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Product listing: Pan-Cadherin Antibody, UniProt ID P12830 #4068 to Scribble Antibody, UniProt ID Q14160 #4475

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, D. melanogaster, Human, Monkey, Mouse, Rat, Zebrafish

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

Background: Cadherins are a superfamily of transmembrane glycoproteins that contain cadherin repeats of approximately 100 residues in their extracellular domain. Cadherins mediate calcium-dependent cell-cell adhesion and play critical roles in normal tissue development (1). The classic cadherin subfamily includes N-, P-, R-, B-, and E-cadherins, as well as about ten other members that are found in adherens junctions, a cellular structure near the apical surface of polarized epithelial cells. The cytoplasmic domain of classical cadherins interacts with β-catenin, γ-catenin (also called plakoglobin), and p120 catenin. β-catenin and γ-catenin associate with α-catenin, which links the cadherin-catenin complex to the actin cytoskeleton (1,2). While β- and γ-catenin play structural roles in the junctional complex, p120 regulates cadherin adhesive activity and trafficking (1-4). Investigators consider E-cadherin an active suppressor of invasion and growth of many epithelial cancers (1-3). Research studies indicate that cancer cells have upregulated N-cadherin in addition to loss of E-cadherin. This change in cadherin expression is called the "cadherin switch." N-cadherin cooperates with the FGF receptor, leading to overexpression of MMP-9 and cellular invasion (3). Research studies have shown that in endothelial cells, VE-cadherin signaling, expression, and localization correlate with vascular permeability and tumor angiogenesis (5,6). Investigators have also demonstrated that expression of P-cadherin, which is normally present in epithelial cells, is also altered in ovarian and other human cancers (7,8).

