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Monoclonal Antibody Immunohistochemistry Paraffin Regulation of Locomotion

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: α-Synuclein is a protein of 140-amino acids expressed abundantly in the brain. α-Synuclein is also the main component of pathogenic Lewy bodies and Lewy neurites. Research studies have shown that mutations of the α-synuclein gene are linked to Parkinson's disease (1).

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

Application Methods: Immunofluorescence (Frozen), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: α-Synuclein is a protein of 140-amino acids expressed abundantly in the brain. α-Synuclein is also the main component of pathogenic Lewy bodies and Lewy neurites. Research studies have shown that mutations of the α-synuclein gene are linked to Parkinson's disease (1).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: α-Synuclein is a protein of 140-amino acids expressed abundantly in the brain. α-Synuclein is also the main component of pathogenic Lewy bodies and Lewy neurites. Research studies have shown that mutations of the α-synuclein gene are linked to Parkinson's disease (1).

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

Application Methods: Immunofluorescence (Frozen), Immunohistochemistry (Paraffin)

Background: Adenosine Receptor A2a (A2AR) is a G-protein-coupled receptor (GPCR). As a member of the purinergic adenosine receptors (A1, A2, and A3), A2AR activates classic G-protein signaling pathways upon binding of adenosine (1). Adenosine is present in all cells and extracellular fluids. Adenosine signaling, via A2AR, is mobilized during both physiological and pathological conditions. For example, adenosine, via A2AR, modulates neuronal function, acting to fine-tune neuronal function (2). A2AR function is modulated, in part, by its ability to form functional heteromers with other GPCRs, including dopamine receptors (D1 and D3), metabotropic glutamate receptors (mGluR5), and others (3). In the brain, A2AR is enriched in the basal ganglia, suggesting that A2AR may be a potential drug target for neurodegenerative diseases like Parkinson’s disease, drug addiction, and psychiatric disorders (4). Outside of the brain, A2AR may act as an immune checkpoint molecule to maintain an immunosuppressive tumor microenvironment, an environment that exhibits relatively elevated adenosine levels (5, 6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin)

Background: Phosphatidylcholine-specific phospholipase D (PLD) hydrolyzes phosphatidylcholine (PC) to produce choline and phosphatidic acid (PA). PA is the precursor of the second messenger, diacylglycerol (DAG). Two isoforms of PLD (PLD1 and PLD2) have been identified so far. Both are regulated by protein kinases, small GTPases and Ca2+ (1). The PLD2 isoform is highly expressed in many cancers, such as colorectal and breast cancers (2,3). PLD2 also acts as a guanine nucleotide exchange factor for the small GTPase Rac2 independent of its phospholipase activity (4).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunohistochemistry (Paraffin)

Background: Podoplanin (aggrus, glycoprotein 36) is a single-pass transmembrane protein belonging to the type-1 family of sialomucin-like glycoproteins. Podoplanin was first described in the rat as a surface glycoprotein that regulated podocyte morphology (1). It is now commonly used as a marker of lymphatic endothelial cells, where its expression is associated with the process of lymphangiogenesis (2). Its role in this regard is presumably due to its putative involvement in regulating actin cytoskeleton dynamics (3). Research studies have shown that podoplanin expression is upregulated in a number of tumor types including colorectal cancers (4), oral squamous cell carcinomas (5), and germ cell tumors (6), with higher expression levels often associated with more aggressive tumors (7). Research studies have suggested a functional role for podoplanin in the stromal microenvironment of tumors. For example, it has been reported that podoplanin expression in cancer-associated fibroblasts (CAFs) is positively associated with a stromal environment that promotes cancer progression (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunohistochemistry (Paraffin)

Background: CD34 is a type I transmembrane glycophosphoprotein expressed by hematopoietic stem/progenitor cells, vascular endothelium and some fibroblasts (1). CD34 expression has been the hallmark used to identify hematopoietic stem cells for many years. CD34+ hematopoietic stem cells expand and differentiate into all the lymphohematopoietic lineages upon cytokine or growth factor stimulation and lose CD34 expression upon differentiation. However, recent studies performed in various laboratories conflict with that convention (2). The extracellular domain of CD34 is homologous to CD43, a protein involved in cell-cell adhesion, and CD34 has been shown to function as a negative regulator of cell adhesion (3). CD34 associates with CrkL but not CrkII, is a substrate for PKC, and activation of PKC is coupled with surface expression of CD34 (1,4).

