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Dog Polyclonal Antibody

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Chicken, D. melanogaster, Dog, Guinea Pig, Hamster, Human, Monkey, Mouse, Pig, Rat

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

Background: Akt, also referred to as PKB or Rac, plays a critical role in controlling survival and apoptosis (1-3). This protein kinase is activated by insulin and various growth and survival factors to function in a wortmannin-sensitive pathway involving PI3 kinase (2,3). Akt is activated by phospholipid binding and activation loop phosphorylation at Thr308 by PDK1 (4) and by phosphorylation within the carboxy terminus at Ser473. The previously elusive PDK2 responsible for phosphorylation of Akt at Ser473 has been identified as mammalian target of rapamycin (mTOR) in a rapamycin-insensitive complex with rictor and Sin1 (5,6). Akt promotes cell survival by inhibiting apoptosis through phosphorylation and inactivation of several targets, including Bad (7), forkhead transcription factors (8), c-Raf (9), and caspase-9. PTEN phosphatase is a major negative regulator of the PI3 kinase/Akt signaling pathway (10). LY294002 is a specific PI3 kinase inhibitor (11). Another essential Akt function is the regulation of glycogen synthesis through phosphorylation and inactivation of GSK-3α and β (12,13). Akt may also play a role in insulin stimulation of glucose transport (12). In addition to its role in survival and glycogen synthesis, Akt is involved in cell cycle regulation by preventing GSK-3β-mediated phosphorylation and degradation of cyclin D1 (14) and by negatively regulating the cyclin dependent kinase inhibitors p27 Kip1 (15) and p21 Waf1/Cip1 (16). Akt also plays a critical role in cell growth by directly phosphorylating mTOR in a rapamycin-sensitive complex containing raptor (17). More importantly, Akt phosphorylates and inactivates tuberin (TSC2), an inhibitor of mTOR within the mTOR-raptor complex (18,19).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Tight junctions, or zona occludens, form a continuous barrier to fluids across the epithelium and endothelium. They function in regulation of paracellular permeability and in the maintenance of cell polarity, blocking the movement of transmembrane proteins between the apical and the basolateral cell surfaces (reviewed in 1). Zona occludens proteins ZO-1, -2, and -3 (also known as TJP1, 2, and 3) are peripheral membrane adaptor proteins that link junctional transmembrane proteins such as occludin and claudin to the actin cytoskeleton (reviewed in 2). ZO-1 and -2 are required for tight junction formation and function (3,4). In subconfluent proliferating cells, ZO-1 and ZO-2 have been shown to colocalize to the nucleus and play a role in transcriptional regulation, possibly through facilitating nuclear import/export of transcriptional regulators (5-7). The ZO-2 gene is transcribed from two promoters, generating the ZO-2A and ZO-2C isoforms. ZO-2C lacks a 23 amino acid amino-terminal sequence found in other ZO-2 isoforms. While both isoforms appear to be widely expressed, abnormal regulation of the ZO-2 gene may be correlated with development of ductal cancer (8).

$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).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The extracellular matrix (ECM) is a complex structure of secreted macromolecules surrounding mammalian organs and tissues. Controlled interactions between cells and the ECM are important in proliferation, migration, survival, polarity, and differentiation. Cells contact the ECM primarily through heterodimeric integral membrane proteins called integrins. Integrins connect the ECM to the cytoskeleton, and therefore the cell signaling machinery, through protein complexes called focal adhesions (1).The ILK/PINCH/Parvin (IPP) complex is composed of three highly conserved proteins recruited to sites of ECM contact as pre-assembled structures. The IPP acts at the interface of the integrin/actin connection to regulate formation of focal adhesions and integrin signaling. All three proteins contain multiple protein binding domains allowing them to function as adaptor proteins in the formation of focal adhesions. ILK (integrin-linked kinase) also has a catalytic (protein Ser/Thr kinase) domain, and may or may not function as a kinase in vivo. Roles for IPP proteins outside of the IPP complex have been proposed, including regulation of gene expression (2,3).The parvin family consists of 3 members, α-parvin/actopaxin, β-parvin/affixin, and γ-parvin. α-parvin and β-parvin are expressed ubiquitously, while expression of γ-parvin is restricted to hematopoietic cells (4). α-parvin binds to f-actin both directly and via interaction with the focal adhesion protein paxillin (5). α-parvin regulates cell spreading and motility through interactions with the cofilin kinase TESK1 (6), and with the GTPase activating protein CdGAP (7). Phosphorylation of α-parvin during mitosis may have a role in the regulation of actin dynamics during the cell cycle (8).

