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Product listing: Mouse Interleukin-22 (mIL-22), UniProt ID Q9JJY9 #5224 to SignalSlide® HeLa -/+ IFNa IHC Controls, UniProt ID P40763 #55861

The GSK-3 Antibody Sampler Kit contains primary and secondary antibodies to perform two Western blots with each antibody.

Background: Glycogen synthase kinase-3 (GSK-3) was initially identified as an enzyme that regulates glycogen synthesis in response to insulin (1). GSK-3 is a ubiquitously expressed serine/threonine protein kinase that phosphorylates and inactivates glycogen synthase. GSK-3 is a critical downstream element of the PI3K/Akt cell survival pathway whose activity can be inhibited by Akt-mediated phosphorylation at Ser21 of GSK-3α and Ser9 of GSK-3β (2,3). GSK-3 has been implicated in the regulation of cell fate in Dictyostelium and is a component of the Wnt signaling pathway required for Drosophila, Xenopus, and mammalian development (4). GSK-3 has been shown to regulate cyclin D1 proteolysis and subcellular localization (5).

This peptide is used specifically to block GSK-3β (27C10) Rabbit mAb #9315 reactivity.

Background: Glycogen synthase kinase-3 (GSK-3) was initially identified as an enzyme that regulates glycogen synthesis in response to insulin (1). GSK-3 is a ubiquitously expressed serine/threonine protein kinase that phosphorylates and inactivates glycogen synthase. GSK-3 is a critical downstream element of the PI3K/Akt cell survival pathway whose activity can be inhibited by Akt-mediated phosphorylation at Ser21 of GSK-3α and Ser9 of GSK-3β (2,3). GSK-3 has been implicated in the regulation of cell fate in Dictyostelium and is a component of the Wnt signaling pathway required for Drosophila, Xenopus, and mammalian development (4). GSK-3 has been shown to regulate cyclin D1 proteolysis and subcellular localization (5).

This sampler kit provides an economical means of evaluating key members of the Hedgehog signaling pathway. The kit contains enough primary and secondary antibody to perform two western miniblot experiments.
The HER/ErbB Family Antibody Sampler Kit provides an economical means to evaluate the HER/ErbB Family, including the phosphorylation of EGFR, HER2/ErbB2, HER3/ErbB3, and HER4/ErbB4. The control antibodies to each family member are also included. The kit contains enough antibody to perform two western blot experiments with each primary antibody.
$320
100 µg
This peptide is used to block HER2/ErbB2 (29D8) Rabbit mAb #2165 reactivity in immunohistochemistry protocols.
APPLICATIONS

Application Methods: Immunohistochemistry (Paraffin)

Background: The ErbB2 (HER2) proto-oncogene encodes a 185 kDa transmembrane, receptor-like glycoprotein with intrinsic tyrosine kinase activity (1). While ErbB2 lacks an identified ligand, ErbB2 kinase activity can be activated in the absence of a ligand when overexpressed and through heteromeric associations with other ErbB family members (2). Amplification of the ErbB2 gene and overexpression of its product are detected in almost 40% of human breast cancers (3). Binding of the c-Cbl ubiquitin ligase to ErbB2 at Tyr1112 leads to ErbB2 poly-ubiquitination and enhances degradation of this kinase (4). ErbB2 is a key therapeutic target in the treatment of breast cancer and other carcinomas and targeting the regulation of ErbB2 degradation by the c-Cbl-regulated proteolytic pathway is one potential therapeutic strategy. Phosphorylation of the kinase domain residue Tyr877 of ErbB2 (homologous to Tyr416 of pp60c-Src) may be involved in regulating ErbB2 biological activity. The major autophosphorylation sites in ErbB2 are Tyr1248 and Tyr1221/1222; phosphorylation of these sites couples ErbB2 to the Ras-Raf-MAP kinase signal transduction pathway (1,5).

The Hippo Pathway Proteins Antibody Sampler Kit provides an economical means of detecting proteins that have been identified as upstream regulators of the Hippo Signaling Pathway. The kit provides enough antibody to perform two western blot experiments with each primary antibody.
The Hippo Signaling Antibody Sampler Kit provides an economical means of detecting target proteins of the Hippo signaling pathway. The kit contains enough primary antibody to perform two western blots per primary.
The Histone Deacetylase (HDAC) Antibody Sampler Kit provides a fast and economical means to evaluate the endogenous levels of HDACs. The kit contains enough primary and secondary antibodies to perform two Western blot experiments.

