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Polyclonal Antibody Cytoplasm

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Bid is a pro-apoptotic “BH3 domain-only” member of the Bcl-2 family originally discovered to interact with both the anti-apoptotic family member Bcl-2 and the pro-apoptotic protein Bax (1). Bid is normally localized in the cytosolic fraction of cells as an inactive precursor and is cleaved at Asp60 by caspase-8 during Fas signaling, leading to translocation of the carboxyl terminal p15 fragment (tBid) to the mitochondrial outer membrane (2-4). Translocation of Bid is associated with release of cytochrome c from the mitochondria, leading to complex formation with Apaf-1 and caspase-9 and resulting in caspase-9 activation (5-7). Thus, Bid relays an apoptotic signal from the cell surface to the mitochondria triggering caspase activation (8,9).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: SH2-containing inositol phosphatase 1 (SHIP1) is a hematopoietic phosphatase that hydrolyzes phosphatidylinositol-3,4,5-triphosphate to phosphatidylinositol-3,4-bisphosphate (1). SHIP1 is a cytosolic phosphatase with an SH2 domain in its amino terminus and two NPXY Shc binding motifs in its carboxy terminus (1,2). Upon receptor cross-linking, SHIP is first recruited to the membrane junction through binding of its SH2 domain to the phospho-tyrosine in the ITIM motif (2), followed by tyrosine phosphorylation on the NPXY motif (2). The membrane relocalization and phosphorylation on the NPXY motif is essential for the regulatory function of SHIP1 (3-5). Its effect on calcium flux, cell survival, growth, cell cycle arrest, and apoptosis is mediated through the PI3K and Akt pathways (3-5). Tyr1021 is located in one of the NPXY motifs in SHIP1, and its phosphorylation is important for SHIP1 function (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). Autophagy is generally activated by conditions of nutrient deprivation but has also been associated with a number of physiological processes including development, differentiation, neurodegeneration, infection, and cancer (3). The molecular machinery of autophagy was largely discovered in yeast and referred to as autophagy-related (Atg) genes. Formation of the autophagosome involves a ubiquitin-like conjugation system in which Atg12 is covalently bound to Atg5 and targeted to autophagosome vesicles (4-6). This conjugation reaction is mediated by the ubiquitin E1-like enzyme Atg7 and the E2-like enzyme Atg10 (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Cripto, also known as teratocarcinoma derived growth factor 1 (TDGF-1), belongs to the EGF-CFC family of proteins. Members of this family are characterized by an N-terminal signal peptide, a conserved cysteine rich domain (CFC motif), and a short hydrophobic carboxy-terminal tail that contains GPI cleavage and attachment sites. The GPI moiety anchors Cripto and family members to the extracellular plasma membrane (1). An O-linked fucosylation site within the EGF-like motif is required for Cripto and related family members to perform their function as co-receptors for TGF-β-related ligands such as Nodal and Vg1/GDF1 (2,3). Soluble forms of Cripto can be produced - these contain intact EGF and CFC domains, and are thought to have paracrine activities, as opposed to the autocrine activity of Cripto functioning as a coreceptor (4). Understanding of this paracrine activity is not complete, but it is proposed that Cripto may act as co-ligand for Nodal (3).Cripto is an important modulator of embryogenesis and oncogenesis (4). It is highly expressed in early embryos, and in embryonic stem (ES) cells where it is involved in cardiomyocytic differentiation and acts as a negative regulator of neurogenesis (5-7). Transient activation of Cripto is essential for the capacity of stem cell self-renewal and pluripotency in ES cells, and in some adult derived stem cells (8). Signaling through Cripto can also stimulate other activities that promote tumorigenesis such as stimulation of proliferation, cell motility, invasion, angiogenesis and epithelial-mesenchymal transition (EMT) (9-11). Cripto is highly expressed in a broad range of tumors, where it acts as a potent oncogene.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: The Drosophila piwi gene was identified as being required for the self-renewal of germline stem cells (1). Piwi homologs are well conserved among various species including Arabidopsis, C. elegans, and Homo sapiens (1). Both Miwi and Mili proteins are mouse homologs of Piwi and contain a C-terminal Piwi domain (2). Miwi and Mili bind to Piwi-interacting RNAs (piRNAs) in male germ cells and are essential for spermatogenesis in mice (3-5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Monocyte chemotactic protein-1 (MCP-1), also known as CCL2, monocyte chemotactic activating factor (MCAF) or glioma-derived chemotactic factor-2 (GDCF-2), is the product of the human JE gene and a member of the family of C-C (or β) chemokines (1-4). The predicted molecular weight of MCP-1 protein is 11-13 kDa, but it may migrate at 20-30 kDa due to glycosylation. MCP-1 is secreted by a variety of cell types in response to pro-inflammatory stimuli and was originally described for its chemotactic activity on monocytes. This activity has led to studies demonstrating its role in diseases characterized by monocyte infiltrates such as psoriasis (5), rheumatoid arthritis (6) and atherosclerosis (7). MCP-1 may also contribute to tumor progression and angiogenesis (8). Signaling by MCP-1 is mediated by the G-protein coupled receptor CCR2 (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The Silent Information Regulator (SIR2) family of genes is a highly conserved group of genes that encode nicotinamide adenine dinucleotide (NAD)-dependent protein deacetylases, also known as class III histone deacetylases. The first discovered and best characterized of these genes is Saccharomyces cerevisiae SIR2, which is involved in silencing of mating type loci, telomere maintenance, DNA damage response, and cell aging (1). SirT1, the mammalian ortholog of Sir2, is a nuclear protein implicated in the regulation of many cellular processes, including apoptosis, cellular senescence, endocrine signaling, glucose homeostasis, aging, and longevity. Targets of SirT1 include acetylated p53 (2,3), p300 (4), Ku70 (5), forkhead (FoxO) transcription factors (5,6), PPARγ (7), and the PPARγ coactivator-1α (PGC-1α) protein (8). Deacetylation of p53 and FoxO transcription factors represses apoptosis and increases cell survival (2,3,5,6). Deacetylation of PPARγ and PGC-1α regulates the gluconeogenic/glycolytic pathways in the liver and fat mobilization in white adipocytes in response to fasting (7,8). SirT1 deacetylase activity is inhibited by nicotinamide and activated by resveratrol. In addition, SirT1 activity may be regulated by phosphorylation, as it is phosphorylated at Ser27 and Ser47 in vivo; however, the function of these phosphorylation sites has not yet been determined (9).

