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Render Timestamp: 2024-12-20T11:03:37.550Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-11-22 18:01:14.794
Product last modified at: 2024-12-10T21:15:14.957Z
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PDP - Template Name: Antibody Sampler Kit
PDP - Template ID: *******4a3ef3a

Human Reactive PANoptosis Antibody Sampler Kit #34886

    Product Information

    Product Description

    The Human Reactive PANoptosis Antibody Sampler Kit provides an economical means of detecting the activation of PANoptosis in human samples. The kit includes enough antibodies to perform two western blot experiments with each primary antibody.

    Specificity / Sensitivity

    Each antibody in the Human Reactive PANoptosis Antibody Sampler Kit detects endogenous levels of its target protein. MLKL (D2I6N) Rabbit mAb cross-reacts with an unidentified protein of 130 kDa in some cell lines. IL-1β (D3U3E) Rabbit mAb is not observed to detect endogenous levels of mature IL-1β. It can detect up to 100 pg of recombinant mature IL-1β. Caspase-3 (D3R6Y) Rabbit mAb detects full-length caspase-3 as well as the large subunit (p20) of caspase-3 resulting from cleavage during apoptosis. Gasdermin D (E9S1X) Rabbit mAb recognizes both the full-length Gasdermin D and the 30 kDa amino-terminal fragment produced during pyroptosis by caspase-1. Phospho-MLKL (Ser358) (D6H3V) Rabbit mAb recognizes endogenous levels of MLKL protein only when phosphorylated at Ser358. This antibody may also bind to MLKL when dually phosphorylated at Thr357 and Ser358. Phospho-RIP3 (Ser227) (D6W2T) Rabbit mAb recognizes endogenous levels of RIP3 protein only when phosphorylated at Ser227. A band is also detected at 30 kDa that appears to be a cleavage product of RIP3. Cleaved Gasdermin D (Asp275) (E7H9G) Rabbit mAb recognizes endogenous levels of Gasdermin D protein only when cleaved at Asp275. Cleaved-IL-1β (Asp116) (D3A3Z) Rabbit mAb recognizes endogenous levels of mature IL-1β protein only when cleaved at Asp116.

    Source / Purification

    Monoclonal antibodies are produced by immunizing animals with recombinant proteins specific to human IL-1β and the p20 subunit of human caspase-3; with synthetic peptides corresponding to residues near the carboxy termini of human MLKL and RIP3, or residues surrounding Leu60 of mouse Gasdermin D, Asp275 of human Gasdermin D, Asp116 of human IL-1β, Ser358 of human MLKL, and Ser227 of human RIP3 protein.

    Background

    Programmed cell death (PCD) plays important roles in organismal development and immune responses. There are three major PCD pathways: apoptosis, pyroptosis, and necroptosis. Apoptosis is a non-inflammatory cell death and is characterized by a series of proteolytic cleavage, beginning with the initiator caspases (caspases-8/9), then the executioner caspases (caspases-3/6/7), followed by cleavage of substrate proteins to drive apoptotic cell death (1,2). During pyroptosis, caspase-1 is proteolytically activated through a protein complex called inflammasome, then the activated caspase-1 can cleave Gasdermin D (GSDMD), IL-1β, and IL-18. The freed GSDMD N-terminal domains from the cleavage form pores in the plasma membrane to drive pyroptotic cell lysis and release of the cleaved and matured IL-1β and IL-18, as well as damage-associated molecular patterns (DAMPs) (3,4). The key steps in necroptosis include the receptor-interacting protein kinase 3 (RIPK3)-dependent phosphorylation of mixed lineage kinase domain-like protein (MLKL), translocation of phosphorylated MLKL to plasma membrane, and disruption of plasma membrane integrity (5,6). In contrast to the non-inflammatory nature of apoptosis, both pyroptosis and necroptosis are proinflammatory (7). While early studies of these PCD pathways focused on their distinct individual features and underlying mechanisms, recent findings point to crosstalk and redundancies among these processes under certain conditions, where the three pathways are activated, not independently of each other, and compensatory responses occur when one pathway is blocked. This new form of PCD with key features of pyroptosis, apoptosis, and/or necroptosis has been termed PANoptosis (8,9). PANoptosis is a coordinated cell death pathway driven by a cytoplasmic protein complex named the PANoptosome, whose components provide scaffold and catalytic functions to engage pyroptosis, apoptosis, and/or necroptosis (10,11).
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