Background: Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

This peptide is used to block HP1α Antibody #2616 and HP1α (C7F11) Rabbit mAb #2623 reactivity in dot blot protocols.

Background: Heterochromatin protein 1 (HP1) is a family of heterochromatic adaptor molecules involved in both gene silencing and higher order chromatin structure (1). All three HP1 family members (α, β, and γ) are primarily associated with centromeric heterochromatin; however, HP1β and γ also localize to euchromatic sites in the genome (2,3). HP1 proteins are approximately 25 kDa in size and contain a conserved amino-terminal chromodomain, followed by a variable hinge region and a conserved carboxy-terminal chromoshadow domain. The chromodomain facilitates binding to histone H3 tri-methylated at Lys9, a histone "mark" closely associated with centromeric heterochromatin (4,5). The variable hinge region binds both RNA and DNA in a sequence-independent manner (6). The chromoshadow domain mediates the dimerization of HP1 proteins, in addition to binding multiple proteins implicated in gene silencing and heterochromatin formation, including the SUV39H histone methyltransferase, the DNMT1 and DNMT3a DNA methyltransferases, and the p150 subunit of chromatin-assembly factor-1 (CAF1) (7-9). In addition to contributing to heterochromatin formation and propagation, HP1 and SUV39H are also found complexed with retinoblastoma (Rb) and E2F6 proteins, both of which function to repress euchromatic gene transcription in quiescent cells (10,11). HP1 proteins are subject to multiple types of post-translational modifications, including phosphorylation, acetylation, methylation, ubiquitination, and sumoylation, suggesting multiple means of regulation (12-14).

The HSP/Chaperone Sampler Kit provides an economical means to investigate protein folding within the cell. The kit contains enough primary and secondary antibodies to perform two Western blot experiments with each antibody.
The HSP27 Antibody Kit provides an economical means to evaluate the activation status of the HSP27 protein. The kit contains enough primary antibody to perform two western blot experiments per primary antibody.

Background: Heat shock protein (HSP) 27 is one of the small HSPs that are constitutively expressed at different levels in various cell types and tissues. Like other small HSPs, HSP27 is regulated at both the transcriptional and posttranslational levels (1). In response to stress, the HSP27 expression increases several-fold to confer cellular resistance to the adverse environmental change. HSP27 is phosphorylated at Ser15, Ser78, and Ser82 by MAPKAPK-2 as a result of the activation of the p38 MAP kinase pathway (2,3). Phosphorylation of HSP27 causes a change in its tertiary structure, which shifts from large homotypic multimers to dimers and monomers (4). It has been shown that phosphorylation and increased concentration of HSP27 modulates actin polymerization and reorganization (5,6).

The Human Reactive Inflammasome Antibody Sampler Kit II provides an economical means of detecting multiple inflammasome components. The kit contains enough primary antibodies to perform at least two western blot experiments.

Background: The innate immune system works as the first line of defense in protection from pathogenic microbes and host-derived signals of cellular distress. One way in which these “danger” signals trigger inflammation is through activation of inflammasomes, which are multiprotein complexes that assemble in the cytosol after exposure to pathogen-associated molecular patterns (PAMPs) or danger-associated molecular patterns (DAMPs) and result in the activation of caspase-1 and subsequent cleavage of proinflammatory cytokines IL-1β and IL-18 (Reviewd in 1-6). Inflammasome complexes typically consist of a cytosolic pattern recognition receptor (PRR; a nucleotide-binding domain and leucine-rich-repeat [NLR] or AIM2-like receptor [ALR] family member), an adaptor protein (ASC/TMS1), and pro-caspase-1. A number of distinct inflammasome complexes have been identified, each with a unique PRR and activation triggers. The best characterized is the NLRP3 complex, which contains NLRP3, ASC/TMS1, and pro-caspase-1. The NLRP3 inflammasome is activated in a two-step process. First, NF-κB signaling is induced through PAMP- or DAMP-mediated activation of TLR4 or TNFR, resulting in increased expression of NLRP3, pro-IL-1β, and pro-IL-18 (priming step, signal 1). Next, indirect activation of NLRP3 occurs by a multitude of signals (whole pathogens, PAMPs/DAMPs, potassium efflux, lysosomal-damaging environmental factors [uric acid, silica, alum] and endogenous factors [amyloid-β, cholesterol crystals], and mitochondrial damage), leading to complex assembly and activation of caspase-1 (signal 2). The complex inflammasome structure is built via domain interactions among the protein components. Other inflammasomes are activated by more direct means: double-stranded DNA activates the AIM2 complex, anthrax toxin activates NLRP1, and bacterial flagellin activates NLRC4. Activated caspase-1 induces secretion of proinflammatory cytokines IL-1β and -18, but also regulates metabolic enzyme expression, phagosome maturation, vasodilation, and pyroptosis, an inflammatory programmed cell death. Inflammasome signaling contributes to the onset of a number of diseases, including atherosclerosis, type II diabetes, Alzheimer’s disease, and autoimmune disorders.

