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Product listing: VWF (D8L8G) XP® Rabbit mAb, UniProt ID P04275 #65707 to PathScan® Phospho-Stat3 (Tyr705) Sandwich ELISA Kit, UniProt ID P40763 #7300

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: VWF (Von Willebrand factor) is a multimeric plasma glycoprotein that promotes adhesion of platelets to sites of vascular injury (1). Mature circulating VWF is made up of disulfide-bonded multimers that are in a complex with factor VIII (2). VWF is stored in secretory Weibel-Palade bodies in endothelial cells (3,4). It is synthesized as a large precursor protein and undergoes extensive posttranslational modifications including dimerization in the endoplasmic reticulum followed by cleavage of the pro-peptide and multimerization in the Golgi apparatus (3,4). VWF is important in hemostasis, and genetic defects in the structure and modification of VWF can cause von Willebrand disease (VWD), the most common congenital bleeding disorder in humans (5).  Alternatively, increased levels of VWF have been shown to be involved in acute coronary thrombosis and are a clinical risk marker for atherosclerosis (6). VWF has also been shown to have a role in inflammation, functioning as an adhesive site for a variety of leukocyte subsets (7). Through siRNA experiments and the use VWF-deficient mice, it has also been shown that VWF regulates angiogenesis (8).

$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).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct flow cytometric analysis of human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: The Syk family protein tyrosine kinase Zap-70 is expressed in T and NK cells and plays a critical role in mediating T cell activation in response to T cell receptor (TCR) engagement (1). Following TCR engagement, Zap-70 is rapidly phosphorylated on several tyrosine residues through autophosphorylation and transphosphorylation by the Src family tyrosine kinase Lck (2-6). Tyrosine phosphorylation correlates with increased Zap-70 kinase activity and downstream signaling events. Expression of Zap-70 is correlated with disease progression and survival in patients with chronic lymphocytic leukemia (7,8).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: The Syk family protein tyrosine kinase Zap-70 is expressed in T and NK cells and plays a critical role in mediating T cell activation in response to T cell receptor (TCR) engagement (1). Following TCR engagement, Zap-70 is rapidly phosphorylated on several tyrosine residues through autophosphorylation and transphosphorylation by the Src family tyrosine kinase Lck (2-6). Tyrosine phosphorylation correlates with increased Zap-70 kinase activity and downstream signaling events. Expression of Zap-70 is correlated with disease progression and survival in patients with chronic lymphocytic leukemia (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: The Syk family protein tyrosine kinase Zap-70 is expressed in T and NK cells and plays a critical role in mediating T cell activation in response to T cell receptor (TCR) engagement (1). Following TCR engagement, Zap-70 is rapidly phosphorylated on several tyrosine residues through autophosphorylation and transphosphorylation by the Src family tyrosine kinase Lck (2-6). Tyrosine phosphorylation correlates with increased Zap-70 kinase activity and downstream signaling events. Expression of Zap-70 is correlated with disease progression and survival in patients with chronic lymphocytic leukemia (7,8).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Zap-70 (D1C10E) XP® Rabbit mAb #3165.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: The Syk family protein tyrosine kinase Zap-70 is expressed in T and NK cells and plays a critical role in mediating T cell activation in response to T cell receptor (TCR) engagement (1). Following TCR engagement, Zap-70 is rapidly phosphorylated on several tyrosine residues through autophosphorylation and transphosphorylation by the Src family tyrosine kinase Lck (2-6). Tyrosine phosphorylation correlates with increased Zap-70 kinase activity and downstream signaling events. Expression of Zap-70 is correlated with disease progression and survival in patients with chronic lymphocytic leukemia (7,8).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: The Syk family protein tyrosine kinase Zap-70 is expressed in T and NK cells and plays a critical role in mediating T cell activation in response to T cell receptor (TCR) engagement (1). Following TCR engagement, Zap-70 is rapidly phosphorylated on several tyrosine residues through autophosphorylation and transphosphorylation by the Src family tyrosine kinase Lck (2-6). Tyrosine phosphorylation correlates with increased Zap-70 kinase activity and downstream signaling events. Expression of Zap-70 is correlated with disease progression and survival in patients with chronic lymphocytic leukemia (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The Syk family protein tyrosine kinase Zap-70 is expressed in T and NK cells and plays a critical role in mediating T cell activation in response to T cell receptor (TCR) engagement (1). Following TCR engagement, Zap-70 is rapidly phosphorylated on several tyrosine residues through autophosphorylation and transphosphorylation by the Src family tyrosine kinase Lck (2-6). Tyrosine phosphorylation correlates with increased Zap-70 kinase activity and downstream signaling events. Expression of Zap-70 is correlated with disease progression and survival in patients with chronic lymphocytic leukemia (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Western Blotting