$111
20 µl
$260
100 µl
$630
300 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The inhibitor of apoptosis protein (IAP) family consists of an evolutionarily conserved group of apoptosis inhibitors containing a conserved 70 amino acid BIR (baculovirus inhibitor repeat) domain (1,2). Human members of this family include c-IAP1, c-IAP2, XIAP, survivin, livin, and NAIP. Overexpression of IAP family members, particularly survivin and livin, in cancer cell lines and primary tumors suggests an important role for these proteins in cancer progression (3-5). In general, the IAP proteins function through direct interactions to inhibit the activity of several caspases, including caspase-3, caspase-7, and caspase-9 (5,6). In addition, binding of IAP family members to the mitochondrial protein Smac blocks their interaction with caspase-9, thereby allowing the processing and activation of the caspase (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Nerve growth factor (NGF) is a small, secreted protein and member of the neurotrophin family of growth factors that promote neuronal cell survival and differentiation (1). Producing cells release NGF that bind and activate TrkA high affinity receptors to mediate NGF-driven signaling. NGF also binds to a low affinity p75 (NTR) receptors, which belong to the death receptor family (2). Although NGF has been classically described as favoring neuron survival and differentiation, nerve growth factor can promote apoptosis in cells that contain p75 (NTR) and lack TrkA. NGF can induce neuron death in a variety of neurodegenerative conditions, including Alzheimer disease (3). Besides its neurotrophic actions, NGF has an effect on non-neuronal cells and may help mediate inflammation, angiogenesis, and stimulate breast cancer cell growth (4-6). NGF signaling is looking increasingly promising as potential drug targets for diseases.

