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Polyclonal Antibody Immunofluorescence Immunocytochemistry Integrin Binding

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Integrins are α/β heterodimeric cell surface receptors that play a pivotal role in cell adhesion and migration, as well as in growth and survival (1,2). The integrin family contains at least 18 α and 8 β subunits that form 24 known integrins having distinct tissue distribution and overlapping ligand specificities (3). Integrins not only transmit signals to cells in response to the extracellular environment (outside-in signaling), but also sense intracellular cues to alter their interaction with extracellular environment (inside-out signaling) (1,2).The αVβ5 integrin is expressed in various tissues and cell types, including endothelia, epithelia and fibroblasts (4). It plays a role in matrix adhesion to VN, FN, SPARC and bone sialoprotein (5) and functions in the invasion of gliomas and metastatic carcinoma cells (6,7). αVβ5 integrin plays a major role in growth-factor-induced tumor angiogenesis, where cooperative signaling by the αVβ5 integrin and growth factors regulates endothelial cell proliferation and survival (8).

$122
20 µl
$303
100 µl
$717
300 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The Syk family protein tyrosine kinase Zap-70 is expressed in T and NK cells and plays a critical role in mediating T cell activation in response to T cell receptor (TCR) engagement (1). Following TCR engagement, Zap-70 is rapidly phosphorylated on several tyrosine residues through autophosphorylation and transphosphorylation by the Src family tyrosine kinase Lck (2-6). Tyrosine phosphorylation correlates with increased Zap-70 kinase activity and downstream signaling events. Expression of Zap-70 is correlated with disease progression and survival in patients with chronic lymphocytic leukemia (7,8).

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

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

Background: The Src family of protein tyrosine kinases, which includes Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, are important in the regulation of growth and differentiation of eukaryotic cells (1). Src activity is regulated by tyrosine phosphorylation at two sites, but with opposing effects. While phosphorylation at Tyr416 in the activation loop of the kinase domain upregulates enzyme activity, phosphorylation at Tyr527 in the carboxy-terminal tail by Csk renders the enzyme less active (2).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Pig, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Paxillin is a multidomain protein that localizes primarily to focal adhesion sites in the extracellular matrix (1). Paxillin is one of the key components of integrin signaling, and tyrosine phosphorylation of paxillin is required for integrin-mediated cytoskeletal reorganization (2). Paxillin is phosphorylated by another focal adhesion component, focal adhesion kinase (FAK), at Tyr118 (3,4). Phospho-Paxillin (Tyr118) may provide a docking site for recruitment of other signaling molecules to focal adhesions. It has been shown that the SH2 domain of Crk binds to the phosphorylated Tyr118 of paxillin (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: βIG-H3 (TGFBI/RGD-CAP/Kerato-epithelin) is a 683-amino acid secretory protein induced by TGF-β that plays a role in cell adhesion, differentiation, and apoptosis (1-4). βIG-H3 contains an internal cysteine-rich EMI domain followed by four fasciclin-1 domains and a carboxy terminal RGD domain (1,2). It contributes to cell adhesion through interactions with integrins as well as a number of extracellular matrix (ECM) proteins including collagen, fibronectin, and laminin (5-7). ECM βIG-H3 is found in a wide variety of tissues (8-12). Mutations in the βIG-H3 gene as well as elevated protein levels are most notably associated with corneal dystrophies (13).

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

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

Background: During their synthesis, secretory proteins translocate into the endoplasmic reticulum (ER) where they are post-translationally modified and properly folded. To reach their native conformation, many secretory proteins require the formation of intra- or inter-molecular disulfide bonds (1). This process is called oxidative protein folding. Protein disulfide isomerase (PDI) catalyzes the formation and isomerization of these disulfide bonds (2). Studies on mechanisms of oxidative folding suggest that molecular oxygen oxidizes the ER-protein Ero1, which in turn oxidizes PDI through disulfide exchange (3). This event is then followed by PDI-catalyzed disulfide bond formation in folding proteins (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: α-Actinin belongs to the spectrin family of cytoskeletal proteins. It was first recognized as an actin cross-linking protein, forming an antiparallel homodimer with an actin binding head at the amino terminus of each monomer. The α-actinin protein interacts with a large number of proteins involved in signaling to the cytoskeleton, including those involved in cellular adhesion, migration, and immune cell targeting (1). The interaction of α-actinin with intercellular adhesion molecule-5 (ICAM-5) helps to promote neurite outgrowth (2). In osteoblasts, interaction of α-actinin with integrins stabilizes focal adhesions and may protect cells from apoptosis (3). The cytoskeletal α-actinin isoforms 1 and 4 (ACTN1, ACTN4) are non-muscle proteins that are present in stress fibers, sites of adhesion and intercellular contacts, filopodia, and lamellipodia. The muscle isoforms 2 and 3 (ACTN2, ACTN3) localize to the Z-discs of striated muscle and to dense bodies and plaques in smooth muscle (1).