ARG82784

Human Caspase 3 ELISA Kit

Human Caspase 3 ELISA Kit for ELISA and Human

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Component

Cat No Component Name Package Temp
ARG82784-001 Antibody-coated microplate 8 X 12 strips 4°C. Unused strips should be sealed tightly in the air-tight pouch.
ARG82784-002 Standard 2 X 10 ng/vial 4°C
ARG82784-003 Standard/Sample diluent 30 ml (Ready to use) 4°C
ARG82784-004 Antibody conjugate concentrate (100X) 1 vial (100 µl) 4°C
ARG82784-005 Antibody diluent buffer 12 ml (Ready to use) 4°C
ARG82784-006 HRP-Streptavidin concentrate (100X) 1 vial (100 µl) 4°C
ARG82784-007 HRP-Streptavidin diluent buffer 12 ml (Ready to use) 4°C
ARG82784-008 25X Wash buffer 20 ml 4°C
ARG82784-009 TMB substrate 10 ml (Ready to use) 4°C (Protect from light)
ARG82784-010 STOP solution 10 ml (Ready to use) 4°C
ARG82784-011 Plate sealer 4 strips Room temperature

Overview

Product Description ARG82784 Human Caspase 3 ELISA Kit is an Enzyme Immunoassay kit for the quantification of Human Caspase 3 in serum and cell culture supernatants.
Tested Reactivity Hu
Tested Application ELISA
Target Name Caspase 3
Conjugation HRP
Conjugation Note Substrate: TMB and read at 450 nm.
Sensitivity 15.6 pg/ml
Sample Type Serum and cell culture supernatants.
Standard Range 31.2 - 2000 pg/ml
Sample Volume 100 µl
Precision Intra-Assay CV: 6.1%
Inter-Assay CV: 7.1%
Alternate Names CPP-32; Caspase-3; EC 3.4.22.56; Apopain; CASP-3; CPP32; Cysteine protease CPP32; SCA-1; SREBP cleavage activity 1; CPP32B; Protein Yama

Application Instructions

Assay Time ~ 5 hours

Properties

Form 96 well
Storage Instruction Store the kit at 2-8°C. Keep microplate wells sealed in a dry bag with desiccants. Do not expose test reagents to heat, sun or strong light during storage and usage. Please refer to the product user manual for detail temperatures of the components.
Note For laboratory research only, not for drug, diagnostic or other use.

Bioinformation

Database Links

GeneID: 836 Human CASP3

Swiss-port # P42574 Human Caspase-3

Gene Symbol CASP3
Gene Full Name caspase 3, apoptosis-related cysteine peptidase
Background The protein encoded by this gene is a cysteine-aspartic acid protease that plays a central role in the execution-phase of cell apoptosis. The encoded protein cleaves and inactivates poly(ADP-ribose) polymerase while it cleaves and activates sterol regulatory element binding proteins as well as caspases 6, 7, and 9. This protein itself is processed by caspases 8, 9, and 10. It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease. [provided by RefSeq, Aug 2017]
Function Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage. [UniProt]
Cellular Localization Cytoplasm. [UniProt]
PTM Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits. Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease. Active heterodimers between the small subunit of caspase-7 protease and the large subunit of caspase-3 also occur and vice versa.

S-nitrosylated on its catalytic site cysteine in unstimulated human cell lines and denitrosylated upon activation of the Fas apoptotic pathway, associated with an increase in intracellular caspase activity. Fas therefore activates caspase-3 not only by inducing the cleavage of the caspase zymogen to its active subunits, but also by stimulating the denitrosylation of its active site thiol. [UniProt]

Specific References

Oral Galvanism Side Effects: Comparing Alloy Ions and Galvanic Current Effects on the Mucosa-like Model

ELISA / Human / Cell culture supernatant

Natalia Chepelova et al.
J Funct Biomater.,  (2023)

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