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Product listing: Phospho-Histone H3 (Ser10) Blocking Peptide, UniProt ID P68431 #1000 to RIP (D94C12) XP® Rabbit mAb (Biotinylated), UniProt ID Q13546 #45726

$320
100 µg
This peptide is used to block Phospho-Histone H3 (Ser10) (D2C8) XP Rabbit mAb #3377 reactivity.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Modulation of chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of DNA wound around eight core histone proteins (two each of H2A, H2B, H3, and H4), is the primary building block of chromatin (1). The amino-terminal tails of core histones undergo various post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (2-5). These modifications occur in response to various stimuli and have a direct effect on the accessibility of chromatin to transcription factors and, therefore, gene expression (6). In most species, histone H2B is primarily acetylated at Lys5, 12, 15, and 20 (4,7). Histone H3 is primarily acetylated at Lys9, 14, 18, 23, 27, and 56. Acetylation of H3 at Lys9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms (2,3). Phosphorylation at Ser10, Ser28, and Thr11 of histone H3 is tightly correlated with chromosome condensation during both mitosis and meiosis (8-10). Phosphorylation at Thr3 of histone H3 is highly conserved among many species and is catalyzed by the kinase haspin. Immunostaining with phospho-specific antibodies in mammalian cells reveals mitotic phosphorylation at Thr3 of H3 in prophase and its dephosphorylation during anaphase (11).

Ammonium bicarbonate buffer is supplied as a one molar (1M) concentrated stock in HPLC grade water. This buffer is recommended for use in PTMScan protocols for LC-MS applications during the digestion procedures.
HEPES (4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid) is a commonly used biological buffer due to superior physiological pH stability over a range of temperatures and conditions.
$109
5 x 20ml
100 ml
4% (w/v) Formaldehyde from Cell Signaling Technology is a ready-to-use fixative agent for fluorescent immunocytochemical and flow cytometry assays. It is formulated in 1X PBS, methanol-free, prepared from high-quality paraformaldehyde, and packaged under an inert atmosphere of nitrogen.
APPLICATIONS

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

$45
96 tests
The FastScan™ ELISA Microwell Strip Plate, 96 Well is a clear polystyrene plate that is coated with a proprietary antibody for use with colorimetric FastScan™ ELISA kits.Each 96-well plate is composed of 12 x 8-well strips/modules. Either the entire plate can be used at one time for an experiment, or it can be subdivided to use only the necessary number of 8-well strips.
$63
125 ml
ELISA Wash Buffer (20X) is specifically formulated for use with both FastScan™ and PathScan® ELISA Kits. It is the recommended buffer to be used for all wash steps within the protocols for both kits.
Urea is an organic compound that is highly soluble in water with strong protein denaturing properties. These properties make it ideal for use in preparation of Urea Lysis buffer for preparing cell and tissue extracts prior to PTMScan®-based applications. Urea, Ultrapure, PTMScan® Qualified from Cell Signaling Technology is offered in a convenient 54.05g size that allows for the preparation of 100ml of Urea Lysis Buffer with a final formulation of 20mM HEPES, 9M urea, and 1X Phosphatase Inhibitor Cocktail when following the Directions for Use.
$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: IHC-Leica® Bond™, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Type 1 collagen is the most abundant collagen in many human tissues, including bone, skin, and tendons. It is a trimeric complex comprised of two molecules of COL1A1 (alpha-1 type 1 collagen) and one molecule of COL1A2 (alpha-2 type 1 collagen) (1-3). The expression levels of COL1A1 are regulated by multiple mechanisms, including mRNA stability, translation, and posttranslational modification (3-5). Overexpression of COL1A1 has been positively associated with tissue fibrosis disorders, including systemic sclerosis (6), while loss-of-function mutations in the COL1A1 gene are a major causative factor for osteogenesis imperfecta (brittle bone disease) (7). Notably, COL1A1 expression levels have also been associated with tumor development in gastric, lung, thyroid, and breast cancers. Research studies suggest that upregulation of COL1A1 can generate a modified extracellular matrix environment that promotes cancer cell survival, proliferation, metastasis, and invasion (8-11).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: IHC-Leica® Bond™, Immunohistochemistry (Paraffin), Western Blotting