Background: β2-microglobulin (B2M) is a principal component of the Major Histocompatibility Complex (MHC) class I molecule, a ternary membrane protein complex that displays fragments derived from proteolyzed cytosolic proteins on the surface of cells for recognition by the surveillance immune system (1,2). As an integral component of the MHC class I complex, β2-microglobulin plays a critically important role in immune system function (3). It has important relevance to cancer biology research; for example, research studies have shown that nearly one-third of diffuse large B cell lymphomas contain mutations that inactivate β2-microglobulin gene function, thereby allowing tumor cells to escape immune detection (4). In addition, β2-microglobulin has been identified as an amyloid preprotein with collagen-binding affinity (5); its accumulation in osteoarthritic lesions of long-term dialysis patients is reportedly a contributing factor to the condition known as amyloid osteoarthropathy (6).

The Mouse Immune Cell Phenotyping IHC Antibody Sampler Kit provides an economical means of detecting the accumulation of immune cell types in formalin-fixed, paraffin-embedded tissue samples.

Background: Cluster of Differentiation 3 (CD3) is a multiunit protein complex expressed on the surface of T-cells that directly associates with the T-cell receptor (TCR). CD3 is composed of four polypeptides: ζ, γ, ε and δ. Engagement of TCR complex with antigens presented in Major Histocompatibility Complexes (MHC) induces tyrosine phosphorylation in the immunoreceptor tyrosine-based activation motif (ITAM) of CD3 proteins. CD3 phosphorylation is required for downstream signaling through ZAP-70 and p85 subunit of PI-3 kinase, leading to T cell activation, proliferation, and effector functions (1). Cluster of Differentiation 8 (CD8) is a transmembrane glycoprotein expressed primarily on cytotoxic T cells, but has also been described on a subset of dendritic cells in mice (2,3). On T cells, CD8 is a co-receptor for the TCR, and these two distinct structures are required to recognize antigen bound to MHC Class I (2). Cluster of Differentiation 4 (CD4) is expressed on the surface of T helper cells, regulatory T cells, monocytes, macrophages, and dendritic cells, and plays an important role in the development and activation of T cells. On T cells, CD4 is the co-receptor for the TCR, and these two distinct structures recognize antigen bound to MHC Class II. CD8 and CD4 co-receptors ensure specificity of the TCR–antigen interaction, prolong the contact between the T cell and the antigen presenting cell, and recruit the tyrosine kinase Lck, which is essential for T cell activation (2). Granzyme B is a serine protease expressed by CD8+ cytotoxic T lymphocytes and natural killer (NK) cells and is a key component of the immune response to pathogens and transformed cancer cells (4). Forkhead box P3 (FoxP3) is crucial for the development of T cells with immunosuppressive regulatory properties and is a well-established marker for T regulatory cells (Tregs) (5). CD19 is a co-receptor expressed on B cells that amplifies the signaling cascade initiated by the B cell receptor (BCR) to induce activation. It is a biomarker of B lymphocyte development, lymphoma diagnosis, and can be utilized as a target for leukemia immunotherapies (6,7). F4/80 (EMR1) is a heavily glycosylated G-protein-coupled receptor and is a well-established marker for mouse macrophages (8). CD11c (integrin αX, ITGAX) is a transmembrane glycoprotein highly expressed by dendritic cells, and has also been observed on activated NK cells, subsets of B and T cells, monocytes, granulocytes, and some B cell malignancies including hairy cell leukemia (9,10).

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).

The NF-κB Family Antibody Sampler Kit II provides an economical means of detecting members of the NF-κB family. The kit includes enough antibody to perform two western blots with each primary antibody.

Background: Transcription factors of the nuclear factor κB (NF-κB)/Rel family play a pivotal role in inflammatory and immune responses (1,2). There are five family members in mammals: RelA, c-Rel, RelB, NF-κB1 (p105/p50), and NF-κB2 (p100/p52). Both p105 and p100 are proteolytically processed by the proteasome to produce p50 and p52, respectively. Rel proteins bind p50 and p52 to form dimeric complexes that bind DNA and regulate transcription. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins (3-5). NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKKα (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which translocates to the nucleus (9-11).

