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Product listing: Ku80 (C48E7) Rabbit mAb, UniProt ID P13010 #2180 to LSD1 Antibody, UniProt ID O60341 #2139

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

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

Background: Ku is a heterodimeric protein composed of two subunits (Ku70 and Ku80) originally identified by researchers as autoantigens associated with several autoimmune diseases including scleroderma, polymyositis, and systemic lupus erythematosus (1). Ku is an abundant, ubiquitously expressed nuclear protein that binds to and stabilizes the ends of DNA at telomeres or double-stranded DNA breaks (2-5). The Ku70/Ku80 heterodimer has ATP-dependent DNA helicase activity and functions as the DNA-binding regulatory component of DNA-dependent protein kinase (DNA-PK) (6-8). The assembly of the DNA-PK complex at DNA ends is required for nonhomologous end-joining (NHEJ), one mechanism involved in double-stranded DNA break repair and V(D)J recombination (8). DNA-PK has been shown to phosphorylate many proteins, including p53, serum response factor, c-Jun, c-Fos, c-Myc, Oct-1, Sp-1, and RNA polymerase II (1,8). The combined activities of Ku70/Ku80 and DNA-PK implicate Ku in many cellular functions, including cell cycle regulation, DNA replication and repair, telomere maintenance, recombination, and transcriptional activation.

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The c-Cbl proto-oncogene is a ubiquitously expressed cytoplasmic adaptor protein that is especially predominant in hematopoietic cells (1,2). c-Cbl is rapidly tyrosine-phosphorylated in response to stimulation of a variety of cell-surface receptors and becomes associated with a number of intracellular signaling molecules such as protein tyrosine kinases, phosphatidylinositol-3 kinase, Crk, and 14-3-3 proteins (3,4). c-Cbl possesses a highly conserved amino-terminal phosphotyrosine binding domain (TKB) and a C3HC4 RING finger motif. The TKB recognizes phosphorylated tyrosines on activated receptor tyrosine kinases (RTKs) as well as other nonreceptor tyrosine kinases. The RING finger motif recruits ubiquitin-conjugating enzymes. These two domains are primarily responsible for the ubiquitin ligase activity of c-Cbl and downregulation of RTKs (3). Research studies have indicated that in human cancer tissues, c-Cbl is frequently tyrosine-phosphorylated in a tumor-specific manner (5). Phosphorylation of Tyr731 of c-Cbl provides a docking site for downstream signaling components such as p85 and Fyn (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: PPARγ coactivator-1α (PGC-1α) was originally identified as a transcriptional coactivator whose expression closely correlated with adaptive thermogenesis following exposure to cold temperatures (1). Named for its association with the nuclear receptor peroxisome-proliferator activated receptor (PPARγ), PGC-1α interacts with a diverse array of transcription factors to regulate numerous aspects of cell physiology (2). PGC-1α helps to regulate cell processes important in adaptive thermogenesis and energy metabolism, including the related functions of glucose uptake, gluconeogenesis, insulin secretion, and mitochondrial biogenesis (3). Long thought to be a potential therapeutic target for the treatment of type II diabetes, obesity, cardiomyopathy, or other metabolic disorders (reviewed in 4), a recent functional survey found no obvious differences in PPARγ activity associated with recognized PGC-1α variants (5).

$260
100 µl
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Mouse, Rat

Application Methods: Western Blotting

Background: Spinocerebellar ataxia 1 (SCA1), an autosomal dominant neurodegenerative disorder, is characterized by slurred speech, loss of limb coordination, and gait abnormalities resulting from the degeneration of cerebellar Purkinje cells and of a subset of brainstem neurons (1). Individuals with SCA1 have a highly polymorphic CAG repeat expansion encoding a polyglutamine tract in ataxin-1 (2). Akt phosphorylates ataxin-1 at Ser776, which regulates an association with 14-3-3. This interaction increases ataxin-1 stabilization and accumulation resulting in enhanced neurodegeneration (3). In addition, HSP70 controls the effect that phosphorylation has on ataxin-1 stability (4).

$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).

