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Monoclonal Antibody Ihc-Leica® bond™ Human

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: ICOS (Inducible Co-Stimulator, CD278) is a member of the CD28 family that regulates T cell activity and immune responses (1). The ICOS protein contains an extracellular IgV like domain, a transmembrane domain, and an intracellular domain with a YMFM motif (1-2). ICOS is primarily expressed on activated CD4+ and CD8+ T cells (1). Upon binding to its ligand, ICOS potentiates the T cell response to antigen through activation of the PI3K signaling pathway (2). In addition to enhancing T cell activation and proliferation, ICOS plays an important role in the regulation of T follicular helper cells (4). Research studies suggest that ICOS is a potential therapeutic target, and could serve as a prognostic biomarker for neoplastic therapy involving CTLA-4 blockade (5-7).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: S100A8 and S100A9 are calcium-binding proteins that form a noncovalent heterodimer present in monocytes, neutrophils, macrophages, and some epithelial cells (1, 2). S100A8 and S100A9 are secreted by a tubulin-dependent mechanism during inflammatory conditions and have antimicrobial and chemotactic functions (3-5). Extracellular S100A8/S100A9 also induces an inflammatory response in endothelial cells, including induction of proinflammatory chemokines and adhesion molecules and increased vascular permeability (6). S100A8/S100A9 induces and recruits myeloid-derived suppressor cells (MDSC) in tumor-bearing mice (7). MDSC produce additional S100A8/S100A9 themselves, resulting in a positive feedback mechanism that sustains MDSC accumulation (7). S100A8/S100A9 is also highly expressed in psoriatic skin, where it directly upregulates transcription of complement protein C3, which contributes to disease (8). In addition, tumor-infiltrating myeloid cells induce expression of S100A8 and S100A9 in cancer cells, which increases invasiveness and metastasis (9).

$426
100 µl
APPLICATIONS
REACTIVITY
Human

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

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).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: OX40 (TNFRSF4, CD134) is a member of the tumor necrosis factor (TNF) receptor superfamily that regulates T cell activity and immune responses. The OX40 protein contains four cysteine rich domains, a transmembrane domain, and a cytoplasmic tail containing a QEE motif (1,2). OX40 is primarily expressed on activated CD4+ and CD8+ T-cells, while the OX40 ligand (OX40L, TNFSF4, CD252) is predominantly expressed on activated antigen presenting cells (3-7). The engagement of OX40 with OX40L leads to the recruitment of TNF receptor-associated factors (TRAFs) and results in the formation of a TCR-independent signaling complex. One component of this complex, PKCθ, activates the NF-κB pathway (2,8). OX40 signaling through Akt can also enhance TCR signaling directly (9). Research studies indicate that the OX40L-OX40 pathway is associated with inflammation and autoimmune diseases (10). Additional research studies show that OX40 agonists augment anti-tumor immunity in several cancer types (11,12).