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

Application Methods: 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).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: In multicellular organisms, intercellular junctions play essential roles in tissue integrity and maintenance of cell polarity. Tight junctions (TJs) form a continuous barrier to fluids across the epithelium and endothelium (reviewed in 1). Adherens junctions (AJs) are dynamic structures that form cell-cell contacts linking cells into a continuous sheet (reviewed in 2). The actin filament-binding protein, Afadin, binds to nectin forming a connection to the actin cytoskeleton (3). AJs are formed when nectin assembles cadherin at the cell-cell adhesion site and these junctions are then involved in the formation and maintenance of TJs (4,5). Afadin has two splice variants: l-afadin, which is ubiquitously expressed, and s-afadin, which is expressed predominantly in neural tissue. s-Afadin is a shorter form lacking one of the three proline-rich regions found in l-afadin, as well as the carboxyl-terminal F-actin binding region (6). Human s-afadin is identical to AF-6, the ALL-1 fusion partner involved in acute myeloid leukemias (7). Recent work has also shown that afadin is involved in controlling the directionality of cell movement when it is localized at the leading edge of moving cells (8,9).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Catenin δ-1 (p120 catenin) has an amino-terminal coiled-coil domain followed by a regulatory domain containing multiple phosphorylation sites and a central Armadillo repeat domain of ten linked 42-amino acid repeats. The carboxy-terminal tail has no known function (1). Catenin δ-1 fulfills critical roles in the regulation of cell-cell adhesion as it regulates E-cadherin turnover at the cell surface to determine the level of E-cadherin available for cell-cell adhesion (2). Catenin δ-1 has both positive and negative effects on cadherin-mediated adhesion (3). Actin dynamics are also regulated by catenin δ-1, which modulates RhoA, Rac, and cdc42 proteins (1). Analogous to β-catenin, catenin δ-1 translocates to the nucleus, although its role at this location is unclear. Many studies show that catenin δ-1 is expressed irregularly or is absent in various types of tumor cells, suggesting that catenin δ-1 may function as a tumor suppressor (4).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Catenin δ-1 (p120 catenin) has an amino-terminal coiled-coil domain followed by a regulatory domain containing multiple phosphorylation sites and a central Armadillo repeat domain of ten linked 42-amino acid repeats. The carboxy-terminal tail has no known function (1). Catenin δ-1 fulfills critical roles in the regulation of cell-cell adhesion as it regulates E-cadherin turnover at the cell surface to determine the level of E-cadherin available for cell-cell adhesion (2). Catenin δ-1 has both positive and negative effects on cadherin-mediated adhesion (3). Actin dynamics are also regulated by catenin δ-1, which modulates RhoA, Rac, and cdc42 proteins (1). Analogous to β-catenin, catenin δ-1 translocates to the nucleus, although its role at this location is unclear. Many studies show that catenin δ-1 is expressed irregularly or is absent in various types of tumor cells, suggesting that catenin δ-1 may function as a tumor suppressor (4).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Catenin δ-1 (p120 catenin) has an amino-terminal coiled-coil domain followed by a regulatory domain containing multiple phosphorylation sites and a central Armadillo repeat domain of ten linked 42-amino acid repeats. The carboxy-terminal tail has no known function (1). Catenin δ-1 fulfills critical roles in the regulation of cell-cell adhesion as it regulates E-cadherin turnover at the cell surface to determine the level of E-cadherin available for cell-cell adhesion (2). Catenin δ-1 has both positive and negative effects on cadherin-mediated adhesion (3). Actin dynamics are also regulated by catenin δ-1, which modulates RhoA, Rac, and cdc42 proteins (1). Analogous to β-catenin, catenin δ-1 translocates to the nucleus, although its role at this location is unclear. Many studies show that catenin δ-1 is expressed irregularly or is absent in various types of tumor cells, suggesting that catenin δ-1 may function as a tumor suppressor (4).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: CUB domain containing protein 1 (CDCP1, SIMA135) is a putative stem cell marker shown in research studies to be highly expressed in some human cancer cells and in both typical and atypical (cancerous) colons (1). Expression of CDCP1 may be epigenetically regulated, as methylation of promoter CpG sequences results in decreased CDCP1 expression (2). The corresponding CDCP1 gene encodes a glycoprotein that acts as a complex, multidomain transmembrane antigen. CDCP1 has three extracellular CUB domains that may be involved in cell adhesion or extracellular matrix interactions (1,3). Src-family kinases may phosphorylate CDCP1 at five tyrosine residues within its cytoplasmic domain to provide a potential binding site for SH2 domain-containing proteins (3). CDCP1 is a putative hematopoietic stem cell marker (4,5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: CUB domain containing protein 1 (CDCP1, SIMA135) is a putative stem cell marker shown in research studies to be highly expressed in some human cancer cells and in both typical and atypical (cancerous) colons (1). Expression of CDCP1 may be epigenetically regulated, as methylation of promoter CpG sequences results in decreased CDCP1 expression (2). The corresponding CDCP1 gene encodes a glycoprotein that acts as a complex, multidomain transmembrane antigen. CDCP1 has three extracellular CUB domains that may be involved in cell adhesion or extracellular matrix interactions (1,3). Src-family kinases may phosphorylate CDCP1 at five tyrosine residues within its cytoplasmic domain to provide a potential binding site for SH2 domain-containing proteins (3). CDCP1 is a putative hematopoietic stem cell marker (4,5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: CUB domain containing protein 1 (CDCP1, SIMA135) is a putative stem cell marker shown in research studies to be highly expressed in some human cancer cells and in both typical and atypical (cancerous) colons (1). Expression of CDCP1 may be epigenetically regulated, as methylation of promoter CpG sequences results in decreased CDCP1 expression (2). The corresponding CDCP1 gene encodes a glycoprotein that acts as a complex, multidomain transmembrane antigen. CDCP1 has three extracellular CUB domains that may be involved in cell adhesion or extracellular matrix interactions (1,3). Src-family kinases may phosphorylate CDCP1 at five tyrosine residues within its cytoplasmic domain to provide a potential binding site for SH2 domain-containing proteins (3). CDCP1 is a putative hematopoietic stem cell marker (4,5).

$303
100 µl
APPLICATIONS
REACTIVITY
Dog, Hamster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Connexin 43 (Cx43) is a member of the large family of gap junction proteins. Connexins assemble as a hexamer and are transported to the plasma membrane to create a hemichannel that can associate with hemichannels on nearby cells to create cell-to-cell channels. Clusters of these channels assemble to make gap junctions. Gap junction communication is important in development and regulation of cell growth. Phosphorylation of Cx43 is important in regulating assembly and function of gap junctions (1,2). Ser368 of Cx43 is phosphorylated by protein kinase C (PKC) after activation by phorbol esters, which decreases cell-to-cell communication (3). Src can interact with and phosphorylate Cx43 to alter gap junction communication (4,5).