$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

Application Methods: Western Blotting

Background: Bone morphogenetic proteins (BMPs) constitute a large family of signaling molecules that regulate a wide range of critical processes including morphogenesis, cell-fate determination, proliferation, differentiation, and apoptosis (1,2). BMP receptors are members of the TGF-β family of Ser/Thr kinase receptors. Ligand binding induces multimerization, autophosphorylation, and activation of these receptors (3-5). They subsequently phosphorylate Smad1 at Ser463 and Ser465 in the carboxy-terminal motif SSXS, as well as Smad5 and Smad9 (Smad8) at their corresponding sites. These phosphorylated Smads dimerize with the coactivating Smad4 and translocate to the nucleus, where they stimulate transcription of target genes (5).MAP kinases and CDKs 8 and 9 phosphorylate residues in the linker region of Smad1, including Ser206. The phosphorylation of Ser206 recruits Smurf1 to the linker region and leads to the degradation of Smad1 (6). Phosphorylation of this site also promotes Smad1 transcriptional action by recruiting YAP to the linker region (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Calcium-binding proteins of different subfamilies regulate the second messenger calcium. Calbindin, calmodulin, S-100, parvalbumin and troponin C are members of the low molecular weight calcium-binding protein family (1). Calbindin is expressed in discrete neuronal populations within the CNS and is thought to act as an intracellular calcium buffering protein. Most Purkinje cells express calbindin, which is expressed when neurons start to migrate and differentiate. In contrast, other calcium buffering proteins, such as parvalbumin, are expressed later during development and in parallel with increasing neuronal activity (2).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Alix, a phylogenetically conserved cytosolic scaffold protein, contains an N-terminal Bro1 domain, a coiled-coil region and a C-terminal proline-rich domain (1,2). Originally identified as an ALG-2 (apoptosis-linked gene 2)-interacting protein involved in programmed cell death (3,4), Alix also regulates many other cellular processes, such as endocytic membrane trafficking and cell adhesion through interactions with ESCRT (endosomal sorting complex required for transport) proteins, endophilins, and CIN85 (Cbl-interacting protein of 85 kDa) (5,6).

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

Application Methods: Western Blotting

Background: Rab4 is a member of the Ras superfamily of small Rab GTPases implicated in endocytosis. Rab4 is localized at early endosomes/recycling endosomes and functions as a key regulator for sorting/recycling of membrane and proteins (1,2). Rab4 has two isoforms, Rab4A and Rab4B, both of which are localized in similar cellular compartments and are believed to have similar functions (4). Rab4 interacts with several Rab4 effectors in a complex on a special endosome site that promotes membrane/protein recycling (1,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: The ErbB2 (HER2) proto-oncogene encodes a 185 kDa transmembrane, receptor-like glycoprotein with intrinsic tyrosine kinase activity (1). While ErbB2 lacks an identified ligand, ErbB2 kinase activity can be activated in the absence of a ligand when overexpressed and through heteromeric associations with other ErbB family members (2). Amplification of the ErbB2 gene and overexpression of its product are detected in almost 40% of human breast cancers (3). Binding of the c-Cbl ubiquitin ligase to ErbB2 at Tyr1112 leads to ErbB2 poly-ubiquitination and enhances degradation of this kinase (4). ErbB2 is a key therapeutic target in the treatment of breast cancer and other carcinomas and targeting the regulation of ErbB2 degradation by the c-Cbl-regulated proteolytic pathway is one potential therapeutic strategy. Phosphorylation of the kinase domain residue Tyr877 of ErbB2 (homologous to Tyr416 of pp60c-Src) may be involved in regulating ErbB2 biological activity. The major autophosphorylation sites in ErbB2 are Tyr1248 and Tyr1221/1222; phosphorylation of these sites couples ErbB2 to the Ras-Raf-MAP kinase signal transduction pathway (1,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: EB1 (end-binding protein 1) is a microtubule associated protein (1). EB1 localizes to the growing ends of microtubules, the centrosome and the mitotic spindle (2-4). EB1 is also found to associate with the adenomatous polyposis coli (APC) protein (5). Recent studies also suggest that EB1 plays a role in microtubule-based transport (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), 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, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Methylation of DNA at cytosine residues in mammalian cells is a heritable, epigenetic modification that is critical for proper regulation of gene expression, genomic imprinting and development (1,2). Three families of mammalian DNA methyltransferases have been identified: DNMT1, DNMT2 and DNMT3 (1,2). DNMT1 is constitutively expressed in proliferating cells and functions as a maintenance methyltransferase, transferring proper methylation patterns to newly synthesized DNA during replication. DNMT3A and DNMT3B are strongly expressed in embryonic stem cells with reduced expression in adult somatic tissues. DNMT3A and DNMT3B function as de novo methyltransferases that methylate previously unmethylated regions of DNA. DNMT2 is expressed at low levels in adult somatic tissues and its inactivation affects neither de novo nor maintenance DNA methylation. DNMT1, DNMT3A and DNMT3B together form a protein complex that interacts with histone deacetylases (HDAC1, HDAC2, Sin3A), transcriptional repressor proteins (RB, TAZ-1) and heterochromatin proteins (HP1, SUV39H1), to maintain proper levels of DNA methylation and facilitate gene silencing (3-8). Improper DNA methylation contributes to diseased states such as cancer (1,2). Hypermethylation of promoter CpG islands within tumor suppressor genes correlates with gene silencing and the development of cancer. In addition, hypomethylation of bulk genomic DNA correlates with and may contribute to the onset of cancer. DNMT1, DNMT3A and DNMT3B are over-expressed in many cancers, including acute and chronic myelogenous leukemias, in addition to colon, breast and stomach carcinomas (9-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human

