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Product listing: NCAM (CD56) Antibody, UniProt ID P13591 #3606 to Clusterin (D7N2K) XP® Rabbit mAb, UniProt ID P10909 #34642

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: NCAM (neural cell adhesion molecule, CD56) is an adhesion glycoprotein with five extracellular immunoglobulin-like domains followed by two fibronectin type III repeats. Structural diversity is introduced by alternative splicing resulting in different cytoplasmic domains (1). NCAM mediates neuronal attachment, neurite extension and cell-cell interactions through homo and heterophilic interactions. PSA (polysialic acid) post-translationally modifies NCAM and increases the metastatic potential of small cell lung carcinoma, Wilms+ tumor, neuroblastoma and rhabdomyosarcoma (2). CD56 and CD16 are commonly used to identify NK cells although some cells with the T cell markers CD3 and CD4 also express CD56 (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Aquaporin 2 (AQP2) is a water transport protein that forms water channels in kidney tubules and plays a predominant role in controlling organism water homeostasis (1). Members of the aquaporin family are multiple pass transmembrane proteins that form homotetramers to facilitate the flow of water across the plasma membrane. At least thirteen aquaporins have been indentified to date (AQP0 through AQP12) and together this family of small, hydrophobic proteins plays a role in an array of biological processes that include urine formation, cell motility, fertilization, cell junction formation and regulation of overall water homeostasis (2). AQP2 tetramers form water channels that facilitate water transport and excretion in the kidney (3). This transport protein is localized to the plasma membrane is response to endocrine signaling. Posterior pituitary hormones arginine vasopressin (AVP) and ADH regulate osmotic water cell permeability by triggering phosphorylation and subsequent exocytosis of AQP2 (1,4). Mutations in the corresponding AQP2 gene cause a rare form of diabetes known as nephrogenic diabetes insipidus. This autosomal dominant disorder is characterized by abnormal water reabsorption by kidney tubules due, in part, to either nonfunctional or mislocalized AQP2 protein (5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The 26S proteasome is a highly abundant proteolytic complex involved in the degradation of ubiquitinated substrate proteins. It consists largely of two sub-complexes, the 20S catalytic core particle (CP) and the 19S/PA700 regulatory particle (RP) that can cap either end of the CP. The CP consists of two stacked heteroheptameric β-rings (β1-7) that contain three catalytic β-subunits and are flanked on either side by two heteroheptameric α-rings (α1-7). The RP includes a base and a lid, each having multiple subunits. The base, in part, is composed of a heterohexameric ring of ATPase subunits belonging to the AAA (ATPases Associated with diverse cellular Activities) family. The ATPase subunits function to unfold the substrate and open the gate formed by the α-subunits, thus exposing the unfolded substrate to the catalytic β-subunits. The lid consists of ubiquitin receptors and DUBs that function in recruitment of ubiquitinated substrates and modification of ubiquitin chain topology (1,2). Other modulators of proteasome activity, such as PA28/11S REG, can also bind to the end of the 20S CP and activate it (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein ubiquitination and deubiquitination are reversible processes catalyzed by ubiquitinating enzymes and deubiquitinating enzymes respectively (1,2). Deubiquitinating enzymes (DUBS) are categorized into five subfamilies based on catalytic domain structure: USP, UCH, OTU, MJD, and JAMM. The deubiquitinase cellular zinc-finger anti-NF-κB (Cezanne-1, OTUD7B) is an OTU family deubiquitinase that contains amino-terminal catalytic and ubiquitin-associated (UBA) domains, and a carboxy-terminal A20-like zinc finger (A20-ZnF) that is involved in ubiquitin binding (3,4). Research studies demonstrate that Cezanne-1 negatively regulates canonical NF-κB signaling induced by TNF receptor signaling by removing K63-linked ubiquitin chains from the RIP1 adaptor protein (5,6). Cezanne-1 negatively regulates non-canonical NF-κB signaling through the deubiquitination and stabilization of the TRAF3 signal transduction protein (7). Additional research suggests that Cezanne-1 is a breast cancer oncogene as the corresponding OTUD7B gene is amplified in a subset of breast cancers and enhances EGFR signaling through a mechanism involving receptor stabilization (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: T cell Ig- and mucin-domain-containing molecules (TIMs) are a family of transmembrane proteins expressed by various immune cells. TIM-1 (HAVCR1 (hepatitis A virus cellular receptor 1), KIM-1 (kidney injury molecule-1) was originally identified as a receptor for hepatitis A virus (1). TIM-1 also acts as a costimulatory receptor on T cells and following activation, associates with the TCR complex to upregulate signaling and cytokine production (2-5). Another TIM family member, TIM-4, is expressed by antigen presenting cells and is a ligand for TIM-1 (6). TIM-1 expressed by Th1 and Th17 cells was also recently shown to interact with P-selectin to mediate T cell trafficking during inflammation and autoimmune disease (7). NKT cells also express TIM-1, and engagement of TIM-1 on NKT cells leads to increased production of IL-4, but decreased production of IFN-gamma (8). TIM-1 is also a receptor for phosphatidylserine exposed by cells undergoing apoptosis. Detection of phosphatidylserine by TIM-1 expressed on NKT cells results in activation, proliferation, and cytokine production (9). Expression of TIM-1 on regulatory B cells is required for optimal production of IL-10. Mice lacking the TIM-1 mucin domain have decreased production of IL-10 by regulatory B cells, hyperactive T cells, increased levels of inflammatory cytokines, and enhanced severity of autoimmune disease (10,11). In addition, TIM-1 polymorphisms are associated with susceptibility to atopic diseases including asthma (12,13). Finally, expression of TIM-1 is increased in renal tubular epithelial cells following kidney injury (14).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