This kit contains reagents to examine total protein levels of the five NF-κB/Rel family members: p65/RelA, RelB, c-Rel, NF-κB1 (p105/p50) and NF-κB2 (p100/p52).

Background: Transcription factors of the nuclear factor κB (NF-κB)/Rel family play a pivotal role in inflammatory and immune responses (1,2). There are five family members in mammals: RelA, c-Rel, RelB, NF-κB1 (p105/p50), and NF-κB2 (p100/p52). Both p105 and p100 are proteolytically processed by the proteasome to produce p50 and p52, respectively. Rel proteins bind p50 and p52 to form dimeric complexes that bind DNA and regulate transcription. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins (3-5). NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKKα (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which translocates to the nucleus (9-11).

This kit contains reagents to examine the activation state and total protein levels of key components in the noncanonical NF-κB pathway: TRAF2, TRAF3, NIK, IKKα, p100, and RelB.
The NF-κB p65 Antibody Sampler Kit contains reagents to examine NF-κB p65/RelA phosphorylation at Ser468 and Ser536; acetylation at Lys310; and total p65 levels.

Background: Transcription factors of the nuclear factor κB (NF-κB)/Rel family play a pivotal role in inflammatory and immune responses (1,2). There are five family members in mammals: RelA, c-Rel, RelB, NF-κB1 (p105/p50), and NF-κB2 (p100/p52). Both p105 and p100 are proteolytically processed by the proteasome to produce p50 and p52, respectively. Rel proteins bind p50 and p52 to form dimeric complexes that bind DNA and regulate transcription. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins (3-5). NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKKα (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which translocates to the nucleus (9-11).

This peptide is used to block NF-κB p65 (C22B4) Rabbit mAb #4764 reactivity in dot blot protocols.

Background: Transcription factors of the nuclear factor κB (NF-κB)/Rel family play a pivotal role in inflammatory and immune responses (1,2). There are five family members in mammals: RelA, c-Rel, RelB, NF-κB1 (p105/p50), and NF-κB2 (p100/p52). Both p105 and p100 are proteolytically processed by the proteasome to produce p50 and p52, respectively. Rel proteins bind p50 and p52 to form dimeric complexes that bind DNA and regulate transcription. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins (3-5). NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKKα (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which translocates to the nucleus (9-11).

$489
96 assays
1 Kit
The PathScan® Phospho-IKKα (Ser176/180) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of IKKα when phosphorylated at Ser176/180. A phospho-IKKα (Ser176/180) rabbit mAb has been coated onto the microwells. After incubation with cell lysates, phospho-IKKα (Ser176/180) protein is captured by the coated antibody. Following extensive washing, an IKKα mouse detection mAb is added to detect the captured IKKα protein. Anti-mouse IgG, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of the absorbance for the developed color is proportional to the quantity of IKKα phosphorylated at Ser176/180.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins (1-3). Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB (3-7). The key regulatory step in this pathway involves activation of a high molecular weight IκB kinase (IKK) complex whose catalysis is generally carried out by three tightly associated IKK subunits. IKKα and IKKβ serve as the catalytic subunits of the kinase and IKKγ serves as the regulatory subunit (8,9). Activation of IKK depends upon phosphorylation at Ser177 and Ser181 in the activation loop of IKKβ (Ser176 and Ser180 in IKKα), which causes conformational changes, resulting in kinase activation (10-13).

$489
96 assays
1 Kit
The PathScan® Phospho-IKKβ (Ser177/181) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of IKKβ when phosphorylated at Ser177/181. A phospho-IKKβ (Ser177/181) rabbit mAb has been coated onto the microwells. After incubation with cell lysates, phospho-IKKβ (Ser177/181) protein is captured by the coated antibody. Following extensive washing, an IKKβ mouse detection mAb is added to detect the captured IKKβ protein. Anti-mouse IgG, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of the absorbance for the developed color is proportional to the quantity of IKKβ phosphorylated at Ser177/181.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins (1-3). Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB (3-7). The key regulatory step in this pathway involves activation of a high molecular weight IκB kinase (IKK) complex whose catalysis is generally carried out by three tightly associated IKK subunits. IKKα and IKKβ serve as the catalytic subunits of the kinase and IKKγ serves as the regulatory subunit (8,9). Activation of IKK depends upon phosphorylation at Ser177 and Ser181 in the activation loop of IKKβ (Ser176 and Ser180 in IKKα), which causes conformational changes, resulting in kinase activation (10-13).