Background: X-C motif chemokine receptor 1 (XCR1, GPR5, CCXCR1), part of the G protein-coupled superfamily, is expressed by a subset of dendritic cells and acts as a receptor for chemokines XCL1 and XCL2 (1-2,4). XCR1-positive dendritic cells cross-present antigens to naïve CD8+ T cells, priming them to become activated cytotoxic CD8+ T cells (3-5). In mouse models, the XCL1-XCR1 signaling axis was shown to be involved in the formation of self-tolerance through the development of Treg cells within the thymus (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Myeloperoxidase (MPO) is a peroxidase enzyme that is part of the host defense system of polymorphonuclear leukocytes (reviewed in 1). The gene for MPO was cloned independently from several laboratories (2-5). A decrease in MPO expression was noticed upon differentiation of HL-60 cells (5). MPO catalyzes the reaction of hydrogen peroxide and chloride (or other halides) to produce hypochlorous acid and other potent antimicrobial oxidants. Knockout mice of MPO are impaired in clearing select microbial infections (6). Processing of mature MPO from an initial 80-90 kDa translation product involves insertion of a heme moiety, glycosylation, and proteolytic cleavage. The mature protein is a tetramer of two heavy chains (60 kDa) and two light chains (12 kDa). It is abundantly expressed in neutrophils and monocytes and secreted during their activation. Heightened MPO levels have been associated with tissue damage and a number of pathological conditions (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Serum albumin is the most abundant protein in plasma. It accounts for over 50% of total human plasma protein content, having a concentration of approximately 40 g/L. Albumin is predominantly synthesized in the liver and is a major transportation component for many endogenous and exogenous compounds, including fatty acids, steroid hormones, metabolites and drugs. It is also responsible for maintaining colloid osmotic pressure and may affect microvascular integrity (1).

The Mouse-Reactive STING Pathway Antibody Sampler Kit provides an economical means of detecting activation and expression of key components of the STING pathway using phospho-specific and control antibodies. The kit includes enough antibody to perform two western blot experiments with each primary antibody.

Background: Stimulator of interferon genes (STING, TMEM173, MITA) is a transmembrane adaptor protein that is a critical component of the cellular innate immune response to pathogenic cytoplasmic DNA (1,2). STING is a ubiquitously expressed protein found predominantly in the ER (1). The enzyme cGAMP synthase (cGAS) produces the second messenger cyclic-GMP-AMP (cGAMP) in response to cytoplasmic DNA (3,4). cGAMP binds and activates STING (3,4). In addition, detection of cytoplasmic DNA by nucleic acid sensors, including DDX41 or IFI16, results in STING activation (5,6). Following activation, STING translocates with TBK1 to perinuclear endosomes and gets phosphorylated by ULK1 at Ser366 (Ser365 in mouse) (7, 8). The TBK1 kinase phosphorylates and activates IRF-3 and NF-κB, which leads to the induction of type I interferon and other immune response genes (1,2,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Frozen), Western Blotting

Background: Amyloid β (Aβ) precursor protein (APP) is a 100-140 kDa transmembrane glycoprotein that exists as several isoforms (1). The amino acid sequence of APP contains the amyloid domain, which can be released by a two-step proteolytic cleavage (1). The extracellular deposition and accumulation of the released Aβ fragments form the main components of amyloid plaques in Alzheimer's disease (1). APP can be phosphorylated at several sites, which may affect the proteolytic processing and secretion of this protein (2-5). Phosphorylation at Thr668 (a position corresponding to the APP695 isoform) by cyclin-dependent kinase is cell-cycle dependent and peaks during G2/M phase (4). APP phosphorylated at Thr668 exists in adult rat brain and correlates with cultured neuronal differentiation (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Gasdermin D (GSDMD), a member of the gasdermin family that includes GSDMA, GSDMB, and GSMDC, has been reported to have a critical role as a downstream effector of pyroptosis (1,2). Pyroptosis is a lytic type of cell death triggered by inflammasomes, multiprotein complexes assembled in response to pathogen-associated molecular patterns (PAMPs) or danger-associated molecular patterns (DAMPs) that result in the activation of caspase-1 and subsequent cleavage of pro-inflammatory cytokines IL-1β and IL-18 (3). Gasdermin D was identified by two independent groups as a substrate of inflammatory caspases, caspase-1 and caspase-11/4/5, producing two fragments: GSDMD-N and GSDMD-C. Cleavage results in release of an intramolecular inhibitory interaction between the N- and C-terminal domains, allowing the N-terminal fragment GSMDM-N to initiate pyroptosis through the formation of pores on the plasma membrane (4-7).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: IHC-Leica® Bond™, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: CD141/Thrombomodulin (TM, THBD, BDCA-3) is an integral membrane protein expressed on the surface of endothelial cells (1). Acting as a cofactor with Thrombin, CD141/Thrombomodulin activates and initiates the Protein C anticoagulant pathway (1-2). CD141/Thrombomodulin is expressed by a small subset of human CD11c+ myeloid dendritic cells (3-4). These CD141+XCR1+ dendritic cells cross-present antigens to naïve CD8+ T cells, priming them to become activated cytotoxic CD8+ T cells (3-5).

