Exalpha Biologicals, Inc.

Accelerating the Pace of Discovery

Product Highlight

Mouse anti-M13 phage coat protein g8p

Antibodies recognising M13 filamentous phage coat proteins are instrumental in the selection and detection of phages expressing specific antibody fragments or peptide sequences at their surface. The monoclonal antibodies manufactured and supplied by Exalpha react with either the pIII (g3p) or pVIII (g8p) proteins of M13 filamentous bacteriophage. All antibodies are available in a purified format. The antibodies are fully validated and are suitable for a wide range of techniques including:

  • ELISA
  • Flow Cytometry
  • Western Blot
  • Immunohistochemistry
  • Immunoprecipitation
For more information, click here for our M13 Bacteriophage information page.

News

Two more of our excellent products have been published by PubMed:

Potential actionable targets in appendiceal cancer detected by immunohistochemistry, fluorescent in situ hybridization, and mutational analysis
Borazanci, E., et al., J. Gastrointest. Oncol., 8, 164-172 (2017)
Using Exalpha SPARC Antibody (Cat. No. X1867P)

Molecular mechanism underlying the pharmacological interactions of the protein kinase C-β inhibitor enzastaurin and erlotinib in non-small cell lung cancer cells
Steen, N.V., et al., Am. J. Cancer Res., 7, 816-830 (2017)
Using Exalpha's FITC labeled anti PY20 Antibody (Cat. No. X1017)

Exalpha Biologicals, Inc.

Caspase-12 (IN)

  • Product Code: X1114P
  • Size: 100 µg
  • Availability: In Stock In Stock
  • Price (USD): $383

Cat #

X1114P		 Quantity:      

Data Sheet

Product Name

Caspase-12 (IN)

Host/Source

Rabbit

Isotype

IgG

Product Type

Polyclonal Antibody

Reactivity

Human, Mouse, Rat

Applications

Western Blot

Purification

Antigen Immunoaffiinity Purification

Size

100 µg

Price (USD)

$383

Background

Three distinct signaling pathways lead to programmed cell death (apoptosis). The death receptor and mitochondrion pathways are the mains, in which the key apoptotic proteases capase-8 and caspase-9, respectively, are involved. The endoplasmic reticulum (ER) stress is the third apoptotic pathway and caspase-12 is involved (1,2). Caspase-12 is localized to the ER but not to cytoplasm or mitochondrion. Caspase-12 is activated by ER stress, including disruption of ER calcium homeostasis, and mediates ER stress-induced apoptosis. Caspase-12 is co-localized to the ER with several proteins that are involved in Alzheimer’s disease including γ-secretase presenilin and β-amyloid precursor protein (APP). Caspase-12 mediates cytotoxicity induced by amyloid-β. Caspase-12 is ubiquitously expressed in mouse tissues (1).

Immunogen

Synthetic peptide corresponding to amino acids 100 to 116 of the murine caspase-12

Positive Control

Murine spleen tissue lysate

Formulation

Provided in phosphate buffered saline solution containing 0.02% sodium azide as a preservative

Customer Storage

Product should be stored at -20°C. Aliquot to avoid freeze/thaw cycles

Target Molecular Weight

38.9 kDa

Product Image

Image Legend

Western blot analysis using anti-Capase-12 (IN) antibody at1 µg/ml on mouse brain tissue in the absense (1) and presense (2) of blocking peptide.

Database Links:

SwissProtQ6UXS9Human

References

1. Nakagawa, T., et al., Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 2000, 403, 98-103.

2. Mehmet, H., Caspases find a new place to hide. Nature 2000, 403, 29-30

3. Van de Craen M, et al., Characterization of seven murine caspase family members. FEBS Lett 1997, 403, 61-9


Product Specific References


This product has been used in:

1. Hetz, C., et al, 'Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein' EMBO Journal 2003, 22, , 5435-54
2. Hetz, C., et al, 'The Disulfide Isomerase Grp58 Is a Protective Factor against Prion Neurotoxicity' Journal of Neuroscience 2005, 25, , 2793-2802
3. Rao, Rammohan V., et al, 'Coupling Endoplasmic Reticulum Stress to the Cell Death Program' The Journal of Biological Chemistry 2002, 277, 24, 21836-21842
4. Moreno, J.A., et al. ‘Sustained translational repression by eIF2α–P mediates prion neurodegeneration.’ Nature, 485, 507-511 (2012)
5. Sun, W., et al. ‘Magnolia Extract (BL153) Protection of Heart from Lipid Accumulation Caused Cardiac Oxidative Damage, Inflammation, and Cell Death in High-Fat Diet Fed Mice’ Oxid. Med. Cell. Longev. (2014), 205849
6. Zhao, Y., et al. ‘A Novel Mechanism by Which SDF-1β Protects Cardiac Cells From Palmitate-Induced Endoplasmic Reticulum Stress and Apoptosis via CXCR7 and AMPK/p38 MAPK-Mediated Interleukin-6 Generation’ Diabetes (2013), 62, 2545-2558