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

Application Methods: Western Blotting

Background: Desmosomes are a class of intracellular junction that tightly link adjacent cells in mechanically stressed tissues such as the epithelium and myocardium (1). They derive their characteristic strength from the protein Desmoplakin, which acts as a tether by binding the cytoplasmic component of the Desmosome at it’s N-terminus (2) while its C-terminus is anchored to the intermediate-filament cytoskeleton (3). This association mitigates the impact of mechanical forces on the desmosome by distributing them throughout the cytoskeleton and tissue (4). Desmoplakin is essential for normal desmosomal adhesion (5); defects can result in pathologies that include cardiomyopathy (6), keratoderma (7), or the skin blistering disease Epidermolysis bullosa (8).

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

Application Methods: 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).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: 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).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: 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
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: p130 Cas (Crk-associated substrate) is a docking protein containing multiple protein-protein interaction domains. The amino-terminal SH3 domain may function as a molecular switch regulating CAS tyrosine phosphorylation, as it interacts with focal adhesion kinase (FAK) (1) and the FAK-related kinase PYK2 (2), as well as the tyrosine phosphatases PTP-1B (3) and PTP-PEST (4). The carboxy-terminal Src binding domain (SBD) contains a proline-rich motif that mediates interaction with the SH3 domains of Src-family kinases (SFKs) and a tyrosine phosphorylation site (Tyr668 and/or Tyr670) that can promote interaction with the SH2 domain of SFKs (5). The p130 Cas central substrate domain, the major region of tyrosine phosphorylation, is characterized by 15 tyrosines present in Tyr-X-X-Pro (YXXP) motifs, including Tyr165, 249, and 410. When phosphorylated, most YXXP motifs are able to serve as docking sites for proteins with SH2 or PTB domains including adaptors, C-Crk, Nck, and inositol 5'-phosphatase 2 (SHIP2) (6). The tyrosine phosphorylation of p130 Cas has been implicated as a key signaling step in integrin control of normal cellular behaviors including motility, proliferation, and survival. Aberrant Cas tyrosine phosphorylation may contribute to cell transformation by certain oncoproteins (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: p130 Cas (Crk-associated substrate) is a docking protein containing multiple protein-protein interaction domains. The amino-terminal SH3 domain may function as a molecular switch regulating CAS tyrosine phosphorylation, as it interacts with focal adhesion kinase (FAK) (1) and the FAK-related kinase PYK2 (2), as well as the tyrosine phosphatases PTP-1B (3) and PTP-PEST (4). The carboxy-terminal Src binding domain (SBD) contains a proline-rich motif that mediates interaction with the SH3 domains of Src-family kinases (SFKs) and a tyrosine phosphorylation site (Tyr668 and/or Tyr670) that can promote interaction with the SH2 domain of SFKs (5). The p130 Cas central substrate domain, the major region of tyrosine phosphorylation, is characterized by 15 tyrosines present in Tyr-X-X-Pro (YXXP) motifs, including Tyr165, 249, and 410. When phosphorylated, most YXXP motifs are able to serve as docking sites for proteins with SH2 or PTB domains including adaptors, C-Crk, Nck, and inositol 5'-phosphatase 2 (SHIP2) (6). The tyrosine phosphorylation of p130 Cas has been implicated as a key signaling step in integrin control of normal cellular behaviors including motility, proliferation, and survival. Aberrant Cas tyrosine phosphorylation may contribute to cell transformation by certain oncoproteins (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: p130 Cas (Crk-associated substrate) is a docking protein containing multiple protein-protein interaction domains. The amino-terminal SH3 domain may function as a molecular switch regulating CAS tyrosine phosphorylation, as it interacts with focal adhesion kinase (FAK) (1) and the FAK-related kinase PYK2 (2), as well as the tyrosine phosphatases PTP-1B (3) and PTP-PEST (4). The carboxy-terminal Src binding domain (SBD) contains a proline-rich motif that mediates interaction with the SH3 domains of Src-family kinases (SFKs) and a tyrosine phosphorylation site (Tyr668 and/or Tyr670) that can promote interaction with the SH2 domain of SFKs (5). The p130 Cas central substrate domain, the major region of tyrosine phosphorylation, is characterized by 15 tyrosines present in Tyr-X-X-Pro (YXXP) motifs, including Tyr165, 249, and 410. When phosphorylated, most YXXP motifs are able to serve as docking sites for proteins with SH2 or PTB domains including adaptors, C-Crk, Nck, and inositol 5'-phosphatase 2 (SHIP2) (6). The tyrosine phosphorylation of p130 Cas has been implicated as a key signaling step in integrin control of normal cellular behaviors including motility, proliferation, and survival. Aberrant Cas tyrosine phosphorylation may contribute to cell transformation by certain oncoproteins (5).