$115
20 µl
$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: TNFRSF18, also known as glucocorticoid-induced tumor necrosis factor-receptor (TNFR)-related protein (GITR) and activation-inducible TNFR family receptor, encodes a type 1 membrane protein of the TNF-receptor superfamily (1). Three alternatively spliced transcript variants encoding distinct isoforms have been reported (2). GITR is an immune cell co-stimulatory receptor expressed constitutively at high levels on CD4+CD25+ T regulatory cells (Tregs), at low levels on naive and memory T cells, and is induced upon T cell activation (3-5). Studies show GITR can also be induced on NK cells, macrophages, and DCs (3, 4, 6). Although GITR does not have intrinsic enzymatic activity, TNFSF18 (also known as GITRL) expressed on antigen presenting cells binds to GITR resulting in recruitment of TNFR-associated factor family members and activation of the NF-kappa-B pathway in T cells (7). GITR ligation has been shown to play a role in CD8+ T cell activation, cytoxicity, and memory T cell survival (8-10). In the thymus, GITR is thought to play a key role in dominant immunological self-tolerance through thymic Treg differentiation and expansion (11). Of note, GITR ligation inhibits Treg suppressive function (12-13) and promotes effector T cell resistance to Treg suppression (14-15). Due to the combined effects on both Treg suppression and effector cell activation, GITR represents a unique opportunity for immunotherapeutic intervention in cancer (16).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: CD14 is a leucine-rich repeat-containing pattern recognition receptor with expression largely restricted to the monocyte/macrophage cell lineage (1). Research studies have shown that CD14 is a bacterial lipopolysaccharide (LPS) binding glycoprotein, expressed as either a GPI-linked membrane protein or a soluble plasma protein (2). LPS induces an upregulation of GPI-linked CD14 expression, which facilitates TLR4 signaling and macrophage activation in response to bacterial infection (3-5).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Forkhead box (Fox) proteins are a family of evolutionarily conserved transcription factors containing a sequence known as Forkhead box or winged helix DNA binding domain (1). The human genome contains 43 Fox proteins that are divided into subfamilies. The FoxP subfamily has four members, FoxP1 - FoxP4, which are broadly expressed and play important roles in organ development, immune response and cancer pathogenesis (2-4). The FoxP subfamily has several characteristics that are atypical among Fox proteins: their Forkhead domain is located at the carboxy-terminal region and they contain motifs that promote homo- and heterodimerization. FoxP proteins usually function as transcriptional repressors (4,5).FoxP3 is crucial for the development of T cells with regulatory properties (Treg) (6). Mutations in FoxP3 are associated with immune dysregulation, polyendocrinopathy, enteropathy, and X-linked syndrome (IPEX) (7), while overexpression in mice causes severe immunodeficiency (8). Research studies have shown that FoxP3 functions as a tumor suppressor in several types of cancer (9-11).

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: The B cell antigen receptor (BCR) is composed of membrane immunoglobulin molecules non-covalently associated with the heterodimeric signaling component, CD79A and CD79B (also known as Igα and Igβ, respectively) (1,2). The presence of this receptor complex is essential for B cell development and function (3). Following antigen binding, CD79A/CD79B heterodimers are phosphorylated and initiate intracellular signaling through Src family kinases, Lyn, Blk, and Fyn, as well as Syk and Btk tyrosine kinases (4,5). The complexity of BCR signaling results in a variety of distinct cellular functions, such as proliferation, tolerance, apoptosis, and differentiation (6). BCR-antigen ligation also leads to internalization of the complex, trafficking to late endosomes, and antigen presentation in major histocompatibility molecules on the B cell surface (7,8). CD79B enhances the phosphorylation of CD79A (9). Alternatively spliced transcript variants encoding different isoforms of CD79B have been identified (10). CD79B is widely expressed on B cell malignancies and may serve as a target for therapeutic intervention (11,12).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: IHC-Leica® Bond™, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin)

Background: Mucins are a family of macromolecules that line and protect the respiratory epithelium from microbes and pollutants in the local environment. Of the family members that are known to date, some are produced in a cell type and tissue-specific manner, suggesting distinct biological roles for members. Some members polymerize after secretion to form gel-like substances that coat the epithelial layer. MUC5AC and MUC5B are members of the family that polymerize in this manner. Others do not polymerize, and others yet, have a transmembrane domain and remain physically attached to the epithelia (1). While it is known that mucins are protective to the respiratory epithelium, it has been reported that changes in expression of mucins are associated with several forms of lung disease such as cystic fibrosis, COPD, asthma, pulmonary fibrosis, and others (2,3,4,1). Multiple epithelial malignancies have been described to show changes in expression, localization, and glycosylation of MUC5AC. This wide association with multiple malignancy types has led to the emergence of MUC5AC as both a prognostic and therapeutic target for cancer (5).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: CD44 is a type I transmembrane glycoprotein that mediates cell-cell and cell-matrix interaction through its affinity for hyaluronic acid (HA) and possibly through other parts of the extracellular matrix (ECM). CD44 is highly polymorphic, possesses a number of alternative splice variants and undergoes extensive post-translational modifications (1,2). Increased surface levels of CD44 are characteristic of T cell activation, and expression of the protein is upregulated during the inflammatory response. Research studies have shown that interactions between CD44 and HER2 are linked to an increase in ovarian carcinoma cell growth (1-3). CD44 interacts with ezrin, radixin and moesin (ERM), linking the actin cytoskeleton to the plasma membrane and the ECM (4-6). CD44 is constitutively phosphorylated at Ser325 in resting cells. Activation of PKC results in phosphorylation of Ser291, dephosphorylation of Ser325, disassociation of ezrin from CD44, and directional motility (4).