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

Application Methods: Western Blotting

Background: Protein phosphatase 1 (PP1) is a ubiquitous eukaryotic protein serine/threonine phosphatase involved in the regulation of various cell functions. Substrate specificity is determined by the binding of a regulatory subunit to the PP1 catalytic subunit (PP1c). It is estimated that over fifty different regulatory subunits exist (1).The myosin phosphatase holoenzyme is composed of three subunits: PP1c, a targeting/regulatory subunit (MYPT/myosin-binding subunit of myosin phosphatase), and a 20 kDa subunit of unknown function (M20). MYPT binding to PP1cδ alters the conformation of the catalytic cleft and increases enzyme activity and specificity (2). Two MYPT isoforms that are 61% identical have been described. MYPT1 is widely expressed, while MYPT2 expression appears to be exclusive to heart and brain (3). Related family members include MBS85, MYPT3, and TIMAP (4).Myosin phosphatase regulates the interaction of actin and myosin in response to signaling through the small GTPase Rho. Rho activity inhibits myosin phosphatase via Rho-associated kinase (ROCK). Phosphorylation of MYPT1 at Thr696 and Thr853 results in phosphatase inhibition and cytoskeletal reorganization (5,6).

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

Application Methods: Western Blotting

Background: Vinculin is a cytoskeletal protein that plays an important role in the regulation of focal adhesions and embryonic development (1-4). Three structural vinculin domains include an amino-terminal head, a short, flexible proline-rich region and a carboxy-terminal tail (1). In the inactive state, the head and tail domains of vinculin interact to form a closed confirmation. The open and active form of vinculin translocates to focal adhesions where it is thought to be involved in anchoring F-actin to the membrane and regulation of cell migration (2). Phospholipid binding to the tail domain and subsequent phosphorylation of vinculin at Ser1033 and Ser1045 by PKC-α and Tyr100 and Tyr1065 by Src kinases weakens the head-tail interaction (5,6). This change in vinculin allows the binding of a number of other proteins, including talin, α-actinin and paxillin, which disrupts the head-tail interaction and initiates the conformational change from the inactive to active state (2,4). Vinculin deficiencies are associated with a decrease in cell adhesion and an increase in cell motility, suggesting a possible role in metastatic growth (7,8). This is supported by a demonstrated relationship between decreased vinculin expression and increased carcinogenesis and metastasis in colorectal carcinoma (9).

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

Application Methods: Western Blotting

Background: Protein ubiquitination and deubiquitination are reversible processes catalyzed by ubiquitinating enzymes (UBEs) and deubiquitinating enzymes (DUBs) respectively (1,2). DUBs are categorized into five subfamilies-USP, UCH, OTU, MJD, and JAMM. Ubiquitin-specific protease 9, X-linked (USP9X) possesses a well-conserved catalytic domain with cysteine peptidase activity, which allows for cleavage of ubiquitin and polyubiquitin conjugates. USP9X is the mammalian homolog of the Drosophila fat-facets (faf) gene, which is essential for normal eye development and viability of the early fly embryo (3,4). While USP9X expression is also critical for normal mammalian development (5-7), many of its substrates are only beginning to be elucidated. There is mounting evidence that USP9X functions in the formation of epithelial cell-cell contacts through deubiquitination-dependent stabilization of molecules involved in maintaining the integrity of both adherens and tight junctions. Indeed, USP9X has been found to associate with AF-6, the β-catenin-E-cadherin complex, and EFA6 (8-11). Research studies have also demonstrated that USP9X is an integral component of the TGF-β/BMP signaling cascade by opposing TRIM33-mediated monoubiquitination of SMAD4 (12). USP9X is overexpressed in a variety of human cancers and contributes to enhanced cell survival, in part, through its ability to deubiquitinate and stabilize the Mcl-1 oncoprotein (13). There is some evidence, however, that suggests the role of USP9X in tumorigenesis is context dependent. Research studies have implicated USP9X in a tumor suppressor role during the early stages of pancreatic ductal adenocarcinoma (PDAC) and in an oncogenic role during advanced stages of PDAC (14,15).