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).

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

Application Methods: Western Blotting

Background: Integrins are α/β heterodimeric cell surface receptors that play a pivotal role in cell adhesion and migration, as well as in growth and survival (1,2). The integrin family contains at least 18 α and 8 β subunits that form 24 known integrins with distinct tissue distribution and overlapping ligand specificities (3). Integrins not only transmit signals to cells in response to the extracellular environment (outside-in signaling), but also sense intracellular cues to alter their interaction with the extracellular environment (inside-out signaling) (1,2).Integrin α5/β1 is involved in multiple biological processes including embryonic development, angiogenesis and tumor metastasis (4,5). By interaction with its fibronectin ligand, α5/β1 transduces signals that regulate cell adhesion, migration, matrix assembly and cytoskeletal organization (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: The potassium/chloride cotransporter 2 (KCC2, SLC12A5) is a neuron-specific transport protein responsible for regulating the cotransport of potassium and chloride ions. KCC2 uses the energy of the electrochemical potassium gradient to export chloride ions from cells, therefore maintaining intracellular chloride ion concentrations in mature neurons (1,2). The intracellular concentration of chloride ions determines the neuronal response to the inhibitory neurotransmitter GABA and glycine. As a result, KCC2 can play a critical role in regulating neuronal excitability in mature central nervous system neurons (3-5). Altered KCC2 expression and reduced KCC2 activity can result in an increase in intracellular chloride ion concentrations and subsequent hyperexcitability of neuronal systems. Cases of aberrant KCC2 function are associated with neurological disorders, such as multiple forms of epilepsy, neuropathic pain, and schizophrenia (6-10).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: IHC-Leica® Bond™, Immunohistochemistry (Paraffin), Western Blotting

Background: Tissue Factor (TF)/CD142 (Coagulation factor III/Thromboplastin) is a type-I transmembrane glycoprotein that serves as the cell surface receptor and cofactor for blood coagulation factors VII and VIIa, and thus plays a central role in hemostasis and thrombosis (1). The TF:VIIa receptor-ligand complex is widely recognized as the initiator of the extrinsic blood coagulation protease cascade, which ultimately leads to the generation of fibrin and thrombin (1). A member of the type-II cytokine receptor superfamily, TF has also been shown to engage the PI3K (2) and MAPK (3) signaling cascades upon binding to factor VIIa in order to drive cellular responses such as cell migration, growth, and proliferation. Although the function of TF under physiologic conditions is to coordinate blood clotting in response to tissue damage, TF is implicated in pathologic conditions such as tumorigenesis. Indeed, TF is aberrantly expressed in colorectal cancer, breast cancer, pancreatic cancer, and glioblastoma multiforme (4). It has been shown to promote tumor angiogenesis, tumor growth, metastasis, and venous thrombosis (5). Given that TF overexpression is associated with numerous types of solid tumors, it has garnered much attention as a potential therapeutic target.

