse
  • Species Reactivities Human
  • Code # M029-3
  • Size 100 μg
  • Price
    $278.49
Specifications

Alternative Names

CASP4, caspase 4, apoptosis-related cysteine peptidase, TX ICH-2, Mih1, TX, ICEREL-II,ICE(rel)II

Background

The interleukin-1β converting enzyme (ICE)/CED-3 family proteases has been implicated in playing a fundamental role in programmed cell death. TX is a member of the ICE/CED-3 gene family encoding a cysteine protease that has a more than 50% sequence homology with ICE, especially in the region encoding the mature p20 and p10 ICE subunits and 30% sequence homology with Nedd-2/Ich-1L and CED-3. TX is able to cleave itself and the p30 ICE precursor and induces apoptosis in transfected cells1). TX is also a member of the caspase (CASP) family, CASP-4. An early biochemical event that occurs apoptosis in many cell types is the proteolytic cleavage of poly (ADP-ribose) polymerase (PARP), a nuclear enzyme involved in DNA repair. The several mammalian ICE homologues, ICE, TX, Nedd-2/Ich-1L and CPP32, are capable of cleaving PARP.
  • Antibody Type:
    Monoclonal
  • Application:
    WB
  • Clone Number:
    4B9
  • Concentration:
    1 mg/mL
  • Conjugate:
    Unlabeled
  • Description:

    Monoclonal Antibody of 100 μg targeting Caspase 4 for WB.

  • Formulation:
    100 μg IgG in 100 μl volume of PBS containing 50% glycerol, pH 7.2. No preservative iscontained.
  • Gene ID (Human):
  • Gene ID (Mouse):
  • Host Species:
    Mouse
  • Immunogen:
    Recombinant human TX (:1-270 a.a. terminal N)
  • Isotype:
    IgG1 ĸ
  • Product Type:
    Antibody
  • Reactivity:
    This antibody reacts with caspase-4 (43kDa) on Western blotting using total cell lysate from U937,HL60 and HUC-Fm (Human primary cultured fibroblast) ,and also reacts with 44 kDa of myc-tagged-TX expressedin 293T cell. Occasionally, unidentified 68 kD
  • Research Area:
    Apoptosis
  • Short Description:

    Caspase 4 Monoclonal Antibody.

  • Size:
    100 μg
  • Species Reactivity:
    Human
  • Storage Temperature:
    -20°C
  • Target:
    Caspase 4
Citations
  1. Hiratsuka T et al. Yokukansan inhibits neuronal death during ER stress by regulating the unfolded protein response. PLoS One. 5, e13280 (2010),
  2. Hitomi J et al. Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death. J Cell Biol. 165, 347-356 (2004),
  3. Huang TT et al. Activation of multiple apoptotic pathways in human nasopharyngeal carcinoma cells by the prenylated isoflavone, osajin. PLoS One. 6, e18308 (2011),
  4. Ito K et al. The role of the CNOT1 subunit of the CCR4-NOT complex in mRNA deadenylation and cell viability. Protein Cell. 2, 755-763 (2011),
  5. Koyama Y et al. Familial amyotrophic lateral sclerosis (FALS)-linked SOD1 mutation accelerates neuronal cell death by activating cleavage of caspase-4 under ER stress in an in vitro model of FALS. Neurochem Int. 57, 838-843 (2010),
  6. Koyama Y et al. Induction of amyloid beta accumulation by ER calcium disruption and resultant upregulation of angiogenic factors in ARPE19 cells. Invest Ophthalmol Vis Sci. 2008 49, 2376-2383 (2008),
  7. Lin XY et al. Expression analysis of the human caspase-1 subfamily reveals specific regulation of the CASP5 gene by lipopolysaccharide and interferon-gamma. J Biol Chem. 275, 39920-39926 (2000),
  8. Michallet AS et al. Compromising the unfolded protein response induces autophagy-mediated cell death in multiple myeloma cells. PLoS One. 6, e25820 (2011),
  9. Milleron RS, Bratton SB. Heat shock induces apoptosis independently of any known initiator caspase-activating complex. J Biol Chem. 281, 16991-17000 (2006),
  10. Nawrocki ST et al. Myc regulates aggresome formation, the induction of Noxa, and apoptosis in response to the combination of bortezomib and SAHA. Blood. 112, 2917-2926 (2008),
  11. Nishitsuji K et al. The E693Delta mutation in amyloid precursor protein increases intracellular accumulation of amyloid beta oligomers and causes endoplasmic reticulum stress-induced apoptosis in cultured cells. Am J Pathol. 174, 957-969 (2009),
  12. Oda T et al. Distinct mechanism of cell death is responsible for tunicamycin-induced ER stress in SK-N-SH and SH-SY5Y cells. Neurosci Res. 60, 29-39 (2008),
  13. Pastorino JG, Shulga N. Tumor necrosis factor-alpha can provoke cleavage and activation of sterol regulatory element-binding protein in ethanol-exposed cells via a caspase-dependent pathway that is cholesterol insensitive. J Biol Chem. 283, 25638-25649 (2008),
  14. Pastorino JG, Shulga N. Tumor necrosis factor-alpha can provoke cleavage and activation of sterol regulatory element-binding protein in ethanol-exposed cells via a caspase-dependent pathway that is cholesterol insensitive. J Biol Chem. 283, 25638-25649 (2008),
  15. Sollberger G et al. Caspase-4 is required for activation of inflammasomes. J Immunol. 188, 1992-2000 (2012),
  16. Takemoto K et al. Mitochondrial TRAP1 regulates the unfolded protein response in the endoplasmic reticulum. Neurochem Int. 58, 880-887 (2011),
  17. Walsh JG et al. Caspase-1 promiscuity is counterbalanced by rapid inactivation of processed enzyme. J Biol Chem. 286, 32513-32524 (2011),
  18. Walsh JG et al. Caspase-1 promiscuity is counterbalanced by rapid inactivation of processed enzyme. J Biol Chem. 286, 32513-32524 (2011),
  19. Yoshikawa T et al. Increased expression of tight junctions in ARPE-19 cells under endoplasmic reticulum stress. Curr Eye Res. 36, 1153-1163 (2011),
  20. Yukioka F et al. Presenilin-1 mutation activates the signaling pathway of caspase-4 in endoplasmic reticulum stress-induced apoptosis. Neurochem Int. 52, 683-687 (2008)
References
  1. Lin, F-R., et al., Cancer Res. 67, 11914-11923 (2007)
  2. López-Antón, N., et al., J. Biol. Chem. 281, 33078-33086 (2006)
  3. Milleron R. S. and Bratton S. B., J. Biol. Chem. 281, 16991-17000 (2006)
  4. Hitomi, J., et al., J. Cell Biol. 165, 347-356 (2004)
  5. Cerdan, C., et al., Blood 97, 2205-2212 (2001)
  6. Lin, X. Y., et al., J. Biol. Chem. 275, 39920-39926 (2000)