$260
100 µl
$630
300 µl
APPLICATIONS
REACTIVITY
Bovine, Dog, Human, Monkey, Mouse, Pig, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state complexed with the inhibitory IκB proteins (1-3). Activation occurs via phosphorylation of IκBα at Ser32 and Ser36 followed by proteasome-mediated degradation that results in the release and nuclear translocation of active NF-κB (3-7). IκBα phosphorylation and resulting Rel-dependent transcription are activated by a highly diverse group of extracellular signals including inflammatory cytokines, growth factors, and chemokines. Kinases that phosphorylate IκB at these activating sites have been identified (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Dog, Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Autocrine motility factor receptor (AMFR/gp78) is a putative seven transmembrane domain G protein-coupled receptor that functions, in part, at the cell surface as a cytokine receptor for autocrine motility factor/phosphoglucose isomerase (AMF/PGI). AMFR is also localized to an intracellular mitochondria-associated smooth ER domain where it functions as an E3 ubiquitin ligase (1). AMFR function, as both a cytokine receptor and ubiquitin ligase, is linked to a variety of cellular signaling cascades associated with metastasis development and increased invasiveness. AMFR was initially proposed to be a RING-H2 E3 ubiquitin ligase after sequence analysis identified a catalytic RING finger and CUE motif, which are responsible for ubiquitin ligase activity and ubiquitin binding, respectively (2,3). Indeed, AMFR is a key component and amongst the best characterized ubiquitin ligases of the endoplasmic reticulum associated degradation (ERAD) machinery, a process involving recognition of misfolded proteins, ubiquitination, deglycosylation, retro-translocation to the cytosol, and targeting to the proteasome (4). Recent studies have shown that AMFR plays an important role in cholesterol homeostasis via the sterol-mediated ubiquitination of HMG-CoA reductase and its cofactor Insig-1 (5,6). Furthermore, AMFR has been implicated in the degradation of apolipoprotein B100 (7). It was recently reported that AMFR degrades the metastasis suppressor KAI-1/CD-82, representing the first evidence that AMFR ubiquitin ligase activity is involved in metastasis development (8). Increased expression of AMFR correlates with a high incidence of recurrence and reduced survival in patients with bladder, colorectal, and gastric cancers (9-11).

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

Application Methods: Western Blotting

Background: The WNK [with no lysine (K)] family of serine/threonine kinases is characterized by having a cysteine in place of lysine in subdomain II of its kinase activation domain (1,2). The lysine necessary for phosphoryl transfer is located in an atypical position in the catalytic domain. Four WNK family members have been identified in humans (WNK1-4) and have been implicated in regulating ion permeability (3). Mutations in the WNK1 and WNK4 genes in humans cause pseudohypoaldosteronism type II (PHAII), an autosomal dominant disorder leading to hypertension, hyperkalemia, and renal tubular acidosis (4). WNK4 is specifically expressed in the kidney, whereas WNK1 has a wider distribution but is predominantly expressed in polarized epithelia (1-3). Heterozygous mutations in WNK1 in mice result in a significant decrease in blood pressure, while homozygous mutations are embryonic lethal (5). WNK1 is phosphorylated by Akt at Thr60 (6). In addition, WNK1 may be autophosphorylated at Ser382 in the activation loop, and this is thought to be required for its kinase activity (7).

$122
20 µl
$303
100 µl
$717
300 µl
APPLICATIONS
REACTIVITY
Bovine, D. melanogaster, Dog, Hamster, Human, Mouse, Pig, Rat