$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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: L-arginine plays a critical role in regulating the immune system (1-3). In inflammation, cancer and certain other pathological conditions, myeloid cell differentiation is inhibited leading to a heterogeneous population of immature myeloid cells, known as myeloid-derived suppressor cells (MDSCs). MDSCs are recruited to sites of cancer-associated inflammation and express high levels of arginase-1 (4). Arginase-1 catalyzes the final step of the urea cycle converting L-arginine to L-ornithine and urea (5). Thus MDSCs increase the catabolism of L-arginine resulting in L-arginine depletion in the inflammatory microenvironment of cancer (4,6). The reduced availability of L-arginine suppresses T-cell proliferation and function and thus contributes to tumor progression (4,6). Arginase-1 is of great interest to researchers looking for a therapeutic target to inhibit the function of MDSCs in the context of cancer immunotherapy (7). In addition, research studies have demonstrated that Arginase-1 distinguishes primary hepatocellular carcinoma (HCC) from metastatic tumors in the liver, indicating its value as a potential biomarker in the diagnosis of HCC (8,9).

$145
20 µl
$426
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Programmed cell death 1 ligand 1 (PD-L1, B7-H1, CD274) is a member of the B7 family of cell surface ligands that regulate T cell activation and immune responses. The PD-L1 ligand binds the PD-1 transmembrane receptor and inhibits T cell activation. PD-L1 was discovered following a search for novel B7 protein homologs and was later shown to be expressed by antigen presenting cells, activated T cells, and tissues including placenta, heart, and lung (1-3). Similar in structure to related B7 family members, PD-L1 protein contains extracellular IgV and IgC domains and a short, cytoplasmic region. Research studies demonstrate that PD-L1 is expressed in several tumor types, including melanoma, ovary, colon, lung, breast, and renal cell carcinomas (4-6). Expression of PD-L1 in cancer is associated with tumor infiltrating lymphocytes, which mediate PD-L1 expression through the release of interferon gamma (7). Additional research links PD-L1 expression to cancers associated with viral infections (8,9).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: B7 homolog 3 (B7-H3, CD276) is a member of the B7 family of cell surface ligands that regulate T cell activation and immune responses. B7-H3 protein contains two extracellular Ig-like V-type domains and two IgG-like C2-type domains, a transmembrane domain, and a short intracellular domain (1,2). Early research examining the biological process of B7-H3 suggested that B7-H3 is a positive regulator of T cell response (1). Subsequent research studies indicated that B7-H3 is a negative regulator of T cell response, and that the protein inhibits T cell proliferation (2,3). One possibility is that B7-H3 interacts with two distinct sets of receptors, resulting in seemingly opposite biological outcomes (2). B7-H3 is expressed by antigen presenting cells, activated T cells, and a few normal tissues, including placenta and prostate (1,4,5). Expression of B7-H3 is seen in several cancer types, including prostate, breast, colon, lung, and gastric cancers, and in endothelial cells from tumor associated vasculature (6-8).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: B7 homolog 4 (B7-H4, VTCN1) is a member of the B7 family of cell surface ligands that regulate T cell activation and immune responses (1-3). B7-H4 protein contains two extracellular Ig-like V-type domains, a transmembrane domain, and a short, two amino acid intracellular domain (3). The B7-H4 protein is shown to inhibit T cell activation, proliferation, and cytokine production (1,4,5). Although B7-H4 mRNA is widely expressed, B7-H4 protein is restricted to antigen presenting cells and B cells (1). The B7-H4 protein is also found in several tumor types, including ovarian cancer and breast cancer (6). Research studies indicate that B7-H4 protein is present on the surface of ovarian tumor cells, and that targeted inhibition of B7-H4 using recombinant antibodies restores T cell activation pathways. These studies suggest some potential therapeutic value in blocking B7-H4 function and restoring T cell function in cancer patients (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: IFIT1 (interferon-induced protein with tetratricopeptide repeats 1) belongs to the IFIT family of proteins, which consists of four members in humans (IFIT1, IFIT2, IFIT3, and IFIT5) and three members in mice (IFIT1, IFIT2, and IFIT3) (1). IFIT1 expression is induced by Type I Interferons resulting from viral infection (2). IFIT1 is an antiviral protein that directly binds viral RNA that has a 5’ triphosphate group (PPP-RNA) (2). In humans, the viral PPP-RNA bound IFIT1 forms a complex with IFIT2 and IFIT3 to sequester the viral PPP-RNA and prevent replication (2). IFIT1 has also been shown to inhibit translation by binding to the eukaryotic initiation factor-3 (eIF-3) (3).