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

Application Methods: Western Blotting

Background: SF2/ASF is a member of the Ser-Arg-rich (SR) protein family of highly conserved nuclear phosphoproteins involved in pre-mRNA splicing (1). Besides its role in nuclear pre-mRNA splicing, SF2/ASF has been shown to shuttle between the nucleus and cytoplasm, suggesting additional roles in mRNA transport and cytoplasmic events (2). SF2/ASF associates with translating ribosomes and stimulates translation (3). It also activates translation initiation by suppressing the activity of 4E-BP1, which is mediated by SF2/ASF association with mTOR and the phosphatase PP2A (4). More recent studies have demonstrated a role for SF2/ASF in microRNA processing (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Members of the Myc/Max/Mad network function as transcriptional regulators with roles in various aspects of cell behavior including proliferation, differentiation and apoptosis (1). These proteins share a common basic-helix-loop-helix leucine zipper (bHLH-ZIP) motif required for dimerization and DNA-binding. Max was originally discovered based on its ability to associate with c-Myc and found to be required for the ability of Myc to bind DNA and activate transcription (2). Subsequently, Max has been viewed as a central component of the transcriptional network, forming homodimers as well as heterodimers with other members of the Myc and Mad families (1). The association between Max and either Myc or Mad can have opposing effects on transcriptional regulation and cell behavior (1). The Mad family consists of four related proteins; Mad1, Mad2 (Mxi1), Mad3 and Mad4, and the more distantly related members of the bHLH-ZIP family, Mnt and Mga. Like Myc, the Mad proteins are tightly regulated with short half-lives. In general, Mad family members interfere with Myc-mediated processes such as proliferation, transformation and prevention of apoptosis by inhibiting transcription (3,4).

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

Application Methods: Immunofluorescence (Frozen), Western Blotting

Background: Myelinated axons contain un-myelinated gaps called nodes of Ranvier. These regularly spaced gaps are critical for the proper propagation and rapid conduction of nerve impulses in the central and peripheral nervous system (1). The structure and organization of the nodes of Ranvier is dictated by interaction between the axon and glial cells (2). Voltage-gated sodium channels concentrated at the nodes and potassium channels clustered at the paranodes are responsible for propagation of the action potentials (3,4). Other proteins that contribute to the architecture and function of the nodes of Ranvier include βIV spectrin (5), ankyrin-G (6), and the L1 cell adhesion molecules, neurofascin and NrCAM (7,8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The mTORC1 kinase complex plays a critical role in cell growth regulation (1, 2). mTORC1 activity is modulated by cellular and environmental factors (e.g., energy levels, growth factors, and amino acids) (3, 4). Amino acid sensing is mediated through several protein complexes, including GATOR (GAP Activity TOward Rags). GATOR is composed of two protein subcomplexes (GATOR1 and GATOR2) that function in opposing fashion to regulate mTORC1 activity. NPRL2 was identified as a component of the GATOR1 subcomplex (also containing DEPDC5 and NPRL3) that functions to negatively regulate mTORC1 activity through activation of RagA and RagB GTPases (5). Conversely, the GATOR2 subcomplex (containing Mios, WDR24, WDR59, Seh1L, and Sec13) positively regulates mTORC1 activity (5). In addition, NPRL2, also known as TUSC4 (tumor suppressor candidate 4), has been shown to prevent the degradation of tumor suppressor BRCA1. Overexpression of TUSC4 (NPRL2) protein inhibits proliferation of breast cancer cells (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: 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, Monkey, Mouse, Rat