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

Background: Akt, also referred to as PKB or Rac, plays a critical role in controlling survival and apoptosis (1-3). This protein kinase is activated by insulin and various growth and survival factors to function in a wortmannin-sensitive pathway involving PI3 kinase (2,3). Akt is activated by phospholipid binding and activation loop phosphorylation at Thr308 by PDK1 (4) and by phosphorylation within the carboxy terminus at Ser473. The previously elusive PDK2 responsible for phosphorylation of Akt at Ser473 has been identified as mammalian target of rapamycin (mTOR) in a rapamycin-insensitive complex with rictor and Sin1 (5,6). Akt promotes cell survival by inhibiting apoptosis through phosphorylation and inactivation of several targets, including Bad (7), forkhead transcription factors (8), c-Raf (9), and caspase-9. PTEN phosphatase is a major negative regulator of the PI3 kinase/Akt signaling pathway (10). LY294002 is a specific PI3 kinase inhibitor (11). Another essential Akt function is the regulation of glycogen synthesis through phosphorylation and inactivation of GSK-3α and β (12,13). Akt may also play a role in insulin stimulation of glucose transport (12). In addition to its role in survival and glycogen synthesis, Akt is involved in cell cycle regulation by preventing GSK-3β-mediated phosphorylation and degradation of cyclin D1 (14) and by negatively regulating the cyclin dependent kinase inhibitors p27 Kip1 (15) and p21 Waf1/Cip1 (16). Akt also plays a critical role in cell growth by directly phosphorylating mTOR in a rapamycin-sensitive complex containing raptor (17). More importantly, Akt phosphorylates and inactivates tuberin (TSC2), an inhibitor of mTOR within the mTOR-raptor complex (18,19).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: TRAFs (TNF receptor-associated factors) are a family of multifunctional adaptor proteins that bind to surface receptors and recruit additional proteins to form multiprotein signaling complexes capable of promoting cellular responses (1-3). Members of the TRAF family share a common carboxy-terminal "TRAF domain", which mediates interactions with associated proteins; many also contain amino-terminal Zinc/RING finger motifs. The first TRAFs identified, TRAF1 and TRAF2, were found by virtue of their interactions with the cytoplasmic domain of TNF-receptor 2 (TNFRII) (4). The six known TRAFs (TRAF1-6) act as adaptor proteins for a wide range of cell surface receptors and participate in the regulation of cell survival, proliferation, differentiation, and stress responses.

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

Application Methods: Western Blotting

Background: Cyclophilins are a highly conserved family of peptidylprolyl cis-trans-isomerases (PPIA) that are targets of the immunosuppressant drug cyclosporin A (CsA) (1,2). The complex of cyclophilin and CsA can bind to and inhibit calcineurin which leads to inhibition of the transcription factor NFAT and decreased production of cytokines (3,4). As isomerases, cyclophilins have been proposed to aid in protein folding. Cyclophilin A can bind to the p55 Gag protein of HIV and appears necessary for HIV infection (5,6). There is also some evidence that cyclophilins have nuclease activity and play a role in apoptosis (7).

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

Application Methods: Western Blotting

Background: High temperature requirement protein A2 (HtrA2)/Omi is a serine protease with homology to the E. coli HtrA protein (DegP) and is thought to be involved in apoptosis and stress-induced degradation of misfolded proteins (1). While HtrA2 was orignally identified to be present in either the nucleus (1) or endoplasmic reticulum (2), subsequent studies have shown that it localizes in mitochondria and is released during apoptosis (3-8). HtrA2 is produced as a 50 kDa zymogen that is cleaved to generate a 36 kDa mature protein that exposes an amino terminal motif (AVPS) resembling that of the IAP inhibitor Smac/Diablo (3-8). Like Smac, interaction between HtrA2 and IAP family members, such as XIAP, antagonizes their inhibition of caspase activity and protection from apoptosis (3-8). Interestingly, HtrA2 knock-out mice did not show signs of reduced apoptosis, but rather had a loss of neurons in the striatum and a Parkinson's-like phenotype, suggesting that HtrA2 might have a neuroprotective function (9-11). This activity is associated with the protease activity of HtrA2 (9). Furthermore, research studies have shown that loss of function mutations in the HtrA2 gene are associated with Parkinson's disease (12).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The retinoblastoma tumor suppressor protein Rb regulates cell proliferation by controlling progression through the restriction point within the G1-phase of the cell cycle (1). Rb has three functionally distinct binding domains and interacts with critical regulatory proteins including the E2F family of transcription factors, c-Abl tyrosine kinase, and proteins with a conserved LXCXE motif (2-4). Cell cycle-dependent phosphorylation by a CDK inhibits Rb target binding and allows cell cycle progression (5). Rb inactivation and subsequent cell cycle progression likely requires an initial phosphorylation by cyclin D-CDK4/6 followed by cyclin E-CDK2 phosphorylation (6). Specificity of different CDK/cyclin complexes has been observed in vitro (6-8) and cyclin D1 is required for Ser780 phosphorylation in vivo (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Evi-1 (Ecotropic virus integration site 1) was originally identified as a common site of viral integration in murine myeloid leukemia. It is involved in human myeloid disorders through chromosome translocation and inversion (1) and is also implicated in solid tumor formation (2). Evi-1 is a zinc finger transcription factor which also plays an important role in animal development (3). It has many isoforms due to alternative usage of 5'-ends (4), alternative splicing (5), and intergenic splicing which results in the formation of a fusion protein with MDS1 in normal tissues (6).