$469
Reagents for 4 x 96 well plates
1 Kit
CST's PathScan® Phospho-IκB-α (Ser32) Sandwich ELISA Antibody Pair is offered as an economical alternative to our PathScan® Phospho-IκBα (Ser32) Sandwich ELISA Kit #7355. Capture and Detection antibodies (100X stocks) and HRP-conjugated secondary antibody (1000X stock) are supplied. Sufficient reagents are supplied for 4 x 96 well ELISAs. The IκBα Capture Antibody is coated in PBS overnight in a 96 well microplate. After blocking, cell lysates are added followed by a Phospho-IκBα (Ser32) Detection Antibody and anti-Rabbit IgG, HRP conjugated antibody. HRP substrate, TMB, is added for color development. The magnitude of the absorbance for this developed color is proportional to the quantity of Phospho-IκBα (Ser32) protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state complexed with the inhibitory IκB proteins (1-3). Activation occurs via phosphorylation of IκBα at Ser32 and Ser36 followed by proteasome-mediated degradation that results in the release and nuclear translocation of active NF-κB (3-7). IκBα phosphorylation and resulting Rel-dependent transcription are activated by a highly diverse group of extracellular signals including inflammatory cytokines, growth factors, and chemokines. Kinases that phosphorylate IκB at these activating sites have been identified (8).

$489
96 assays
1 Kit
CST's PathScan® Phospho-IκBα (Ser32) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Phospho-IκBα (Ser32) protein. An IκBα Mouse mAb has been coated onto the microwells. After incubation with cell lysates, both nonphospho- and phospho-IκBα proteins are captured by the coated antibody. Following extensive washing, Phospho-IκBα (Ser32) Antibody is added to detect the captured phospho-IκBα (Ser32) protein. Anti-rabbit IgG, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of phospho-IκBα (Ser32) protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state complexed with the inhibitory IκB proteins (1-3). Activation occurs via phosphorylation of IκBα at Ser32 and Ser36 followed by proteasome-mediated degradation that results in the release and nuclear translocation of active NF-κB (3-7). IκBα phosphorylation and resulting Rel-dependent transcription are activated by a highly diverse group of extracellular signals including inflammatory cytokines, growth factors, and chemokines. Kinases that phosphorylate IκB at these activating sites have been identified (8).

$489
96 assays
1 Kit
The PathScan® Phospho-LAT (Tyr191) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of phospho-LAT (Tyr191). A LAT mouse antibody has been coated onto the microwells. After incubation with cell lysates, LAT protein (phosphorylated and non-phosphorylated) is captured by the coated antibody. Following extensive washing, a phospho-LAT (Tyr191) rabbit detection antibody is added to detect the captured phospho-LAT (Tyr191). HRP-linked anti-rabbit antibody is then used to recognize the bound detection antibody. The HRP substrate TMB is added to develop color. The magnitude of the absorbance for this developed color is proportional to the quantity of phospho-LAT (Tyr191).Antibodies in kit are custom formulations specific to kit
REACTIVITY
Human

Background: LAT, a transmembrane adaptor protein expressed in T, NK and mast cells, is an important mediator for T cell receptor (TCR) signaling (1). Upon TCR engagement, activated Zap-70 phosphorylates LAT at multiple conserved tyrosine residues within SH2 binding motifs, exposing these motifs as the docking sites for downstream signaling targets (2,3). The phosphorylation of LAT at Tyr171 and Tyr191 enables the binding of Grb2, Gads/SLP-76, PLCγ1 and PI3 kinase through their SH2 domain and translocates them to the membrane. This process eventually leads to activation of the corresponding signaling pathways (1-4).