Application Methods: Western Blotting

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

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The nuclear protein coilin (COIL) is found in eukaryotic nucleoplasm and serves a marker for sub-organelles known as Cajal bodies (1,2). Cajal bodies (CB) are nuclear structures that are home to various RNA-processing complexes, including those responsible for pre-mRNA splicing, processing of rRNA and histone pre-mRNA, and telomere maintenance (1-3). The presence of coilin protein is essential for CB formation, and the protein plays a role in maintaining Cajal body structural integrity (4,5). Research studies indicate that coilin binds RNA, including telomerase RNA (hTR), pre-rRNA, and U2 snRNA, in addition to DNA (5). Additional research indicates that coilin protein may exhibit specific RNase activity towards hTR and U2 snRNA transcripts, and that this activity may be regulated through phosphorylation of coilin (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: DDX4 is an ATP-dependent DEAD-box RNA helicase found in the chromatoid body of the germ cells (1). This enzyme is specific to germ cells and is necessary for germ cell development (2). Mouse DDX4 was shown to interact with Dicer, suggesting a role in microRNA-mediated RNA silencing (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The Eph receptors are the largest known family of receptor tyrosine kinases (RTKs). They can be divided into two groups based on sequence similarity and on their preference for a subset of ligands: EphA receptors bind to a glycosylphosphatidylinositol-anchored ephrin A ligand; EphB receptors bind to ephrin B proteins that have a transmembrane and cytoplasmic domain (1,2). Research studies have shown that Eph receptors and ligands may be involved in many diseases including cancer (3). Both ephrin A and B ligands have dual functions. As RTK ligands, ephrins stimulate the kinase activity of Eph receptors and activate signaling pathways in receptor-expressing cells. The ephrin extracellular domain is sufficient for this function as long as it is clustered (4). The second function of ephrins has been described as "reverse signaling", whereby the cytoplasmic domain becomes tyrosine phosphorylated, allowing interactions with other proteins that may activate signaling pathways in the ligand-expressing cells (5). Various stimuli can induce tyrosine phosphorylation of ephrin B, including binding to EphB receptors, activation of Src kinase, and stimulation by PDGF and FGF (6). Tyr324 and Tyr327 have been identified as major phosphorylation sites of ephrin B1 in vivo (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Originally identified in Xenopus (1), and later in human cells (2), claspin is a mediator of Chk1 signal transduction at the replication checkpoint and in response to DNA damage. Expression of claspin is cell cycle-regulated, with protein levels peaking at the S/G2 phase (2). Expression is negatively regulated by both proteosome- and caspase-mediated degradation (3), and stabilized by activation of Chk1 (4). Claspin is a chromatin-bound protein, and has been shown to interact with the PNCA complex in the absence of DNA damage (5). Following checkpoint activation it remains chromatin-bound but is released from the PCNA complex and is phosphorylated in an ATR-dependent manner. Phosphorylated claspin interacts with several components of the DNA damage response including BRCA1 (6) and Chk1 (7), leading to ATR-dependent phosphorylation on each of these proteins. Phosphorylated Rad17 has also been shown to bind to and regulate the phosphorylation of claspin (8). It has been proposed that claspin behaves as a tumor suppressor in come cases since down-regulation promotes apoptosis following genotoxic stress (2). Conversely, claspin seems to behave as an oncogene in other instances since overexpression promotes cellular proliferation (6). Upregulated claspin has been suggested to be a sensitive marker of abnormally proliferating cells (9).