Application Methods: Immunofluorescence (Immunocytochemistry), 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
Mouse

Application Methods: Western Blotting

Background: Membrane-bound transcription factor protease site 2 (MBTPS2), also known as site-2 protease (S2P), is a zinc metalloprotease in the Golgi membrane (1,2,3). It regulates cholesterol metabolism (1,2) and unfolded protein response (UPR) (3,4). When cells are deprived of cholesterol, sterol regulatory element-binding proteins (SREBPs) move from the endoplasmic reticulum (ER) to the Golgi apparatus and are cleaved by site-1 protease (S1P) (5,6) and site-2 protease (1,6) sequentially to release the active amino-terminal domains. These amino-terminal domains of SREBPs then translocate into the nucleus to induce expression of genes for cholesterol biosynthesis. During UPR, activating transcription factor 6 (ATF6) transports from ER to Golgi apparatus and is cleaved by S1P and S2P to release a cytosolic fragment. This cytosolic fragment relocates to the nucleus and activates the UPR gene expression (7).

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

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

Background: Ubiquitin can be covalently linked to many cellular proteins by the ubiquitination process, which targets proteins for degradation by the 26S proteasome. Three components are involved in the target protein-ubiquitin conjugation process. Ubiquitin is first activated by forming a thiolester complex with the activation component E1; the activated ubiquitin is subsequently transferred to the ubiquitin-carrier protein E2 and then from E2 to ubiquitin ligase E3 for final delivery to the epsilon-NH2 of the target protein lysine residue (1-3). Combinatorial interactions of different E2 and E3 proteins result in substrate specificity (4). Recent data suggests that activated E2 associates transiently with E3, and the dissociation is a critical step for ubiquitination (5). S phase kinase-associated protein 1 (Skp1) is a critical scaffold protein of the Skp1/CUL1/F-box (SCF) E3 ubiquitin ligase protein complex. Various F-box proteins (e.g., β-TrCP, Skp2) mediate an interaction with Skp1, via their defining and conserved domain of 40 amino acids, and with substrates to be ubiquitinated (e.g., β-catenin, p27) (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Notch signaling is activated upon engagement of the Notch receptor with its ligands, the DSL (Delta, Serrate, Lag2) proteins of single-pass type I membrane proteins. The DSL proteins contain multiple EGF-like repeats and a DSL domain that is required for binding to Notch (1,2). Five DSL proteins have been identified in mammals: Jagged1, Jagged2, Delta-like (DLL) 1, 3 and 4 (3). Ligand binding to the Notch receptor results in two sequential proteolytic cleavages of the receptor by the ADAM protease and the γ-secretase complex. The intracellular domain of Notch is released and then translocates to the nucleus where it activates transcription. Notch ligands may also be processed in a way similar to Notch, suggesting a bi-directional signaling through receptor-ligand interactions (4-6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Musashi-1 and Musashi-2 are RNA-binding proteins which play a role in asymmetric cell division of ectodermal precursor cells by regulating the translation of target mRNA. Both family members augment Notch signaling and repress the translation of m-Numb, a protein that positively modulates differentiation of neural stem