$260
100 µl

Background: N6-methyladenosine (m6A) is a post-transcriptional modification found in various RNA subtypes. While the presence of m6A in RNA was described decades ago, the lack of tools has made interrogating the epitranscriptomic landscape challenging (1,2). With the emergence of new technologies such as miCLIP and NG-RNA-seq, researchers have been able to show that m6A is a biologically relevant mark in mRNA that is enriched in 3’ UTRs and stop codons (3,4). The m6A writer complex consists of a core heterodimer of methyltransferase-like protein 3 (METTL3) and methytransferase-like protein 14 (METTL14), and the additional regulatory proteins Virlizer/VIRMA and Wilms tumor 1-associated protein (WTAP) (5). METTL3 is the catalytic methyltransferase subunit and METTL14 is the target recognition subunit that binds to RNA (6). The Virilzer/VIRMA protein directs m6A methylation to the 3’ UTRs and stop codons, and WTAP targets the complex to nuclear speckles, which are sites of RNA processing (7). Less is known about readers and erasers of m6A, and while the fat mass and obesity-associated protein FTO was the first discovered m6A demethylase, subsequent studies demonstrated that this enzyme may prefer the closely related m6Am mark in vivo (8,9). ALKBH5 was later shown to be a bona fide m6A demethylase enzyme, contributing to the idea that the m6A modification is dynamically regulated (10). Readers of the m6A mark include the YTH protein family, which can bind to m6A and influence mRNA stability and translation efficiency (3,11-13). The m6A mark and machinery have been shown to regulate a variety of cellular functions, including RNA splicing, translational control, pluripotency and cell fate determination, neuronal function, and disease (1, 14-17). The m6A writer complex has been linked to various cancer types including AML and endometrial cancers (18,19). Additionally, m6A has been implicated in resistance to chemotherapy (20).

$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Caspase-1, or interleukin-1ß converting enzyme (ICE/ICEα), is a class I cysteine protease, which also includes caspases -4, -5, -11, and -12. Caspase-1 cleaves inflammatory cytokines such as pro-IL-1ß and interferon-γ inducing factor (IL-18) into their mature forms (1,2). Like other caspases, caspase-1 is proteolytically activated from a proenzyme to produce a tetramer of its two active subunits, p20 and p10. Caspase-1 has a large amino-terminal pro-domain that contains a caspase recruitment domain (CARD). Overexpression of caspase-1 can induce apoptosis (3). Mice deficient in caspase-1, however, have no overt defects in apoptosis but do have defects in the maturation of pro-IL-1β and are resistant to endotoxic shock (4,5). At least six caspase-1 isoforms have been identified, including caspase-1 α, β, γ, δ, ε and ζ (6). Most caspase-1 isoforms (α, β, γ and δ) produce products between 30-48 kDa and induce apoptosis upon over-expression. Caspase-1 ε typically contains only the p10 subunit, does not induce apoptosis and may act as a dominant negative. The widely expressed ζ isoform of caspase-1 induces apoptosis and lacks 39 amino-terminal residues found in the α isoform (6). Activation of caspase-1 occurs through an oligomerization molecular platform designated the "inflammasome" that includes caspase-5, Pycard/Asc, and NALP1 (7).

$299
100 µg
This Cell Signaling Technology antibody is conjugated to violetFluor™ 450 and tested in-house for direct flow cytometric analysis in mouse cells.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry

Background: Major histocompatibility complex class II (MHC class II) molecules are heterodimeric, transmembrane glycoproteins expressed on the surface of antigen-presenting cells such as macrophages, dendritic cells, and B cells. Expression can also be induced on other cell types through interferon-γ signaling (1). Prior to being displayed on the cell membrane, MHC class II molecules are loaded with exogenous peptide antigens approximately 15-24 amino acids in length that were derived from endocytosed extracellular proteins digested in the lysosome (2). Antigen-presentation through MHC class II is required for T cell activation during the immune response to extracellular pathogens (2). In humans, the MHC class II protein complex is encoded by the human leukocyte antigen gene complex (HLA). HLAs corresponding to MHC class II are HLA-DP, HLA-DM, HLA-DOA, HLA-DOB, HLA-DQ, and HLA-DR (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Macrophage Scavenger receptor types I and II (MSR1, and also known as SCARA1) are members of the class A macrophage scavenger receptor family. These proteins bind large quantities of modified lipoproteins and promote endocytosis. Upregulation of MSR1 in infiltrating myeloid cells may mediate clearance of specific damage signals in response to tissue injury, including ischemic stroke (1). MSR1 germ line mutations are also associated with increased prostate cancer susceptibility in some patient cohorts (2). MSR1 is observed to be upregulated in differentiated THP-1 cells (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: IFN-γ plays key roles in both the innate and adaptive immune response. IFN-γ activates the cytotoxic activity of innate immune cells, such as macrophages and NK cells (1,2). IFN-γ production by NK cells and antigen presenting cells (APCs) promotes cell-mediated adaptive immunity by inducing IFN-γ production by T lymphocytes, increasing class I and class II MHC expression, and enhancing peptide antigen presentation (1). The anti-viral activity of IFN-γ is due to its induction of PKR and other regulatory proteins. Binding of IFN-γ to the IFNGR1/IFNGR2 complex promotes dimerization of the receptor complexes to form the (IFNGR1/IFNGR2)2 -IFN-γ dimer. Binding induces a conformational change in receptor intracellular domains and signaling involves Jak1, Jak2, and Stat1 (3). The critical role of IFN-γ in amplification of immune surveillance and function is supported by increased susceptibility to pathogen infection by IFN-γ or IFNGR knockout mice and in humans with inactivating mutations in IFNGR1 or IFNGR2. IFN-γ also appears to have a role in atherosclerosis (4).

Premium Methanol from Cell Signaling Technology is submicron filtered and 99.9% pure. It is recommended for use as a fixative or permeabilization agent in immunofluorescence and flow cytometry assays.Important: Not all CST primary antibodies require samples to be prepared with methanol fixation or permeabilization prior to immunostaining. Please refer to the antibody datasheet to determine if methanol is recommended.
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The triggering receptor expressed on myeloid cells 2 (TREM2) protein is an innate immune receptor that is expressed on the cell surface of microglia, macrophages, osteoclasts, and immature dendritic cells (1). The TREM2 receptor is a single-pass type I membrane glycoprotein that consists of an extracellular immunoglobulin-like domain, a transmembrane domain, and a cytoplasmic tail. TREM2 interacts with the tyrosine kinase-binding protein DAP12 to form a receptor-signaling complex (2). The TREM2 protein plays a role in innate immunity and a rare functional variant (R47H) of TREM2 is associated with the late-onset risk of Alzheimer’s disease (1,3). Research studies using mouse models of Alzheimer’s disease indicate that deficiency and haploinsufficiency of TREM2 can lead to increased β-amyloid (Aβ) accumulation as a result of dysfunctional microglia response (4). These results agree with the distribution of TREM2 in human brain regions (e.g., white matter, the hippocampus, and neocortex) that are involved in Alzheimer's disease pathology (2). In addition, amyloid plaque formation induces expression of TREM2 and amyloid phagocytosis (5). Loss-of-function mutations in the corresponding TREM2 or DAP12 genes can result in Nasu-Hakola disease, a rare form of progressive presenile dementia that results from polycystic osseous lesions (6). TREM2 membrane shedding occurs by cleavage at the extracellular site between H157/S158 generating an N-terminal shedded fragment and a membrane bound C-terminal fragment (7, 8).

$279
100 µg
This Cell Signaling Technology antibody is conjugated to APC and tested in-house for direct flow cytometric analysis in mouse cells.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry

Background: CD24, also know as heat stable antigen HSA, is a P-selectin ligand involved in adhesion. It is a GPI-anchored glycoprotein expressed on many types of cells, including hematopoietic cells, neural cells, and epithelial cells. CD24 is widely used to delineate stages of lymphocyte development (1-3). It also binds to Siglec-10 in humans or Siglec-G in mice (4,5). CD24 is frequently used as a marker to identify and isolate cancer stem cells in various cancer types (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: The p53 tumor suppressor protein plays a major role in cellular response to DNA damage and other genomic aberrations. Activation of p53 can lead to either cell cycle arrest and DNA repair or apoptosis (1). In addition to p53, mammalian cells contain two p53 family members, p63 and p73, which are similar to p53 in both structure and function (2). While p63 can induce p53-responsive genes and apoptosis, mutation of p63 rarely results in tumors (2). Research investigators frequently observe amplification of the p63 gene in squamous cell carcinomas of the lung, head and neck (2,3). The p63 gene contains an alternative transcription initiation site that yields a truncated ΔNp63 lacking the transactivation domain, and alternative splicing at the carboxy-terminus yields the α, β, and γ isoforms (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Axl, Mer and Tyro3 are three members of the TAM family receptor tyrosine kinase that share a common NCAM (neural adhesion molecule)-related extracellular domain and a conserved intracellular tyrosine kinase domain. These receptors bind common homologous vitamin K dependent protein GAS6 and protein S to activate down stream signaling pathway (1). TAM family receptors is involved in the development of immune, nervous, vascular and reproductive systems, autoimmune disease, cancer drug resistance and tumor immunity response (2-5). Axl Tyr698, Mer Tyr749 and Tyro3 Tyr681 are conserved autophosphorylation sites located at the activation loop of the tyrosine kinase domain. Phosphorylation at these sites is required for full kinase activation of each of the corresponding receptors (6,7).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct immunofluorescent analysis in mouse cells and tissues. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated PD-1 (D7D5W) XP® Rabbit mAb (Mouse Specific) #84651.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry)

