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Purified Rabbit Anti-Caspase-12 w/ Control

Purified Rabbit Anti-Caspase-12 w/ Control

(RUO)
Purified Rabbit Anti-Caspase-12 w/ Control

Western blot analysis of caspase-12. Lysate from mouse spleen was probed with anti-caspase-12 (Cat. No. 551430) at dilutions of 1:1000 (lane 1), 1:2000 (lane 2), and 1:4000 (lane 3). Caspase-12 is identified as a band of ~55 kDa.

Western blot analysis of caspase-12. Lysate from mouse spleen was probed with anti-caspase-12 (Cat. No. 551430) at dilutions of 1:1000 (lane 1), 1:2000 (lane 2), and 1:4000 (lane 3). Caspase-12 is identified as a band of ~55 kDa.

Product Details
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BD Pharmingen™
Mouse (QC Testing), Human,Rat (Reported)
Western blot (Routinely Tested)
RUO
AB_394193


Description

Caspases are a family of cysteine proteases that are key mediators of programmed cell death or apoptosis. The precursor forms of caspases are composed of a prodomain, and large and small catalytic subunits. The active forms of caspases are generated by several stimuli including ligand-receptor interactions, growth factor deprivation, and inhibitors of cellular functions. All known caspases require cleavage adjacent to aspartates to liberate one large and one small subunit, which associate into a α2β2 tetramer to form the active enzyme. To date, approximately 14 caspases have been identified in mammals. Caspases can be divided into three groups based upon structural differences and substrate preferences. These include apoptotic initiators (caspase-2, -8, -9, and -10), apoptotic executioners (caspase-3, -6, and -7), and cytokine processors (caspase-1, -4, -5, -13, murine caspase-11, -12, and -14). Caspase-12 has been cloned from the mouse, and based upon sequence homology to other murine caspases (mCASP) can be divided  into a subfamily including mCASP1 and -11. The tissue distribution of mCASP-12 was examined by Northern blot analysis and found to be expressed in most tissues, but was highest in skeletal, muscle, and lung tissue. Caspase-12 has been reported to be activated when the endoplasmic reticulum (ER) undergoes stress, and a participant in ER stress-induced apoptosis pathway. Mice deficient for caspase-12 do not undergo ER stress-induced apoptosis, but their cells are capable of undergoing programmed cell death induced by other stimuli. Murine caspase-12 migrates at ~55 kDa in SDS-PAGE. The antibodies recognize human, mouse, and rat caspase-12. A synthetic peptide corresponding to amino acids 2-17 of murine caspase-12 was used as the immunogen.

Preparation And Storage

The polyclonal antibody was purified from antiserum by negative adsorption and affinity chromatography.

Recommended Assay Procedures

Applications include western blot analysis (1:1000-1:4000). Mouse spleen control lysate [50 µg (1 µg/ml)] is provided as a positive control (Cat. No. 51-16586N; store lysate at -20°C). Additional mouse spleen control lysate (Cat. No. 611462) is sold separately as a ready-to-use western blot control.

Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
  3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
551430 Rev. 1
Components
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Description Quantity/Size Part Number
Mouse spleen control lysate 50 µg (1 ea) 51-16586N
Purified Rabbit Anti-Caspase-12 100 µL (1 ea) 51-8104KC
551430 Rev. 1
Citations & References
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Development References (4)

  1. Nakagawa T, Zhu H, Morishima N, et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature. 2000; 403(6765):98-103. (Biology). View Reference
  2. Van de Craen M, Vandenabeele P, Declercq W, et al. Characterization of seven murine caspase family members. FEBS Lett. 1997; 403(1):61-69. (Biology). View Reference
  3. Wolf BB, Green DR. Suicidal tendencies: apoptotic cell death by caspase family proteinases. J Biol Chem. 1999; 274(29):20049-20052. (Biology). View Reference
  4. Yoneda T, Imaizumi K, Oono K, et al. Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress. J Biol Chem. 2001; 276(17):13935-13940. (Biology). View Reference
551430 Rev. 1

Please refer to Support Documents for Quality Certificates

Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described

Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims.  Comparisons are not made against non-BD technologies, unless otherwise noted.

Non-IVD products are For Research Use Only. Not for use in diagnostic or therapeutic procedures.

 

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