cells into neurons. Thus, Musashi contributes to the maintenance of neural stem cells (1). While Musashi-1 is frequently used as a marker for proliferating neural precursor cells, it is also expressed in epithelial stem cells including intestinal and mammary gland stem cells (2-4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The human WSTF gene is located within the common Williams Syndrome (WS) deletion area at chromosome 7q11.23. Several WSTF gene products have been detected with little difference in length of polypeptides (1-3). Functional motifs identified by sequence-homology searches include a PHD-type zinc finger motif followed by a bromodomain. Both motifs are found in many transcription factors, suggesting that WSTF may function as a transcription factor. A Drosophila gene (acf1) was cloned, which encodes two forms of Acf1 proteins with molecular weight 170 kDa and 185 kDa, respectively (4). It was demonstrated that Acf1 is structurally related to the human WSTF gene. Acf1 forms a complex with another protein, ISWI, and functions in the ATP-dependent catalysis of chromatin assembly (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Axin1 (Axis inhibition protein 1) and Axin2 are multidomain scaffold proteins that negatively regulate Wnt signaling. Axin1 interacts with APC, GSK-3β, Dvl, and β-catenin and promotes the GSK-3β-mediated phosphorylation and subsequent degradation of β-catenin (1,2). Upon stimulation of cells with Wnt, Axin1 is recruited to the membrane by phosphorylated LRP5/6, a process that is believed to be crucial for activation of Wnt signaling (3,4). In addition to its role in the Wnt signaling pathway, Axin1 forms a complex with MEKK1 and activates c-Jun amino-terminal kinase (JNK/SAPK) (5). Axin2 (also known as Conductin or Axil) can functionally substitute for Axin1 in mice (6). Axin2 itself is a direct target of the Wnt signaling pathway and therefore serves to control the duration and/or intensity of Wnt signaling through a negative feedback loop (7-9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The neurological condition Dystonia is associated with sustained muscle contractions and abnormal posturing (1). TorsinA, torsinB, torp2A and torp3A belong to the family of ATPases associated with cellular activites (AAA+) and mutations in torsinA cause early onset dystonia (2). TorsinA has been shown to suppress intracellular protein aggregation in C. elegans and possesses chaperon activity. Interestingly, torsinA is highly expressed in dopaminergic neurons and associates with alpha-synuclein in Lewy bodies, which pathologically characterize Parkinson's Disease (3-5).

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

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

Background: The cytoskeleton consists of three types of cytosolic fibers: microtubules, microfilaments (actin filaments), and intermediate filaments. Globular tubulin subunits comprise the microtubule building block, with α/β-tubulin heterodimers forming the tubulin subunit common to all eukaryotic cells. γ-tubulin is required to nucleate polymerization of tubulin subunits to form microtubule polymers. Many cell movements are mediated by microtubule action, including the beating of cilia and flagella, cytoplasmic transport of membrane vesicles, chromosome alignment during meiosis/mitosis, and nerve-cell axon migration. These movements result from competitive microtubule polymerization and depolymerization or through the actions of microtubule motor proteins (1).