$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).

$303
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: PZR (Protein zero related) is an immunoglobulin superfamily protein that specifically binds the tyrosine phosphatase SHP-2 through its intracellular immunoreceptor tyrosine-based inhibitory motifs (ITIMs) (1,2). PZR is phosphorylated by c-Src, c-Fyn, c-Lyn, Csk, and c-Abl (3). PP1, a Src family kinase inhibitor, inhibits PZR phosphorylation (4,5). There are three alternatively spliced isoforms, designated as PZR, PZRa, and PZRb; both PZRa and PZRb lack ITIMs (6,7). PZR is the main receptor of ConA and has an important role in cell signaling via c-Src (4). PZR is expressed in many cell types and is localized to cell contacts and intracellular granules in BAECs and mesothelioma (REN) cells. PZR has been implicated as a cell adhesion protein that may be involved in SHP-2-dependent signaling at interendothelial cell contacts (3). Hypertyrosine phosphorylation of PZR was observed during embryogenesis in a mouse model of Noonan syndrome (8).

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

Application Methods: Western Blotting

Background: Focal adhesions connect the cytoskeleton with the extracellular matrix (ECM), a complex structure of secreted macromolecules that surrounds mammalian organs and tissues. Integrins clustered on the extracellular side of focal adhesions signal from the ECM to intracellular protein complexes, which in turn signal to the actin cytoskeleton to regulate the tension needed for cell motility. Internal signals also converge on focal adhesions to regulate integrin affinity and avidity. Signaling through focal adhesions regulates cell adhesion, migration, proliferation, apoptosis, and gene expression, and impacts cellular processes such as development, wound healing, immune response, invasion, metastasis, and angiogenesis (reviewed in 1-3). Talin is a large, multidomain focal adhesion protein that interacts with the intracellular domains of integrins and other focal adhesion proteins. Talin is involved in the formation of focal adhesions and in linking focal adhesions to the actin cytoskeleton (4). The interaction between talin and integrins increases the affinity between integrin and both insoluble and soluble ECM proteins (5,6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: The zyxin family of proteins includes LIMD1, ajuba, trip6 and zyxin, each of which contains three LIM domains at the carboxy-terminus. Zyxin family members associate with the actin cytoskeleton and are components of both the cell-cell junction adhesive complex and the integrin-mediated adhesive complex. They shuttle in and out of the nucleus where they may function in transcriptional activation (1).Zyxin is involved in the regulation of mechanical force-induced actin polymerization at focal adhesions (2), and in regulation of adhesion and migration, possibly through recruitment of Ena/VASP proteins to focal adhesions (3). Zyxin interacts with and may regulate the function of the tumor suppressor myopodin, which inhibits tumor growth and metastasis (4).