$489
96 assays
1 Kit
The PathScan® Phospho-Lck (Tyr505) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of phospho-Lck (Tyr505). A phospho-Lck rabbit antibody has been coated onto the microwells. After incubation with cell lysates, phospho-Lck (Tyr505) is captured by the coated antibody. Following extensive washing, a Lck mouse detection mAb is added to detect the captured phospho-Lck (Tyr505). Anti-mouse, HRP-linked antibody is then used to recognize the bound detection antibody. The HRP substrate TMB is added to develop color. The magnitude of the absorbance for this developed color is proportional to the quantity of phospho-Lck (Tyr505).
REACTIVITY
Human

Background: Lck belongs to the Src-like non-receptor tyrosine kinase family with the typical Src family kinase structure: a unique amino terminal domain (Src homology 4 domain, SH4) followed by an SH3 domain, an SH2 domain, a kinase domain (SH1), and a carboxy-terminal negative regulatory domain (1). Lck activity is controlled by the interactions of SH2 and SH3 domains as well as tyrosine phosphorylation status of the activation loop (2,3). Lck is recruited to the T cell receptor (TCR) complex upon stimulation and activates downstream tyrosine kinases to initiate T cell signaling (4). Lck is also found to be involved in the regulation of mitochondrial apoptosis pathways and may be responsible for some anticancer drug induced apoptosis (5,6).

$469
Reagents for 4 x 96 well plates
1 Kit
CST's PathScan® Phospho-NF-κB p65 (Ser536) Sandwich ELISA Antibody Pair is offered as an economical alternative to our PathScan®Phospho-NF-κB p65 (Ser536) Sandwich ELISA Kit #7173. Capture and Detection antibodies (100X stocks) and HRP-conjugated secondary antibody (1000X stock) are supplied. Sufficient reagents are supplied for 4 x 96 well ELISAs. The Phospho-NF-κB p65 Capture Antibody is coated in PBS overnight in a 96 well microplate. After blocking, cell lysates are added followed by a NF-κB p65 (Ser536) Detection Antibody and anti-Rabbit IgG, HRP conjugated antibody. HRP substrate, TMB, is added for color development. The magnitude of the absorbance for this developed color is proportional to the quantity of Phospho-NF-κB p65 (Ser536) protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse

Background: Transcription factors of the nuclear factor κB (NF-κB)/Rel family play a pivotal role in inflammatory and immune responses (1,2). There are five family members in mammals: RelA, c-Rel, RelB, NF-κB1 (p105/p50), and NF-κB2 (p100/p52). Both p105 and p100 are proteolytically processed by the proteasome to produce p50 and p52, respectively. Rel proteins bind p50 and p52 to form dimeric complexes that bind DNA and regulate transcription. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins (3-5). NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKKα (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which translocates to the nucleus (9-11).

$489
96 assays
1 Kit
CST's PathScan® Phospho-NF-KappaB p65 (Ser536) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Phospho-NF-KappaB p65 protein. A Phospho-NF-KappaB p65 (Ser 536) Mouse mAb has been coated onto the microwells. After incubation with cell lysates, phospho-NF-KappaB p65 protein is captured by the coated antibody. Following extensive washing, NF-KappaB p65 Rabbit mAb is added to detect the captured phospho-NF-KappaB p65 protein. Anti-rabbit IgG, HRP-linked Antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of phospho-NF-KappaB p65 (Ser536).Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse

Background: Transcription factors of the nuclear factor κB (NF-κB)/Rel family play a pivotal role in inflammatory and immune responses (1,2). There are five family members in mammals: RelA, c-Rel, RelB, NF-κB1 (p105/p50), and NF-κB2 (p100/p52). Both p105 and p100 are proteolytically processed by the proteasome to produce p50 and p52, respectively. Rel proteins bind p50 and p52 to form dimeric complexes that bind DNA and regulate transcription. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins (3-5). NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKKα (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which translocates to the nucleus (9-11).

$489
96 assays
1 Kit
The PathScan® Phospho-SLP-76 (Ser376) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of SLP-76 protein phosphorylated at Ser376. A SLP-76 rabbit antibody has been coated onto the microwells. After incubation with cell lysates, both phospho- and non-phospho-SLP-76 proteins are captured by the coated antibody. Following extensive washing, a phospho-SLP-76 (Ser376) mouse antibody is added to detect the captured phospho-SLP-76 protein. Anti-mouse IgG, HRP-linked Antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of the absorbance for this developed color is proportional to the quantity of SLP-76 phosphorylated at Ser376.Antibodies in this kit are custom formulations specific to kit.
REACTIVITY
Human