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

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

Background: The cytoskeleton consists of three types of cytosolic fibers: microtubules, microfilaments (actin filaments), and intermediate filaments. Globular tubulin subunits comprise the microtubule building block, with α/β-tubulin heterodimers forming the tubulin subunit common to all eukaryotic cells. γ-tubulin is required to nucleate polymerization of tubulin subunits to form microtubule polymers. Many cell movements are mediated by microtubule action, including the beating of cilia and flagella, cytoplasmic transport of membrane vesicles, chromosome alignment during meiosis/mitosis, and nerve-cell axon migration. These movements result from competitive microtubule polymerization and depolymerization or through the actions of microtubule motor proteins (1).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Several protein-protein interactions are essential to membrane fusion during endocytosis. Membrane fusion requires interaction among SNARE1 proteins associated with both donor and acceptor membranes (1,2). Following membrane fusion, the α-SNAP cytoplasmic adapter protein binds to the SNARE complex. N-ethylmaleimide-sensitive factor (NSF), a hexameric ATPase, then associates with the α-SNAP/SNARE complex to mediate SNARE disassembly during membrane fusion (3,4). The ATPase activity of NSF induces a conformational change in the α-SNAP/SNARE complex that leads to its dissociation from the membrane, membrane fusion and eventual recycling of the SNARE complex for subsequent membrane fusion (3,4).

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

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

Background: The cytoskeleton consists of three types of cytosolic fibers: microtubules, microfilaments (actin filaments), and intermediate filaments. Globular tubulin subunits comprise the microtubule building block, with α/β-tubulin heterodimers forming the tubulin subunit common to all eukaryotic cells. γ-tubulin is required to nucleate polymerization of tubulin subunits to form microtubule polymers. Many cell movements are mediated by microtubule action, including the beating of cilia and flagella, cytoplasmic transport of membrane vesicles, chromosome alignment during meiosis/mitosis, and nerve-cell axon migration. These movements result from competitive microtubule polymerization and depolymerization or through the actions of microtubule motor proteins (1).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Rab5 is a member of the Ras superfamily of small Rab GTPases. Rab5 is localized at the plasma membrane and early endosomes and functions as a key regulator of vesicular trafficking during early endocytosis (1). The conformational change between Rab5 GTP/GDP states is essential for its biological function as a rate limiting regulator at multiple steps during endocytosis (1,2). Rab5 exerts its function by interacting with several Rab5-specific effectors (1-3). These proteins form complexes with Rab5 on a specialized Rab domain of the endosome and promote recycling of Rab5-cargo targets between endosome and the plasma membrane.

$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: Cell growth is a fundamental biological process whereby cells accumulate mass and increase in size. The mammalian TOR (mTOR) pathway regulates growth by coordinating energy and nutrient signals with growth factor-derived signals (1). mTOR is a large protein kinase with two different complexes. One complex contains mTOR, GβL and raptor, which is a target of rapamycin. The other complex, insensitive to rapamycin, includes mTOR, GβL, Sin1, and rictor (1). The mTOR-rictor complex phosphorylates Ser473 of Akt/PKB in vitro (2). This phosphorylation is essential for full Akt/PKB activation. Furthermore, an siRNA knockdown of rictor inhibits Ser473 phosphorylation in 3T3-L1 adipocytes (3). This complex has also been shown to phosphorylate the rapamycin-resistant mutants of S6K1, another effector of mTOR (4).

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

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

Background: Lysine-specific demethylase 1 (LSD1; also known as AOF2 and BHC110) is a nuclear amine oxidase homolog that acts as a histone demethylase and transcription cofactor (1). Gene activation and repression is specifically regulated by the methylation state of distinct histone protein lysine residues. For example, methylation of histone H3 at Lys4 facilitates transcriptional activation by coordinating the recruitment of BPTF, a component of the NURF chromatin remodeling complex, and WDR5, a component of multiple histone methyltransferase complexes (2,3). In contrast, methylation of histone H3 at Lys9 facilitates transcriptional repression by recruiting HP1 (4,5). LSD1 is a component of the CoREST transcriptional co-repressor complex that also contains CoREST, CtBP, HDAC1 and HDAC2. As part of this complex, LSD1 demethylates mono-methyl and di-methyl histone H3 at Lys4 through a FAD-dependent oxidation reaction to facilitate neuronal-specific gene repression in non-neuronal cells (1,6,7). In contrast, LSD1 associates with androgen receptor in human prostate cells to demethylate mono-methyl and di-methyl histone H3 at Lys9 and facilitate androgen receptor-dependent transcriptional activation (8). Therefore, depending on gene context LSD1 can function as either a transcriptional co-repressor or co-activator. LSD1 activity is inhibited by the amine oxidase inhibitors pargyline, deprenyl, clorgyline and tranylcypromine (8).