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Tug (Tether containing UBX domain for GLUT4), also known as ASPL, ASPSCR1, RCC17, UBXD9, UBXN9, was first identified as a chromosomal translocation partner for TFE3 in patients with Alveolar soft part sarcoma (1) and contains an UBX-like domain in its C-terminal region. Tug is found to tether GLUT4 in intracellular vesicles and to release GLUT4 for cell surface translocation upon insulin stimulation (2). Stable Tug depletion or expression of a dominant negative form stimulates GLUT4 redistribution (3).

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

Application Methods: Western Blotting

Background: Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: The Drosophila piwi gene was identified as being required for the self-renewal of germ-line stem cells (1). Piwi homologs are well conserved among various species including Arabidopsis, C. elegans, and human (1). Miwi and Mili proteins are both mouse homologs of Piwi and contain a C-terminal Piwi domain (2). Miwi and Mili bind to Piwi-interacting RNAs (piRNAs) in male germ cells and are essential for spermatogenesis in mouse (3-5).

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

Application Methods: Western Blotting

Background: Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Mena (mammalian enabled), EVL, and VASP are members of the Ena/VASP family, which is involved in controlling cell shape and cell movement by shielding actin filaments from capping proteins (1). Ena/VASP proteins have three specific domains: an amino-terminal EVH1 domain controlling protein localization; a central proline-rich domain mediating interactions with both SH3 and WW domain containing proteins, including profilin; and a carboxy-terminal domain causing tetramerization and binding to actin (2). Mena interacts with actin filaments at the growing ends localizing to lamellipodia and to tips of growth cone filopodia in neurons. Axons projecting from interhemispheric cortico-cortical neurons are misrouted in newborn, homozygous Mena knock-out mice (3). Mena is phosphorylated at Ser236 by PKA, thereby promoting filopodial formation and elongation in the growth cone (4).Three forms of Mena corresponding to 80, 88 and 140 kD are known. The 80 kD protein is broadly expressed in contrast to the 140 kD protein which is enriched in neural cell types. Alternative splicing produces these forms. The 88 kD protein is mainly found in embryonic cell types and is likely the result of post-translational modification. Expression of all three forms is completely eliminated in Mena homozygous mutant animals (1, 3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: The Drosophila piwi gene was identified as being required for the self-renewal of germline stem cells (1). Piwi homologs are well conserved among various species including Arabidopsis, C. elegans, and Homo sapiens (1). Both Miwi and Mili proteins are mouse homologs of Piwi and contain a C-terminal Piwi domain (2). Miwi and Mili bind to Piwi-interacting RNAs (piRNAs) in male germ cells and are essential for spermatogenesis in mice (3-5).

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

Application Methods: Western Blotting

Background: The regulatory associated protein of mTOR (Raptor) was identified as an mTOR binding partner that mediates mTOR signaling to downstream targets (1,2). Raptor binds to mTOR substrates, including 4E-BP1 and p70 S6 kinase, through their TOR signaling (TOS) motifs and is required for mTOR-mediated phosphorylation of these substrates (3,4). Binding of the FKBP12-rapamycin complex to mTOR inhibits the mTOR-raptor interaction, suggesting a mechanism for rapamycin's specific inhibition of mTOR signaling (5). This mTOR-raptor interaction and its regulation by nutrients and/or rapamycin is dependent on a protein called GβL (6). GβL is also part of the rapamycin-insensitive complex between mTOR and rictor (rapamycin-insensitive companion of mTOR), and may mediate rictor-mTOR signaling to downstream targets including PKCα (7). Furthermore, the rictor-mTOR complex has been identified as the previously elusive PDK2 responsible for the phosphorylation of Akt/PKB on Ser473, facilitating phosphorylation of Akt/PKB on Thr308 by PDK1 and required for the full activation of Akt/PKB (8).Recently raptor has been identified as a direct substrate of the AMP-activated protein kinase (AMPK) (9). AMPK phosphorylates raptor on Ser722/Ser792 (9). This phosphorylation is essential for inhibition of the raptor-containing mTOR complex 1 (mTORC1) and induces cell cycle arrest when cells are stressed for energy (9). These findings suggest that raptor is a critical switch that correlates cell cycle progression with energy status.