Background: SH2 domain-containing leukocyte protein of 76 kDa (SLP-76) is a hematopoietic adaptor protein that is important in multiple biochemical signaling pathways and necessary for T cell development and activation (1). ZAP-70 phosphorylates SLP-76 and LAT as a result of TCR ligation. SLP-76 has amino-terminal tyrosine residues followed by a proline rich domain and a carboxy-terminal SH2 domain. Phosphorylation of Tyr113 and Tyr128 result in recruitment of the GEF Vav and the adapter protein Nck (2). TCR ligation also leads to phosphorylation of Tyr145, which mediates an association between SLP-76 and Itk, which is accomplished in part via the proline rich domain of SLP-76 and the SH3 domain of ITK (3). Furthermore, the proline rich domain of SLP-76 binds to the SH3 domains of Grb2-like adapter Gads (3,4). In resting cells, SLP-76 is predominantly in the cytosol. Upon TCR ligation, SLP-76 translocates to the plasma membrane and promotes the assembly of a multi-protein signaling complex that includes Vav, Nck, Itk and PLCγ1 (1). The expression of SLP-76 is tightly regulated; the protein is detected at very early stages of thymocyte development, increases as thymocyte maturation progresses, and is reduced as cells mature to CD4+ CD8+ double-positive thymocytes (5).

$489
96 assays
1 Kit
The PathScan® Phospho-Stat1 (Tyr701) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Stat1 when phosphorylated at Tyr701. A Stat1 Rabbit Antibody has been coated onto the microwells. After incubation with cell lysates, Stat1 (phospho and nonphospho) is captured by the coated antibody. Following extensive washing, biotinylated Phospho-Stat1 (Tyr701) Rabbit Detection Antibody is added to detect phosphorylation of Tyr701 on the captured Stat1 protein. HRP-linked streptavidin is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of the absorbance for this developed color is proportional to the quantity of Stat1 phosphorylated at Tyr701.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: The Stat1 transcription factor is activated in response to a large number of ligands (1) and is essential for responsiveness to IFN-α and IFN-γ (2,3). Phosphorylation of Stat1 at Tyr701 induces Stat1 dimerization, nuclear translocation, and DNA binding (4). Stat1 protein exists as a pair of isoforms, Stat1α (91 kDa) and the splice variant Stat1β (84 kDa). In most cells, both isoforms are activated by IFN-α, but only Stat1α is activated by IFN-γ. The inappropriate activation of Stat1 occurs in many tumors (5). In addition to tyrosine phosphorylation, Stat1 is also phosphorylated at Ser727 through a p38 mitogen-activated protein kinase (MAPK)-dependent pathway in response to IFN-α and other cellular stresses (6). Serine phosphorylation may be required for the maximal induction of Stat1-mediated gene activation.

$489
96 assays
1 Kit
The PathScan® Phospho-Stat3 (Ser727) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Stat3 protein phosphorylated at Ser727. A Stat3 rabbit mAb has been coated onto the microwells. After incubation with cell lysates, Stat3 (phospho or nonphospho) protein is captured by the coated antibody. Following extensive washing, a phospho-Stat3 (Ser727) mouse mAb is added to detect the captured phospho-Stat3 protein. Anti-mouse IgG, HRP-linked Antibody is then used to recognize the bound detection antibody. HRP substrate TMB is added to develop color. The magnitude of the absorbance for this developed color is proportional to the quantity of Stat3 phosphorylated at Ser727.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: The Stat3 transcription factor is an important signaling molecule for many cytokines and growth factor receptors (1) and is required for murine fetal development (2). Research studies have shown that Stat3 is constitutively activated in a number of human tumors (3,4) and possesses oncogenic potential (5) and anti-apoptotic activities (3). Stat3 is activated by phosphorylation at Tyr705, which induces dimerization, nuclear translocation, and DNA binding (6,7). Transcriptional activation seems to be regulated by phosphorylation at Ser727 through the MAPK or mTOR pathways (8,9). Stat3 isoform expression appears to reflect biological function as the relative expression levels of Stat3α (86 kDa) and Stat3β (79 kDa) depend on cell type, ligand exposure, or cell maturation stage (10). It is notable that Stat3β lacks the serine phosphorylation site within the carboxy-terminal transcriptional activation domain (8).