The Human T Cell Co-inhibitory and Co-stimulatory Receptor IHC Antibody Sampler Kit provides an economical means of detecting expression of receptors that modulate T cell activity in formalin-fixed, paraffin-embedded tissue samples.
The Huntingtin Interaction Antibody Sampler kit provides an economical means of detecting transcription-related proteins that interact with Huntingtin (Htt). This kit contains enough antibody to perform two western blot experiments per primary antibody.
The IAP Family Antibody Sampler Kit provides an economical means to investigate the expression of various IAP family members within the cell. The kit contains enough primary and secondary antibodies to perform two Western blot experiments.

Background: The inhibitor of apoptosis protein (IAP) family consists of an evolutionarily conserved group of apoptosis inhibitors containing a conserved 70 amino acid BIR (baculovirus inhibitor repeat) domain (1,2). Human members of this family include c-IAP1, c-IAP2, XIAP, survivin, livin, and NAIP. Overexpression of IAP family members, particularly survivin and livin, in cancer cell lines and primary tumors suggests an important role for these proteins in cancer progression (3-5). In general, the IAP proteins function through direct interactions to inhibit the activity of several caspases, including caspase-3, caspase-7, and caspase-9 (5,6). In addition, binding of IAP family members to the mitochondrial protein Smac blocks their interaction with caspase-9, thereby allowing the processing and activation of the caspase (2).

$320
100 µg
This peptide is used to block IGF-I Receptor β Antibody #3027 reactivity in dot blot protocols.
APPLICATIONS

Application Methods: Immunohistochemistry (Paraffin)

Background: Insulin-like growth factor 1 (IGF-1) is a small (7.65 kDa) growth factor that interacts with both the IGF-1 receptor and the insulin receptor to control cell growth and apoptosis. Release of this endocrine hormone from the liver is stimulated by growth hormone produced in the anterior pituitary (1). Circulating IGF-1 is typically bound to one of six known IGF binding proteins (IGF-BP) (2). At target cells, the IGF-1 ligand binds IGF receptors (or insulin receptors) leading to receptor autophosphorylation and activation (3). Activated receptors mediate downstream signaling pathways (including Akt and MAPK) that regulate cell proliferation, apoptosis, development and longevity. Altered expression or mutation of IGF-1 is associated with several human disorders, including type I diabetes and various forms of cancer (4). Recombinant human IGF-1 has been used in clinical trials as a potential therapeutic agent in the treatment of human diseases (5).

Each control slide contains formalin fixed, paraffin-embedded Jurkat cells, both untreated and treated with etoposide, that serve as a control for cleaved caspase-3 (Asp 175) immunostaining. Western blot analysis was performed on extracts derived from the same cells to verify the efficacy of the etoposide treatment.To be used with antibodies: 9664, 9661, 9662, 2035, 9541.

Background: Caspase-3 (CPP-32, Apoptain, Yama, SCA-1) is a critical executioner of apoptosis, as it is either partially or totally responsible for the proteolytic cleavage of many key proteins, such as the nuclear enzyme poly (ADP-ribose) polymerase (PARP) (1). Activation of caspase-3 requires proteolytic processing of its inactive zymogen into activated p17 and p12 fragments. Cleavage of caspase-3 requires the aspartic acid residue at the P1 position (2).

Each control slide contains formalin fixed, paraffin-embedded HeLa cells, untreated, treated with Human Interferon-α1 (hIFN-α1) #8927 that serve as a control for Phospho-Stat1 (Tyr701) and Phospho-Stat3 (Tyr705) immunostaining. Western blot analysis was performed on extracts derived from the same cells to verify the efficacy of the hIFN-α1 treatment.