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Monoclonal Antibody Western Blotting Fibrinolysis

Also showing Monoclonal Antibody Western Blotting Regulation of Fibrinolysis

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey

Application Methods: Western Blotting

Background: PAI-1 is a secreted protein that belongs to the serine proteinase inhibitor (serpin) superfamily. It inhibits urokinase and tissue plasminogen activators (uPA and tPA) and thus, reduces the conversion of inactive plasminogen to plasmin (1). PAI-1 regulates fibrinolysis and plays an important role in vessel patency and tissue remodeling. Secreted PAI-1 interacts with the extracellular matrix (ECM) component vitronectin, thereby modulating cell-ECM interactions (2,3). PAI-1 is expressed in a variety of tissues with higher expression in liver, vascular endothelial cells, platelets, macrophages, and adipose tissue (1). Increased levels of PAI-1 are associated with deep vein thrombosis (4). Defects in PAI-1 cause plasminogen activator inhibitor-1 deficiency (PAI-1D), which is characterized by increased bleeding after injury or surgery (5). Research studies have shown that high levels of PAI-1 are associated with obesity, aging, insulin resistance, and type 2 diabetes (6-8). PAI-1 is transcriptionally regulated by TGF-β and mediates TGF-β-induced inhibition of cell migration and invasion in cancer cells (9). Studies have shown PAI-1 to be also involved in fibrosis (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Mouse, Pig, Rat

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

Background: Annexin A2 (ANXA2), also known as lipocortin II or calpactin-1 heavy chain, is a 36 kDa member of the annexin superfamily that binds phospholipids and other proteins in a calcium-dependent manner via annexin repeats (1). Annexin A2 contains four such repeats through which it mediates protein-protein and protein-lipid interactions (1-4). It forms a constitutive heterotetramer with S100A10, acting as a bridge between the actin cytoskeleton, plasma membrane, and endocytotic vesicle machinery (5-7). Originally identified as a protein inhibitor of phospholipase A2, annexin A2 has subsequently been shown to interact with an array of protein and non-protein partners, including F-actin, spectrin, SNARE complexes, RNA, and virus particles (4,6,8,9). Annexin A2 has also been shown to have receptor-like activity and is detected on the surface of macrophages and vascular endothelial cells where it mediates macrophage activation and Factor Xa signaling, respectively (10-13). Upregulation of annexin A2 at the cell surface is thought to be modulated by phosphorylation at Tyr23 by Src (14-18). Interestingly, phosphorylation at Tyr23 has recently been shown to be required for cell surface expression of annexin A2 where it mediates motility, invasiveness, and overall metastatic potential of certain pancreatic cancer cells (19,20). Annexin A2 has also been shown to be heavily phosphorylated on serine residues in response to PKC activation via a pleiotropic mechanism (21-23). For a complete list of curated phosphorylation sites on annexin A2, please see PhosphoSitePlus® at www.phosphosite.org.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The human urokinase-type plasminogen activator receptor (uPAR) is a 55-65 kDa, highly glycosylated, GPI-anchored cell surface receptor (the deglycosylated protein is 35 kDa) (1-3). It is a central player in the plasminogen activation pathway. uPAR binds with high affinity to a serine protease urokinase-type plasminogen activator (uPA) and converts plasminogen to its active form plasmin in a spatially restricted manner on the cell surface (4). Plasmin further carries out the activation of uPA, which is inhibited by serpins, such as plasminogen activator inhibitors (5). Therefore, uPAR plays a key role in regulating extracellular proteolysis. In addition, uPAR plays an important role in regulating cell proliferation, adhesion and mobility (6,7). Research studies have shown that overexpression of uPAR is found in various cancer cells and tissues (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The human urokinase-type plasminogen activator receptor (uPAR) is a 55-65 kDa, highly glycosylated, GPI-anchored cell surface receptor (the deglycosylated protein is 35 kDa) (1-3). It is a central player in the plasminogen activation pathway. uPAR binds with high affinity to a serine protease urokinase-type plasminogen activator (uPA) and converts plasminogen to its active form plasmin in a spatially restricted manner on the cell surface (4). Plasmin further carries out the activation of uPA, which is inhibited by serpins, such as plasminogen activator inhibitors (5). Therefore, uPAR plays a key role in regulating extracellular proteolysis. In addition, uPAR plays an important role in regulating cell proliferation, adhesion and mobility (6,7). Research studies have shown that overexpression of uPAR is found in various cancer cells and tissues (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The adhesive glycoprotein thrombospondin-1 (THBS1, TSP1) localizes to the extracellular matrix (ECM) and mediates interactions between cells and the ECM and among cells. Thrombospondin-1 is a multi-domain, glycosylated protein that interacts with a wide variety of extracellular targets, including matrix metalloproteinases (MMPs), collagens, cell receptors, growth factors, and cytokines (1). The protein structure of THBS1 includes an amino-terminal laminin G-like domain, a von Willebrand factor-binding domain, and multiple thrombospondin (TSP) repeated sequences designated as type I, type II, or type III repeats. Each thrombospondin domain interacts with a distinct type of cell surface ligands or protein targets. The amino-terminal domain interacts with aggrecan, heparin, and integrin proteins. Type I TSP repeats interact with MMPs and CD36, while carboxy-terminal repeats bind the thrombospondin receptor CD47 (1). Through these interactions, THBS1 exerts diverse effects on different signaling pathways, such as VEGF receptor/NO signaling, TGFβ signaling, and the NF-κB pathway (2-5). Thrombospondin-1 is an important regulator of many biological processes, including cell adhesion/migration, apoptosis, angiogenesis, inflammation, vascular function, and cancer development (2-5). The activity of thrombospondin-1 is mainly regulated by extracellular proteases. The metalloproteinase ADAMTS1 cleaves thrombospondin, resulting in the release of peptides with anti-angiogenic properties. Elastase and plasmin proteases degrade the THBS1 protein and down regulate its activity (6). As THBS1 is an important protein inhibitor of angiogenesis, the development of thrombospondin-based compounds and their use in therapeutic studies may provide a beneficial approach to the treatment of cancer (7,8).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: CD141/Thrombomodulin (TM, THBD, BDCA-3) is an integral membrane protein expressed on the surface of endothelial cells (1). Acting as a cofactor with Thrombin, CD141/Thrombomodulin activates and initiates the Protein C anticoagulant pathway (1-2). CD141/Thrombomodulin is expressed by a small subset of human CD11c+ myeloid dendritic cells (3-4). These CD141+XCR1+ dendritic cells cross-present antigens to naïve CD8+ T cells, priming them to become activated cytotoxic CD8+ T cells (3-5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Fibroblast activation protein/seprase (FAP) is a cell surface serine integral membrane protease with roles in tissue remodeling during development and wound healing, as well as in cancer and fibrotic disease. FAP has both dipeptidyl peptidase and endopeptidase activities, and cleaves at N-terminal Xaa-Pro sequences. FAP is highly expressed in tumor stroma, and contributes to migration and invasion of tumor cells, as well as that of endothelial cells into the extracellular matrix. FAP is a useful marker of tumorigenic stroma and of cancer-associated fibroblasts (CAFs) and fibrosis (1,2).