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Monoclonal Antibody Ihc-Leica® bond™ Aging

Also showing Monoclonal Antibody Ihc-Leica® bond™ Cell Aging

$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).

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

Application Methods: Flow Cytometry, IHC-Leica® Bond™, Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), 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).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Tissue Factor (TF)/CD142 (Coagulation factor III/Thromboplastin) is a type-I transmembrane glycoprotein that serves as the cell surface receptor and cofactor for blood coagulation factors VII and VIIa, and thus plays a central role in hemostasis and thrombosis (1). The TF:VIIa receptor-ligand complex is widely recognized as the initiator of the extrinsic blood coagulation protease cascade, which ultimately leads to the generation of fibrin and thrombin (1). A member of the type-II cytokine receptor superfamily, TF has also been shown to engage the PI3K (2) and MAPK (3) signaling cascades upon binding to factor VIIa in order to drive cellular responses such as cell migration, growth, and proliferation. Although the function of TF under physiologic conditions is to coordinate blood clotting in response to tissue damage, TF is implicated in pathologic conditions such as tumorigenesis. Indeed, TF is aberrantly expressed in colorectal cancer, breast cancer, pancreatic cancer, and glioblastoma multiforme (4). It has been shown to promote tumor angiogenesis, tumor growth, metastasis, and venous thrombosis (5). Given that TF overexpression is associated with numerous types of solid tumors, it has garnered much attention as a potential therapeutic target.

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: CD80 (B7-1, BB1) and CD86 (B7-2, B70) are members of the B7 family of cell surface ligands that regulate T cell activation and immune responses. CD80 is expressed on activated antigen presenting cells, including dendritic cells, B cells, monocytes, and macrophages. CD86 is expressed on resting monocytes, dendritic cells, activated B lymphocytes, and can be further upregulated in the presence of inflammation (1-3). CD80 and CD86 are ligands for CD28, which functions as a T cell costimulatory receptor. Interaction of CD28 with CD80 or CD86 provides the second signal required for naïve T cell activation, T cell proliferation, and acquisition of effector functions (3-7). Alternatively, CD80 and CD86 also act as ligands to CTLA-4, which results in the downregulation of T cell activity (3,7-9).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Intercellular cell adhesion molecule-1 (CD54 or ICAM-1) is a cell surface glycoprotein that belongs to the immunoglobulin superfamily (IgSF) of adhesion molecules. CD54 is expressed at low levels in diverse cell types, and is induced by cytokines (TNF-α, interleukin-1) and bacterial lipopolysaccharide (1). Apical localization of CD54 on endothelial cells (or basolateral localization on epithelial cells) is a prerequisite for leukocyte trafficking through the endothelial (or epithelial) barrier (1). Apical expression of CD54 on epithelial cells mediates pathogen invasion as well as host defense, a pattern also observed in tumors (1). CD54 also functions as a co-stimulator on antigen presenting cells, binding to its receptor LFA-1 (leukocyte function-associated antigen-1) on the surface of T cells during antigen presentation (2). Cross-linking of CD54 or binding to its ligand triggers activation of Src family kinases and the Rho/ROCK pathway (3-7). Phosphorylation on Tyr485 of CD54 is required for its association with SHP-2 (5). SHP-2 seems essential for CD54-induced Src activation (7).