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunohistochemistry (Paraffin)

Background: Fascin is a monomeric, globular protein that plays a central role in regulating the structure and function of the cortical actin cytoskeleton (1). Fascin promotes cross-linkage of parallel actin filaments during the formation of cell protrusions (lamellipodia and filopodia), and therefore plays an important role in regulating cell migration (2). It has been reported that fascin may also regulate filopodia formation by a mechanism independent of its actin-bundling functions (3), though less is known about this mechanism of action. Research studies have shown that increased fascin expression is associated with increased motility and invasiveness of neoplastic cells, including breast, colon, prostate, and esophageal squamous cell carcinomas (4-6). Fascin binds to the armadillo-repeat domain of β-catenin in vitro and in vivo, and has been shown to co-localize with β-catenin and cadherins at the leading edge of migratory cells (7).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: CD105/Endoglin is an auxiliary receptor for the TGF-β receptor complex, functioning in related signaling pathways (1,2). CD105/Endoglin is a transmembrane protein that exists as a disulfide-linked homodimer. It is mainly expressed in vascular and connective tissues and in endothelial and stromal cells. Upregulated CD105/endoglin expression has been reported during wound healing and tumor vascularization, and in inflammatory tissues and developing embryos (1-4). Mutations inCD105/endoglin have been found to be a causal factor of hereditary hemorrhagic telangiectasia (HHT), a disease characterized by malformation of vascular structure (5,6). The importance of this protein for normal and tumor vascular function makes it a good marker for endothelial cell proliferation as well as a potential therapeutic target in cancer (4-6).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Focal adhesion kinase (FAK) is a widely expressed cytoplasmic protein tyrosine kinase involved in integrin-mediated signal transduction. It plays an important role in the control of several biological processes, including cell spreading, migration, and survival (1). Activation of FAK by integrin clustering leads to autophosphorylation at Tyr397, which is a binding site for the Src family kinases PI3K and PLCγ (2-5). Recruitment of Src family kinases results in the phosphorylation of Tyr407, Tyr576, and Tyr577 in the catalytic domain, and Tyr871 and Tyr925 in the carboxy-terminal region of FAK (6,7).

$303
100 µl
$717
300 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: MEK1 and MEK2, also called MAPK or Erk kinases, are dual-specificity protein kinases that function in a mitogen activated protein kinase cascade controlling cell growth and differentiation (1-3). Activation of MEK1 and MEK2 occurs through phosphorylation of two serine residues at positions 217 and 221, located in the activation loop of subdomain VIII, by Raf-like molecules. MEK1/2 is activated by a wide variety of growth factors and cytokines and also by membrane depolarization and calcium influx (1-4). Constitutively active forms of MEK1/2 are sufficient for the transformation of NIH/3T3 cells or the differentiation of PC-12 cells (4). MEK activates p44 and p42 MAP kinase by phosphorylating both threonine and tyrosine residues at sites located within the activation loop of kinase subdomain VIII.

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

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

Background: MEK1 and MEK2, also called MAPK or Erk kinases, are dual-specificity protein kinases that function in a mitogen activated protein kinase cascade controlling cell growth and differentiation (1-3). Activation of MEK1 and MEK2 occurs through phosphorylation of two serine residues at positions 217 and 221, located in the activation loop of subdomain VIII, by Raf-like molecules. MEK1/2 is activated by a wide variety of growth factors and cytokines and also by membrane depolarization and calcium influx (1-4). Constitutively active forms of MEK1/2 are sufficient for the transformation of NIH/3T3 cells or the differentiation of PC-12 cells (4). MEK activates p44 and p42 MAP kinase by phosphorylating both threonine and tyrosine residues at sites located within the activation loop of kinase subdomain VIII.

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: MEK1 and MEK2, also called MAPK or Erk kinases, are dual-specificity protein kinases that function in a mitogen activated protein kinase cascade controlling cell growth and differentiation (1-3). Activation of MEK1 and MEK2 occurs through phosphorylation of two serine residues at positions 217 and 221, located in the activation loop of subdomain VIII, by Raf-like molecules. MEK1/2 is activated by a wide variety of growth factors and cytokines and also by membrane depolarization and calcium influx (1-4). Constitutively active forms of MEK1/2 are sufficient for the transformation of NIH/3T3 cells or the differentiation of PC-12 cells (4). MEK activates p44 and p42 MAP kinase by phosphorylating both threonine and tyrosine residues at sites located within the activation loop of kinase subdomain VIII.