Human Caspase-2 Alexa Fluor® 532-conjugated Antibody

Catalog # Availability Size / Price Qty
FAB7228X-100UG

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Human Caspase-2 Alexa Fluor® 532-conjugated Antibody Summary

Species Reactivity
Human
Specificity
Detects human Caspase-2 in direct ELISAs. In direct ELISAs, no cross-reactivity with recombinant human Caspase-8 is observed.
Source
Monoclonal Mouse IgG2b Clone # 691233
Purification
Protein A or G purified
Immunogen
E. coli-derived recombinant human Caspase-2
Gly170-Asp333 & Ala348-Tyr452
Accession # P42575
Formulation
Supplied 0.2mg/ml in 1X PBS with RDF1 and 0.09% Sodium Azide
Label
Alexa Fluor 532 (Excitation= 534 nm, Emission= 553 nm)

Applications

Recommended Concentration
Sample
Immunocytochemistry
Optimal dilution of this antibody should be experimentally determined.
 

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

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Preparation and Storage

Shipping
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied

Background: Caspase-2

Caspase-2 (Cysteine-aspartic acid protease 2/Casp2; also NEDD2 and ICH-1) is a 30‑32 kDa member of the peptidase C14A/IL-1 beta -converting family of enzymes (1‑3). It is widely expressed and is an integral component of the apoptotic cascade. Based on the length of its prodomain, caspase-2 has been considered to be an initiator caspase. However, studies have shown that other caspases (such as Casp 3) activate procaspase 2, and Caspase-2 likely acts on key cellular molecules such as BID, Golgin 160 and DFF45/ICAD (2, 4, 5). Thus, Caspase-2 is perhaps more likely to be a specialized executioner caspase. Human procaspase-2 is a 48‑51 kDa, 452 amino acid (aa) protein (4‑7). It is known to exist as a disulfide-linked homodimer via covalent linkage at Cys436 (2, 5). But this dimeric state may not be sufficient for (auto)activation. Actual activation may occur following oligomerization within the context of activating platforms such as DISC (death-inducing signaling complex) or the PIDDosome (8-10). Initially, procaspase-2 undergoes proteolytic cleavage to generate an N‑terminal 333 aa p34/34 kDa subunit, and a 119 aa C‑terminal p14/14 kDa subunit (5). The p34 and p14 subunits are further processed to generate the prodomain (aa 1-169), plus the mature p18 (aa 170-333) and p12 (aa 348-452) subunits (4-6). Notably, each p18:p12 noncovalent heterodimer demonstrates proteolytic activity around a catalytic site at aa 318-322, and, due to an nuclear localization signal within the prodomain, may be found in either nucleus or cytoplasm (11, 12). There are multiple potential isoform variants. Individually, or in combination, there is an alternative start site at Met18, a substitution of two aa for aa 107-452, a second substitution of 14 aa for aa 309-322, and a third substitution of 22 aa for aa 323-452 (6, 7, 13). The human and mouse procaspase 2 precursors are 90% aa identical, with the majority of differences lying in the prodomain.

Entrez Gene IDs
835 (Human); 12366 (Mouse)
Alternate Names
caspase-2; CASP2; CASP-2; caspase 2, apoptosis-related cysteine peptidase; Caspase2; Caspase-2; ICH1; ICH-1; NEDD2; NEDD-2; PPP1R57

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