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

Application Methods: Western Blotting

Background: Nucleoporin 98 kDa (NUP98) is a component of the nuclear pore complex. It is expressed as three different precursors that undergo auto-cleavage to generate a common amino-terminal 98 kDa peptide (NUP98) and carboxy-terminal 6, 96 (NUP96) and 88 (p88) kDa peptides (1,2). NUP98 contains FG and GLFG repeat domains at its amino terminus and a RNA-binding domain in its carboxy terminus (3). The NUP98 gene is localized on chromosome 11p15.5, a region frequently rearranged in leukemias. To date, 15 fusion partners have been identified for NUP98 (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Amyloid β (Aβ) precursor protein (APP) is a 100-140 kDa transmembrane glycoprotein that exists as several isoforms (1). The amino acid sequence of APP contains the amyloid domain, which can be released by a two-step proteolytic cleavage (1). The extracellular deposition and accumulation of the released Aβ fragments form the main components of amyloid plaques in Alzheimer's disease (1). APP can be phosphorylated at several sites, which may affect the proteolytic processing and secretion of this protein (2-5). Phosphorylation at Thr668 (a position corresponding to the APP695 isoform) by cyclin-dependent kinase is cell-cycle dependent and peaks during G2/M phase (4). APP phosphorylated at Thr668 exists in adult rat brain and correlates with cultured neuronal differentiation (5,6).

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

Application Methods: Western Blotting

Background: Rac and Cdc42 are members of the Rho-GTPase family. In mammals, Rac exists as three isoforms, Rac1, Rac2 and Rac3, which are highly similar in sequence. Rac1 and Cdc42, the most widely studied of this group, are ubiquitously expressed. Rac2 is expressed in cells of hematopoietic origin, and Rac3, while highly expressed in brain, is also found in many other tissues. Rac and Cdc42 play key signaling roles in cytoskeletal reorganization, membrane trafficking, transcriptional regulation, cell growth and development (1). GTP binding stimulates the activity of Rac/Cdc42, and the hydrolysis of GTP to GDP through the protein's intrinsic GTPase activity, rendering it inactive. GTP hydrolysis is aided by GTPase activating proteins (GAPs), while exchange of GDP for GTP is facilitated by guanine nucleotide exchange factors (GEFs). Another level of regulation is achieved through the binding of RhoGDI, a guanine nucleotide dissociation inhibitor, which retains Rho family GTPases, including Rac and Cdc42, in their inactive GDP-bound state (2,3).

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

Application Methods: Western Blotting

Background: Protein phosphatase 1 (PP1) is a ubiquitous eukaryotic protein serine/threonine phosphatase involved in the regulation of various cell functions. Substrate specificity is determined by the binding of a regulatory subunit to the PP1 catalytic subunit (PP1c). It is estimated that over fifty different regulatory subunits exist (1).The myosin phosphatase holoenzyme is composed of three subunits: PP1c, a targeting/regulatory subunit (MYPT/myosin-binding subunit of myosin phosphatase), and a 20 kDa subunit of unknown function (M20). MYPT binding to PP1cδ alters the conformation of the catalytic cleft and increases enzyme activity and specificity (2). Two MYPT isoforms that are 61% identical have been described. MYPT1 is widely expressed, while MYPT2 expression appears to be exclusive to heart and brain (3). Related family members include MBS85, MYPT3, and TIMAP (4).Myosin phosphatase regulates the interaction of actin and myosin in response to signaling through the small GTPase Rho. Rho activity inhibits myosin phosphatase via Rho-associated kinase (ROCK). Phosphorylation of MYPT1 at Thr696 and Thr853 results in phosphatase inhibition and cytoskeletal reorganization (5,6).