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

Application Methods: Western Blotting

Background: Adherens junctions are dynamic structures that form cell-cell contacts and are important in development, differentiation, tissue integrity, morphology and cell polarity. They are composed of the transmembrane proteins, cadherins, which bind cadherins on adjacent cells in a calcium-dependent manner. On the cytoplasmic side of adherens junctions, the classic model states that cadherins are linked to the cytoskeleton through β- and α-catenin. α-E-catenin is ubiquitously expressed, α-N-catenin is expressed in neuronal tissue, and α-T-catenin is primarily expressed in heart tissue. Research studies have demonstrated that loss of E-cadherin and α-E-catenin occurs during the progression of several human cancers, indicating that the breakdown of adherens junctions is important in cancer progression (reviewed in 1).Research studies also suggest that, rather than acting as a static link between cadherins and actin, α-catenin regulates actin dynamics directly, possibly by competing with the actin nucleating arp2/3 complex (2,3). α-catenin also plays a role in regulating β-catenin-dependent transcriptional activity, affecting differentiation and response to Wnt signaling. α-catenin binds to β-catenin in the nucleus, preventing it from regulating transcription, and levels of both proteins appear to be regulated via proteasome-dependent degradation (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Adherens junctions are dynamic structures that form cell-cell contacts and are important in development, differentiation, tissue integrity, morphology and cell polarity. They are composed of the transmembrane proteins, cadherins, which bind cadherins on adjacent cells in a calcium-dependent manner. On the cytoplasmic side of adherens junctions, the classic model states that cadherins are linked to the cytoskeleton through β- and α-catenin. α-E-catenin is ubiquitously expressed, α-N-catenin is expressed in neuronal tissue, and α-T-catenin is primarily expressed in heart tissue. Research studies have demonstrated that loss of E-cadherin and α-E-catenin occurs during the progression of several human cancers, indicating that the breakdown of adherens junctions is important in cancer progression (reviewed in 1).Research studies also suggest that, rather than acting as a static link between cadherins and actin, α-catenin regulates actin dynamics directly, possibly by competing with the actin nucleating arp2/3 complex (2,3). α-catenin also plays a role in regulating β-catenin-dependent transcriptional activity, affecting differentiation and response to Wnt signaling. α-catenin binds to β-catenin in the nucleus, preventing it from regulating transcription, and levels of both proteins appear to be regulated via proteasome-dependent degradation (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Plasminogen is the inactive, proenzyme precursor to the serine protease plasmin that degrades fibrin within blood clots, promotes cell migration through proteolytic degradation of extracellular matrix proteins, and regulates angiogenesis and wound healing through activation of matrix metalloproteases (1-4). Inactive plasminogen is produced and secreted by liver cells and is found in the circulatory system and extracellular fluids (1). The plasminogen protein is composed of an amino terminal preactivation peptide followed by five kringle domains and a serine proteinase domain (5). The plasminogen zymogen binds to sites on the cell surface and is subsequently cleaved to release the active serine proteinase plasmin. Identified plasminogen cell surface receptors (including S100A10, enolase and PLGRKT) share carboxy-terminal lysine residues that interact with plasminogen kringle domains, resulting in cell surface localization of plasminogen (6-8). Cleavage of plasminogen can be catalyzed by a number of distinct enzymes, including tissue specific plasminogen activator (tPA), urokinase plasminogen activator (uPA), and kallikrein (1). An additional plasminogen cleavage product is the angiogenesis inhibitor angiostatin, which is derived from the first four kringle domains (9). A number of related angiogenesis inhibitors, derived from various parts of the plasminogen kringle region, have been shown to inhibit endothelial cell growth and proliferation (10). Mutations in the corresponding PLG gene have been linked to plasminogen deficiencies, characterized by decreased plasmin expression and ligneous conjunctivitis in some individuals (11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Receptor type protein tyrosine phosphatase F (PTPRF, LAR) is a transmembrane PTP that helps to regulate insulin signaling, cell proliferation and cell migration. The PTPRF protein is composed of an extracellular segment that contains several Ig-like and fibronectin (Fn-III) domains, a transmembrane region and a pair of cytoplasmic phosphatase domains (1,2). Functional studies reveal that the membrane-associated D1 phosphatase domain is responsible for substrate dephosphorylation, while the D2 domain is important for substrate specificity (3). PTPRF negatively regulates insulin signaling through dephosphorylation of insulin receptor and insulin receptor substrate (4). This phosphatase activates the pro-apoptotic DAPK serine/threonine kinase by removing a phosphate at Tyr491/492, while the kinase Src