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The ADAM (A Disintegrin and A Metalloprotease) family of multidomain membrane proteins influences cell signaling and adhesion by shedding cell surface proteins such as cytokines and growth factors, by influencing cell adhesion to the extracellular matrix (ECM), and by directly remodeling the ECM. Conserved domains in ADAM family members include a prodomain, a zinc-dependent metalloprotease domain, a disintegrin domain, a cysteine-rich domain, an EGF-like sequence, and a short cytoplasmic tail (1,2).The prodomain is thought to aid in protein folding. Disintegrin and cysteine-rich domains mediate adhesion, at least in part, through binding to integrins. Phosphorylation of the cytoplasmic tail as well as its interaction with other signaling proteins may influence intra- and extracellular signaling (1). ADAM9 is widely distributed and has been shown to affect migration in skin keratinocytes (3,4). Research studies have shown that ADAM9 is overexpressed in prostate cancer (5), pancreatic cancer (6), gastric cancer (7), and has been linked to invasion and metastasis in small cell lung cancer (8). Research has also shown that an alternatively spliced short (50 kDa) form of ADAM9 containing protease activity is involved in tumor cell invasion (9).

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

Application Methods: Western Blotting

Background: Secretory proteins are synthesized on polysomes and translocated into the endoplasmic reticulum (ER). Inside ER, these proteins are often modified by disulfide bond formation, amino-linked glycosylation and folding. The ER contains a pool of molecular chaperones, including Grp94, to help ensure correct protein folding. Grp94 is a glucose-regulated protein (1) with sequence homology to Hsp90 (2). In addition to its role in helping to facilitate folding of a number of secretory proteins to their correct conformation (3), studies suggest that Grp94 derived from cancer cells also induces anti-tumor immune responses in mouse tumor models (4, 5). One way in which Grp94 promotes tumor immunogenicity is its ability to bind to and present tumor-derived peptides as antigens (6). Furthermore, Grp94 has also been shown to induce maturation of dendritic cells (7). Taken together, Grp94 functions both as a tumor-specific antigen and as an activator of antigen-presenting cells to elicit an anti-cancer immune response (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Fatty acid binding proteins (FABPs) bind to fatty acids and other lipids to function as cytoplasmic lipid chaperones (1). They participate in the transport of fatty acids and other lipids to various cellular pathways (2). The predominant fatty acid binding protein found in adipocytes is FABP4, also called adipocyte fatty acid binding protein or aP2. FABP4 is also expressed in macrophages (3). FABP4 knockout mice fed a high-fat and high-calorie diet become obese but develop neither insulin resistance nor diabetes, suggesting that this protein might be a link between obesity and insulin resistance and diabetes (4). Mice deficient in both FABP4 and ApoE show protection against atherosclerosis when compared with mice deficient only in ApoE (3). Mice carrying a FABP4 genetic variant exhibit both reduced FABP4 expression and a reduced potential for developing type 2 diabetes and coronary heart disease. A related study in humans indicated a similar pattern, suggesting that FABP4 may be a potential therapeutic target in the treatment of these disorders (1).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Reverse orientation c-erbA gene α (Rev-erbα, EAR-1, or NR1D1) is a widely expressed member of the orphan nuclear receptor family of proteins (1). Rev-erbα is highly expressed in adipose tissue, skeletal muscle, brain and liver, and regulates cellular proliferation and differentiation. Expression increases during differentiation in adipocytes and ectopic expression of Rev-erbα potentiates the adipocyte differentiation of 3T3-L1 cells (2). In addition, expression oscillates with circadian rhythm in liver cells and Rev-erbα regulates expression of BMAL1, ApoA-I and ApoC-III, all key regulators of circadian rhythm (3-7). Phosphorylation of Rev-erbα Ser55 and Ser59 by GSK-3β appears to stabilize Rev-erbα protein levels and is important for synchronizing and maintaining the circadian clock (8). Rev-erbα also regulates inflammation by targeting the NF-κB responsive genes IL-6 and COX-2 (9). Rev-erbα lacks the activation function 2 domain required for ligand-dependent activation of transcription by other members of the nuclear receptor family; thus it behaves as a constitutive repressor protein, recruiting the nuclear receptor co-repressor (N-CoR)/HDAC3 complex to target genes to repress transcription (10).