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Lymphocyte activation gene 3 (LAG-3, CD223) is an immune checkpoint control protein that negatively regulates T cells and immune responses. A CD4-like member of the Ig superfamily, LAG3 contains an extracellular IgV and three IgC domains, a transmembrane domain, and a short cytoplasmic region (1). LAG3 is primarily expressed by activated CD4+ T cells, CD8+ T cells, Tregs and NK cells, where it's activated by MHC Class II molecules, its only known ligand. While it was initially shown to activate Treg cells (2), LAG3 can also inhibit CD8+ T cells (3,4). LAG3 is often co-expressed with PD-1 on the surface of tumor infiltrating lymphocytes, where the two proteins act independently to contribute to tumor-mediated immune suppression (4,5). Blockade of LAG3 is a promising strategy for neoplastic intervention (6).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Actin proteins are major components of the eukaryotic cytoskeleton. At least six vertebrate actin isoforms have been identified. The cytoplasmic β- and γ-actin proteins are referred to as “non-muscle” actin proteins as they are predominantly expressed in non-muscle cells where they control cell structure and motility (1). The α-cardiac and α-skeletal actin proteins are expressed in striated cardiac and skeletal muscles, respectively. The smooth muscle α-actin and γ-actin proteins are found primarily in vascular smooth muscle and enteric smooth muscle, respectively. The α-smooth muscle actin (ACTA2) is also known as aortic smooth muscle actin. These actin isoforms regulate the contractile potential of muscle cells (1).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: c-Kit is a member of the subfamily of receptor tyrosine kinases that includes PDGF, CSF-1, and FLT3/flk-2 receptors (1,2). It plays a critical role in activation and growth in a number of cell types including hematopoietic stem cells, mast cells, melanocytes, and germ cells (3). Upon binding with its stem cell factor (SCF) ligand, c-Kit undergoes dimerization/oligomerization and autophosphorylation. Activation of c-Kit results in the recruitment and tyrosine phosphorylation of downstream SH2-containing signaling components including PLCγ, the p85 subunit of PI3 kinase, SHP2, and CrkL (4). Molecular lesions that impair the kinase activity of c-Kit are associated with a variety of developmental disorders (5), and mutations that constitutively activate c-Kit can lead to pathogenesis of mastocytosis and gastrointestinal stromal tumors (6). Tyr719 is located in the kinase insert region of the catalytic domain. c-Kit phosphorylated at Tyr719 binds to the p85 subunit of PI3 kinase in vitro and in vivo (7).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: CD40, also known as tumor necrosis factor receptor superfamily member 5 (TNFRSF5), is a type I transmembrane protein expressed on the surface of B cells and professional antigen-presenting cells of the immune system, as well as on several non-hematopoietic cell types and cancers (1-4). CD40 interacts with CD40 ligand (CD40L/TNFSF5), which is expressed primarily on activated T cells but has also been reported on blood platelets, mast cells, basophils, NK cells, and B cells (5). Upon engagement with CD40L, CD40 signals through TNF receptor associated factors and MAP kinase signaling pathways, resulting in a wide variety of immune and inflammatory responses, including dendritic cell activation and cross-presentation, T cell-dependent immunoglobulin class switching, memory B cell development, and germinal center formation (6-8). The CD40/CD40L axis is essential for the initiation and progression of cellular and humoral adaptive immunity, and is an important area of interest in the study of tumor immunology, neurodegenerative diseases, vascular diseases, and inflammatory disorders (9-12).