replaces the phosphate to inactivate DAPK at the same time it down regulates PTPRF expression (5). PTPRF is commonly found at focal adhesions where it interacts with liprin, which localizes the phosphatase to the membrane, and the Rac/Rho family GTPase Trio (6). Localization of PTPRF at adherens junctions results in PTPRF modification of β-catenin, which inhibits cell migration by limiting the amount of available cytosolic β-catenin (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: PZR (Protein zero related) is an immunoglobulin superfamily protein that specifically binds the tyrosine phosphatase SHP-2 through its intracellular immunoreceptor tyrosine-based inhibitory motifs (ITIMs) (1,2). PZR is phosphorylated by c-Src, c-Fyn, c-Lyn, Csk, and c-Abl (3). PP1, a Src family kinase inhibitor, inhibits PZR phosphorylation (4,5). There are three alternatively spliced isoforms, designated as PZR, PZRa, and PZRb; both PZRa and PZRb lack ITIMs (6,7). PZR is the main receptor of ConA and has an important role in cell signaling via c-Src (4). PZR is expressed in many cell types and is localized to cell contacts and intracellular granules in BAECs and mesothelioma (REN) cells. PZR has been implicated as a cell adhesion protein that may be involved in SHP-2-dependent signaling at interendothelial cell contacts (3). Hypertyrosine phosphorylation of PZR was observed during embryogenesis in a mouse model of Noonan syndrome (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Reg4 (regenerating islet-derived protein 4) is a member of a multigene family of Reg proteins (1). Reg proteins are secreted glycoproteins belonging to the calcium (C-type) dependent lectin superfamily, although they can in fact bind polysaccharides, mannan, and heparin in the absence of calcium (2,3). Reg4 is expressed in the gastrointestinal (GI) tract, in normal colon mucosa, and is up-regulated in colon adenocarcinoma, pancreatic cancer, gastric adenocarcinoma, inflammatory bowel disease (Crohn’s disease and ulcerative colitis) (4,5).It has recently been shown that Reg4 marks a population of deep secretory cells at the bottom of the crypts in the colon. In the upper gastrointestinal tract, Paneth cells support the Lgr5+ positive stem cells that reside at the base of deep crypts by providing signals such as Wnt3, EGF, and Notch ligands for stem cell maintenance. No Paneth cells however exist in the colon crypts. It is proposed that the Reg4+ population serves as an analogous support system for the LGR5+ positive stem cell population in the colon (1,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Renin is a secreted proteinase whose enzymatic activity is to convert angiotensinogen into angiotensin I in the plasma, initiating a process that results in an elevation of blood pressure and increased sodium retention by the kidney (1). Renin is synthezed in kidney as a procursor, prorenin, which is released into circulation. Both renin and prorenin can bind to (pro)renin receptor and induce angiotensin-independent signaling events leading to activation of MAPKs and up-regulation of TGF-β1 and matrix proteins (2, 3). Defects in renin can cause renal tubular dysgenesis, a severe autosomal recessive disorder of renal tubular development (4, 5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Receptor for Hyaluronic acid-Mediated Motility (RHAMM, known also as CD168 or HMMR) was first identified as a putative receptor for hyaluronic acid (HA) that modulated HA-mediated cell motility (1). RHAMM/CD168 is functionally similar to the HA receptor CD44; however in contrast to CD44, RHAMM/CD168 does not contain a transmembrane domain or a signal peptide leader sequence, and so is not targeted exclusively to the cell membrane (1). RHAMM/CD168 has multiple isoforms; some are reportedly exported to the cell membrane in response to signaling by growth factors and cytokines (e.g., TGF-β) (2, 3), whereas others have been implicated in intracellular functions including mitotic spindle regulation (4). Cell surface RHAMM/CD168 is localized to membrane ruffles, consistent with proteins that regulate cell motility (1). Numerous research studies have reported that the expression of RHAMM/CD168 is positively associated with cancer cell growth, motility and/or metastasis (5-7), in addition to HA-mediated inflammation (8), suggesting the potential for therapeutic approaches that target HA-receptor mediated signaling (9,10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Scribble (Scrib) was originally identified in a genetic screen in Drosophila along with cell polarity determinants Discs Large (Dlg) and Lethal giant larvae (Lgl). Drosophila mutants homozygous for these genes share similar phenotypes, including the loss of apicobasal cell polarity and neoplastic tissue overgrowth. These phenotypic similarities suggest that these three proteins function in a common pathway important for establishing and maintaining apicobasal polarity in epithelial cells (1,2). Scribble contains many leucine-rich repeats and PDZ domains important for localizing scribble to adherens junctions and basolateral regions of mammalian epithelial cells (3). Scribble reportedly binds β-catenin, APC, E-cadherin and the E6 protein from high-risk virus type of HPV through a short motif important for E6-induced cell transformation (4-8). Overexpression of scribble inhibits transformation of rodent epithelial cells by HPV E6/7 proteins (8).