Caspase 2, Apoptosis-Related Cysteine Peptidase (CASP2) antibody

Antigen: Caspase 2, Apoptosis-Related Cysteine Peptidase (CASP2)

Synonyms: ICH1, NEDD2, CASP-2, ICH-1L, ICH-1L/1S, ICH-1, Nedd2, Caspase-2, xCaspase-2

Clonality: Polyclonal

Host: Rabbit

Reactivity: Mouse (Murine), Rat (Rattus)

Conjugate: Un-conjugated

Application: ELISA, Western Blotting (WB)

Catalog no.: ABIN118007

Additional Information

Alternative name: Caspase-2

UniProt: P29594

Immunogen: A synthetic peptide corresponding to the N-terminus of rat Caspase-2 protein conjugatedto Keyhole Limpet Hemocyanin (KLH) through a cysteine residue linker. AA Sequence: M-A-A-S-S-G-R-S-Q-S-S-L-H-R-K-G-L-C-KLH

Cross-Reactivity: Mouse (Murine), Rat (Rattus)

Description: Apoptosis occurs during normal cellular development and involves dramatic changes incellular structure. Disruption of apoptosis may contribute to cancer and other diseases. Caspases are a family of cysteine proteases that are key mediators of programmed celldeath or apoptosis. Caspase-2 has been called ICH-1 in human, CED-3 in C. elegans andNEDD-2 in mouse. Caspase-2 is synthesized as an inactive precursor that is processed incells undergoing apoptosis. The precursor form of all caspases is composed of apro-domain, and large and small catalytic subunits. The active forms of caspases aregenerated by several stimuli, including ligand-receptor interactions, growth factordeprivation and inhibitors of cellular functions. Caspase-2 is activated in vitro bycaspase-1, caspase-3 and granzyme B. Caspase-2 functions as an upstream apoptosisinitiator that participates in the activation of downstream caspases, such as caspase-3,caspase-6 and caspase-7. Caspase-2 is highly expressed in embryonic mouse brain butnot in adult neural tissue. Alternative mRNA splicing produces a long (48 kDa) and short(35 kDa) form of caspase-2. These forms show tissue specificity and function either asinducers or suppressors of apoptosis. Mature caspase-2 is 435 amino acids in lengthcleaved (~50 kDa) and is cleaved upon activation into 10 and 20 kDa subunits.

Characteristics: Synonyms: CASP-2, CASP2, ICH1, ICH-1 protease, NEDD2, Neural precursor cell expresseddevelopmentally down-regulated protein 2

Application Details

Application Notes: This product was assayed against 1.0 g of immunizing peptide in a standard sandwichELISA using HRP conjugated Affinity Purified anti-Rabbit IgG [H&L] (Goat) and TMB as asubstrate for 30 minutes at room temperature. A working dilution of 1: 2,000 to 1: 10,000 issuggested for this product. This affinity purified polyclonal antibody was tested by immunoblotting and was found tobe reactive with 48 kDa mouse and rat caspase-2. A control and rat caspase-2 transfected human 293 cell lysate was used to show by

Concentration: 0.67 mg/ml (by UV absorbance at 280 nm)

Purification: Affinity Purified

Buffer: 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2 with 0.01%(w/v) Sodium Azide as preservative.

Storage: Store vial at -20°C prior to opening. Centrifuge product if not completely clear afterstanding at room temperature. Dilute only prior to immediate use. For extended storagealiquot contents and freeze at -20°C or below. Avoid cycles of freezing and thawing. Shelf life: one year from despatch.

Research Area: Apoptosis/Necrosis, Cancer, Autophagy

Restrictions: For Research Use only

Images

Immunoblotting. Affinity Purified antibody to Caspase-2 was used at a 1:750 dilution to detect rat caspase-2 in transfected human 292 cell lysates by Western blot. Asterisk indicates a 48 kDa caspase-2 protein clearly detected in the rat caspase-2 transfected lysate. No reaction is observed against human caspase-2. Control (lane 1) and transfected (lane 2) lysates were loaded on a 4-20% gel for SDS-PAGE. After primary antibody incubation and washing, a 1:5,000 dilution of HRP conjugated Gt-a-Rabbit IgG preceded color development using Amersham's substrate system.

Publications

Wang, Miura, Bergeron et al.: "Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death." in: Cell, Vol. 78, Issue 5, pp. 739-50, 1994 (PubMed).

Li, Bergeron, Cryns et al.: "Activation of caspase-2 in apoptosis." in: The Journal of biological chemistry, Vol. 272, Issue 34, pp. 21010-7, 1997 (PubMed).

Cohen: "Caspases: the executioners of apoptosis." in: The Biochemical journal, Vol. 326 ( Pt 1), Issue 5693, pp. 1-16, 1997 (PubMed).

Bergeron, Perez, Macdonald et al.: "Defects in regulation of apoptosis in caspase-2-deficient mice." in: Genes & development, Vol. 12, Issue 9, pp. 1304-14, 1998 (PubMed).