$489
(96 assays) Low Volume Microplate
1 Kit
The PathScan® Phospho-Stat3 (Tyr705) Chemiluminescent Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of phospho-Stat3 (Tyr705) protein with a chemiluminescent readout. Chemiluminescent ELISAs often have a wider dynamic range and higher sensitivity than conventional chromogenic detection. This chemiluminescent ELISA, which is offered in low volume microplates, shows increased signal and sensitivity while using smaller sample volume. A Stat3 antibody has been coated on the microwells. After incubation with cell lysates, phospho and nonphospho-Stat3 proteins are captured by the coated antibody. Following extensive washing, a phospho-Stat3 mouse mAb is added to detect the captured phospho-Stat3 (Tyr705) protein. Anti-mouse IgG, HRP-linked antibody is then used to recognize the bound detection antibody. Chemiluminescent reagent is added for signal development. The magnitude of light emission, measured in relative light units (RLU), is proportional to the quantity of phospho-Stat3 (Tyr705) protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse

Background: The Stat3 transcription factor is an important signaling molecule for many cytokines and growth factor receptors (1) and is required for murine fetal development (2). Research studies have shown that Stat3 is constitutively activated in a number of human tumors (3,4) and possesses oncogenic potential (5) and anti-apoptotic activities (3). Stat3 is activated by phosphorylation at Tyr705, which induces dimerization, nuclear translocation, and DNA binding (6,7). Transcriptional activation seems to be regulated by phosphorylation at Ser727 through the MAPK or mTOR pathways (8,9). Stat3 isoform expression appears to reflect biological function as the relative expression levels of Stat3α (86 kDa) and Stat3β (79 kDa) depend on cell type, ligand exposure, or cell maturation stage (10). It is notable that Stat3β lacks the serine phosphorylation site within the carboxy-terminal transcriptional activation domain (8).

$469
Reagents for 4 x 96 well plates
1 Kit
CST's PathScan® Phospho-Stat3 (Tyr705) Sandwich ELISA Antibody Pair is offered as an economical alternative to our PathScan® Phospho-Stat3 (Tyr705) Sandwich ELISA Kit #7300. Capture and Detection antibodies (100X stock) and HRP-Linked Secondary Antibody (1000X stock) are supplied. Sufficient reagents are supplied for 4 x 96 well ELISAs. The Stat3 Rabbit Capture Antibody is coated in PBS overnight in a 96 well microplate. After blocking, cell lysates are added, followed by Phospho-Stat3 (Tyr705) Mouse Detection Antibody and HRP-Linked Anti-Mouse IgG. HRP substrate, TMB, is added for color development. The magnitude of the absorbance for this developed color is proportional to the quantity of phospho-Stat3 (Tyr705) protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse

Background: The Stat3 transcription factor is an important signaling molecule for many cytokines and growth factor receptors (1) and is required for murine fetal development (2). Research studies have shown that Stat3 is constitutively activated in a number of human tumors (3,4) and possesses oncogenic potential (5) and anti-apoptotic activities (3). Stat3 is activated by phosphorylation at Tyr705, which induces dimerization, nuclear translocation, and DNA binding (6,7). Transcriptional activation seems to be regulated by phosphorylation at Ser727 through the MAPK or mTOR pathways (8,9). Stat3 isoform expression appears to reflect biological function as the relative expression levels of Stat3α (86 kDa) and Stat3β (79 kDa) depend on cell type, ligand exposure, or cell maturation stage (10). It is notable that Stat3β lacks the serine phosphorylation site within the carboxy-terminal transcriptional activation domain (8).

$489
96 assays
1 Kit
CST's PathScan® Phospho-Stat3 (Tyr705) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Phospho-Stat3 (Tyr705) protein. A Stat3 rabbit monoclonal antibody has been coated onto the microwells. After incubation with cell lysates, both nonphospho- and phospho-Stat3 proteins are captured by the coated antibody. Following extensive washing, a Phospho-Stat3 (Tyr705) mouse monoclonal antibody is added to detect the captured phospho-Stat3 protein. HRP-linked anti-mouse antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of phospho-Stat3 protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Monkey, Mouse, Rat

Background: The Stat3 transcription factor is an important signaling molecule for many cytokines and growth factor receptors (1) and is required for murine fetal development (2). Research studies have shown that Stat3 is constitutively activated in a number of human tumors (3,4) and possesses oncogenic potential (5) and anti-apoptotic activities (3). Stat3 is activated by phosphorylation at Tyr705, which induces dimerization, nuclear translocation, and DNA binding (6,7). Transcriptional activation seems to be regulated by phosphorylation at Ser727 through the MAPK or mTOR pathways (8,9). Stat3 isoform expression appears to reflect biological function as the relative expression levels of Stat3α (86 kDa) and Stat3β (79 kDa) depend on cell type, ligand exposure, or cell maturation stage (10). It is notable that Stat3β lacks the serine phosphorylation site within the carboxy-terminal transcriptional activation domain (8).