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Monoclonal Antibody Ihc-Leica® bond™ Receptor-Mediated Endocytosis

$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).

$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).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: CD5 is a type-I transmembrane protein belonging to the scavenger receptor cysteine-rich (SRCR) family, characterized by the presence of at least one SRCR domain of 90-110 amino acids. CD5 is expressed by all mature T cells, the B-1a subset of mature B cells, and some leukemic B cells. Its expression is increased in regulatory T and B cells (Tregs/Bregs). Anergic T and B cells also have elevated CD5 expression. Elevated levels of CD5 are also found in many autoimmune disorders (1-3). CD5 is associated with the T cell receptor (TCR) and negatively modulates T cell activation and differentiation. CD5 expression on the tumor infiltrating T lymphocytes is inversely correlated with their antitumor activity (4-6). Recently it was reported that CD5 directly binds to IL6 and can mediate downstream signaling. CD5+ B cells promote tumor growth in animal models (7). Reagents targeting CD5 have been actively pursued as therapeutic interventions for cancer and other conditions (8,9).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: FcγRIIB (CD32B) is a low affinity, IgG Fc-binding receptor expressed on B cells, monocytes, macrophages, and dendritic cells (DCs) (1-3). It is the inhibitory Fc receptor and signals through an immunoreceptor tyrosine-based inhibitory motif (ITIM) within its carboxy-terminal cytoplasmic tail (2). Binding of immune complexes to FcγRIIB results in tyrosine phosphorylation of the ITIM motif at Tyr292 and recruitment of the phosphatase SHIP, which mediates inhibitory effects on immune cell activation (2,4). In this way, FcγRIIB suppresses the effects of activating Fc-binding receptors (3). For example, mice deficient for FcγRIIB have greater T cell and DC responses following injection of immune complexes (5, 6). In addition, FcγRIIB plays a role in B cell affinity maturation (7). Signaling through FcγRIIB in the absence of signaling through the B cell receptor (BCR) is proapoptotic, while signaling through FcγRIIB and the BCR simultaneously attenuates the apoptotic signal and results in selection of B cells with higher antigen affinity (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The mannose receptor (MR/CLEC13D/CD206/MMR/MRC1/Macrophage mannose receptor 1) is an endocytic receptor expressed by populations of dendritic cells, macrophages and nonvascular endothelium (1). The mannose receptor is a heavily glycosylated type I transmembrane protein with three types of extracellular domains and a short carboxy-terminal cytoplasmic domain with no apparent signaling motif (2-4). The extracellular portion of the protein is made up of a CR domain, which binds sulfated glycans, an FNII domain, which binds collagens, and eight C-type lectin domains, which bind carbohydrates containing mannose, fucose or GlcNAc (4-7). The receptor recycles between the plasma membrane and early endosomes (8). Functions include a role in antigen cross-presentation, clearance of endogenous proteins, pathogen detection and trafficking through lymphatic vessels (9-12).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: CD163 is a transmembrane scavenger receptor expressed on the macrophage surface. It has 9 B-type SRCR extracellular domains mediating serum haptoglobin clearing/endocytosis, pathogen binding and signal transduction, and calcium binding (1, 2). CD163 is used as a surface marker of M2 type macrophages, including M2 type tumor associated macrophages (TAMs), which facilitate cancer progression by secreting cytokines to promote angiogenesis, immunosuppression and metastasis (3). Inflammatory stimulation and stress signal can induce extracellular domain shedding of CD163 to generate soluble CD163 (sCD163). The increased sCD163 level in serum is associated with low-grade inflammation in disease conditions (4-7).