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AB32021

Anti-Caspase-2 antibody [Y154]

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(11 Publications)

Rabbit Recombinant Monoclonal Caspase-2 antibody. Suitable for WB and reacts with Human samples. Cited in 11 publications.

View Alternative Names

ICH1, NEDD2, CASP2, Caspase-2, CASP-2, Neural precursor cell expressed developmentally down-regulated protein 2, Protease ICH-1, NEDD-2

2 Images
Western blot - Anti-Caspase-2 antibody [Y154] (AB32021)
  • WB

Lab

Western blot - Anti-Caspase-2 antibody [Y154] (AB32021)

Lane 1 : Wild-type HAP1 cell lysate (20 μg)
Lane 2 : Caspase 2 knockout HAP1 cell lysate (20 μg)

Lanes 1 and 2 : Merged signal (red and green). Green - ab182738 observed at 51 kDa. Red - loading control, ab8226, observed at 42 kDa.

ab32021 was shown to recognize caspase 2 when caspase 2 knockout samples were used, along with additional cross-reactive bands. Wild-type and caspase 2 knockout samples were subjected to SDS-PAGE. ab32021 and ab8226 (loading control to beta actin) were diluted 1/50 and 1/1000 respectively and incubated overnight at 4°C. Blots were developed with Goat anti-Rabbit IgG H&L (IRDye® 800CW) preadsorbed ab216773 and Goat anti-Mouse IgG H&L (IRDye® 680RD) preadsorbed ab216776 secondary antibodies at 1/10000 dilution for 1 h at room temperature before imaging.

All lanes:

Western blot - Anti-Caspase-2 antibody [Y154] (ab32021)

Predicted band size: 51 kDa

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Western blot - Anti-Caspase-2 antibody [Y154] (AB32021)
  • WB

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Western blot - Anti-Caspase-2 antibody [Y154] (AB32021)

All lanes:

Western blot - Anti-Caspase-2 antibody [Y154] (ab32021) at 1/500 dilution

All lanes:

Jurkat (Human T cell leukemia cell line from peripheral blood) whole cell lysate

Predicted band size: 51 kDa

Observed band size: 18 kDa,50 kDa

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  • Carrier free

    Anti-Caspase-2 antibody [Y154] - BSA and Azide free

Key facts

Host species

Rabbit

Clonality

Monoclonal

Clone number

Y154

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

Specificity

This antibody is specific for the pro form and the p18 cleaved form of Caspase-2.

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/500", "WB-species-notes": "<p>Detects bands of approximately 50 kDa (pro form) and 18 kDa (p18 cleaved form).</p>" } } }
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Product details

Species reactivity
Mouse, Rat: We have preliminary internal testing data to indicate this antibody may not react with these species.
Please contact us for more information.

Patented technology
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.

What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:

  • - High batch-to-batch consistency and reproducibility
  • - Improved sensitivity and specificity
  • - Long-term security of supply
  • - Animal-free batch production

For more information, read more on recombinant antibodies.

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
pH: 7.2 - 7.4 Preservative: 0.01% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.05% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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Target data

Is a regulator of the cascade of caspases responsible for apoptosis execution (PubMed : 11156409, PubMed : 15073321, PubMed : 8087842). Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival (PubMed : 15073321). Associates with PIDD1 and CRADD to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis in response to genotoxic stress (PubMed : 15073321).. Isoform 1. Acts as a positive regulator of apoptosis.. Isoform 2. Acts as a negative regulator of apoptosis.. Isoform 3. May function as an endogenous apoptosis inhibitor that antagonizes caspase activation and cell death.
See full target information CASP2
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Publications (11)

Recent publications for all applications. Explore the full list and refine your search

Experimental and therapeutic medicine 28:297 PubMed38868612

2024

18‑α‑glycyrrhetinic acid induces apoptosis in gingival fibroblasts exposed to phenytoin.

Applications

Unspecified application

Species

Unspecified reactive species

Reiri Takeuchi,Takatoshi Nomura,Manabu Yaguchi,Chieko Taguchi,Itaru Suzuki,Haruka Suzuki,Hiroko Matsumoto,Yuichiro Okada,Kazumune Arikawa,Takato Nomoto,Koichi Hiratsuka

Molecular medicine reports 25: PubMed34981821

2022

lncRNA GMDS‑AS1 upregulates IL‑6, TNF‑α and IL‑1β, and induces apoptosis in human monocytic THP‑1 cells via miR‑96‑5p/caspase 2 signaling.

Applications

Unspecified application

Species

Unspecified reactive species

Lei Jiang,Jinghui Li

Nutrition & metabolism 18:74 PubMed34274001

2021

Calcium channel blockers do not protect against saturated fatty acid-induced ER stress and apoptosis in human pancreatic β-cells.

Applications

Unspecified application

Species

Unspecified reactive species

Jan Šrámek,Vlasta Němcová,Jan Kovář

PloS one 13:e0209750 PubMed30589909

2018

MicroRNA-8073: Tumor suppressor and potential therapeutic treatment.

Applications

Unspecified application

Species

Unspecified reactive species

Atsuko Mizoguchi,Aiko Takayama,Taiga Arai,Junpei Kawauchi,Hiroko Sudo

Nature methods 15:909-912 PubMed30377371

2018

A high-throughput pipeline for validation of antibodies.

Applications

Unspecified application

Species

Unspecified reactive species

Krzysztof Sikorski,Adi Mehta,Marit Inngjerdingen,Flourina Thakor,Simon Kling,Tomas Kalina,Tuula A Nyman,Maria Ekman Stensland,Wei Zhou,Gustavo A de Souza,Lars Holden,Jan Stuchly,Markus Templin,Fridtjof Lund-Johansen

Disease models & mechanisms 10:655-669 PubMed28360125

2017

Cellular levels of Grb2 and cytoskeleton stability are correlated in a neurodegenerative scenario.

Applications

Unspecified application

Species

Unspecified reactive species

Piyali Majumder,Kasturi Roy,Brijesh Kumar Singh,Nihar Ranjan Jana,Debashis Mukhopadhyay

International journal of molecular sciences 16:24011-31 PubMed26473837

2015

Ferulic Acid Exerts Anti-Angiogenic and Anti-Tumor Activity by Targeting Fibroblast Growth Factor Receptor 1-Mediated Angiogenesis.

Applications

Unspecified application

Species

Unspecified reactive species

Guang-Wei Yang,Jin-Song Jiang,Wei-Qin Lu

American journal of translational research 6:538-47 PubMed25360218

2014

Regulation of CRADD-caspase 2 cascade by histone deacetylase 1 in gastric cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Qi Shen,Wanfen Tang,Jie Sun,Lifeng Feng,Hongchuan Jin,Xian Wang

Blood cancer journal 3:e153 PubMed24141622

2013

Synergistic apoptotic response between valproic acid and fludarabine in chronic lymphocytic leukaemia (CLL) cells involves the lysosomal protease cathepsin B.

Applications

Unspecified application

Species

Human

J-Y Yoon,D Szwajcer,G Ishdorj,P Benjaminson,W Xiao,R Kumar,J B Johnston,S B Gibson

Cancer cell international 13:42 PubMed23672670

2013

Caspase-2 is involved in cell death induction by taxanes in breast cancer cells.

Applications

WB

Species

Unspecified reactive species

Michael Jelínek,Kamila Balušíková,Dana Kopperová,Vlasta Nĕmcová-Fürstová,Jan Šrámek,Julie Fidlerová,Ilaria Zanardi,Iwao Ojima,Jan Kovář
View all publications
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