Background: The programmed cell death 1 protein (PD-1, PDCD1, CD279) is a member of the CD28 family of immunoreceptors that regulate T cell activation and immune responses (1-3). The PD-1 protein contains an extracellular Ig V domain, a transmembrane domain, and a cytoplasmic tail that includes an immunoreceptor tyrosine-based inhibitory motif (ITIM) and an immunoreceptor tyrosine-based switch motif (ITSM). PD-1 is activated by the cell surface ligands PD-L1 and PD-L2 (4). Upon activation, PD-1 ITIM and ITSM phosphorylation leads to the recruitment of the protein tyrosine phosphatases SHP-1 and SHP-2, which suppress TCR signaling (5-7). In addition to activated T-cells, PD-1 is expressed in activated B-cells and monocytes, although its function in these cell types has not been fully characterized (8). The PD-1 pathway plays an important role in immune tolerance (3); however, research studies show that cancer cells often adopt this pathway to escape immune surveillance (9). Consequently, blockade of PD-1 and its ligands is proving to be a sound strategy for neoplastic intervention (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Neurofibromatosis 2 (NF2) is an autosomal dominant, inherited disorder characterized by the occurrence of vestibular schwannomas, meningiomas, and other nervous system tumors. Both the familial tumors of NF2 and equivalent sporadic tumors found in the general population are caused by inactivation of the NF2 tumor suppressor gene. Merlin (moesin, ezrin, and radixin-like protein) is the NF2 gene product, displaying striking similarity to ezrin, radixin, and moesin (ERM) proteins. Regulation of merlin (also called schwannomin) and ERM proteins involves intramolecular and intermolecular head-to-tail associations between family members (1). Merlin and ERM proteins act as linkers between the plasma membrane and the cytoskeleton, affecting cell morphology, polarity, and signal transduction (2). Merlin is phosphorylated by the Rac/Cdc42 effector p21-activated kinase (PAK) at Ser518, negatively regulating Rac (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Monocyte chemotactic protein-1 (MCP-1), also known as CCL2, monocyte chemotactic activating factor (MCAF) or glioma-derived chemotactic factor-2 (GDCF-2), is the product of the human JE gene and a member of the family of C-C (or β) chemokines (1-4). The predicted molecular weight of MCP-1 protein is 11-13 kDa, but it may migrate at 20-30 kDa due to glycosylation. MCP-1 is secreted by a variety of cell types in response to pro-inflammatory stimuli and was originally described for its chemotactic activity on monocytes. This activity has led to studies demonstrating its role in diseases characterized by monocyte infiltrates such as psoriasis (5), rheumatoid arthritis (6) and atherosclerosis (7). MCP-1 may also contribute to tumor progression and angiogenesis (8). Signaling by MCP-1 is mediated by the G-protein coupled receptor CCR2 (9).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated RIP (D94C12) XP® Rabbit mAb #3493.
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The receptor-interacting protein (RIP) family of serine-threonine kinases (RIP, RIP2, RIP3, and RIP4) are important regulators of cellular stress that trigger pro-survival and inflammatory responses through the activation of NF-κB, as well as pro-apoptotic pathways (1). In addition to the kinase domain, RIP contains a death domain responsible for interaction with the death domain receptor Fas and recruitment to TNF-R1 through interaction with TRADD (2,3). RIP-deficient cells show a failure in TNF-mediated NF-κB activation, making the cells more sensitive to apoptosis (4,5). RIP also interacts with TNF-receptor-associated factors (TRAFs) and can recruit IKKs to the TNF-R1 signaling complex via interaction with NEMO, leading to IκB phosphorylation and degradation (6,7). Overexpression of RIP induces both NF-κB activation and apoptosis (2,3). Caspase-8-dependent cleavage of the RIP death domain can trigger the apoptotic activity of RIP (8).