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

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

Background: PAR-4 (prostate apoptosis response-4) was identified as a protein that is upregulated in prostate tumor cells undergoing apoptosis (1). Additionally, in parallel studies PAR-4 was found in the yeast two-hybrid system to bind to the Wilms' tumor suppressor protein WT1 and may modulate WT1-medated transcriptional activation (2). PAR-4 contains a leucine zipper domain and a death domain and has been implicated as an effector of apoptosis during tumorigenesis as well as in neurodegenerative disorders (3,4). PAR-4 is widely expressed in normal tissues but can be downregulated in some tumor types. The mechanism of PAR-4 mediated apoptosis regulation appears to be complex and dependent on the cellular context. Studies have indicated roles for PAR-4 in activation of the Fas-FADD-caspase-8 pathway as well as inhibition of the NF-κB pro-survival pathway (5-7). Its activity is likely to depend on the cellular context and post-translational modifications. For instance, phosphorylation of PAR-4 by Akt prevents its nuclear translocation thereby promoting cell surivival (8). In contrast, phoshorylation of rat PAR-4 at T155 by PKA appears to positively regulate its apoptotic activity (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The centrosome is composed of a pair of centrioles surrounded by electron-dense pericentriolar material and functions as the microtubule-organizing center responsible for microtubule nucleation and spindle organization during cell cycle progression (1). Percentriolar material 1 (PCM-1) is a large, 228 kDa protein associated with the centrosome in a cell cycle dependent manner (2). PCM-1 localizes to small cytoplasmic granules called centrosomal satellites (3). PCM-1 is required for the assembly of several centrosomal proteins including centrin, pericentrin, ninein, NEK2, and CEP250 (4-8). Chromosomal translocations involving genes encoding PCM-1 and the tyrosine kinases Ret and Jak2 are associated with some cancers, including papillary thyroid carcinoma and myeloid leukemia (9-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Drosha was identified as a nuclear RNase III that catalyzes the initial step of microRNA (miRNA) processing (1). This enzyme processes the long primary transcript pri-miRNAs into stem-looped pre-miRNAs. Interference of Drosha results in the increase of pri-miRNAs and the decrease of pre-miRNAs (1). Drosha exists in a multiprotein complex called Microprocessor along with other components such as DGCR8 (2). Drosha, along with DGCR8, is necessary for miRNA biogenesis (3).

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

Application Methods: Western Blotting

Background: Rab11a, Rab11b and Rab25 are members of the Rab11 family of small Ras-like GTPases. Rab11 (isoforms Rab11a and Rab11b) functions as a key regulator in the recycling of perinuclear, plasma membrane and Golgi compartment endosomes (1,2). Despite some overlap, distinct differences exist between Rab11a and Rab11b in both their cellular distribution and functional roles. Rab11a is ubiquitously expressed while Rab11b is found mainly in the heart and brain (3,4). Like other Rab proteins, Rab11 exerts its function via interactions with Rab11 family interacting proteins (FIPs). While there are three distinct classes of FIPs, all appear to share a conserved carboxy-terminal Rab-binding domain that allows Rab-FIP protein interaction. When bound together, these proteins are thought to regulate membrane-associated protein sorting (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). It 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. These proteins are involved in the formation of cytoplasmic vacuoles called autophagosomes that are delivered to lysosomes for degradation.The class III type phosphoinositide 3-kinase (PI3KC3)/Vps34 regulates vacuolar trafficking as well as autophagy (4,5). Multiple proteins have been shown to be associated with Vsp34, including: p105/Vsp15, Beclin-1, UVRAG, Atg14, and Rubicon, which can determine Vsp34 function (6-11). UVRAG (UV radiation resistance-associated gene) is associated with the Beclin-1/PI3KC3 complex and promotes PI3KC3 enzymatic activity and autophagy, while suppressing proliferation (11). Beclin-1 binding to UVRAG promotes both autophagosome maturation and endocytic trafficking (12). UVRAG is also a potential tumor suppressor protein with frameshift mutations observed in colon and gastric carcinomas (13,14).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Western Blotting

Background: The cytoskeleton consists of three types of cytosolic fibers: microfilaments (actin filaments), intermediate filaments and microtubules. Major types of intermediate filaments are distinguished and expressed in particular cell types: cytokeratins (epithelial cells), glial fibrillary acidic protein or GFAP (glial cells), desmin (skeletal, visceral and certain vascular smooth muscle cells), vimentin (mesenchyme origin) and neurofilaments (neurons). GFAP and vimentin form intermediate filaments in astroglial cells and modulate their motility and shape (1). In particular, vimentin filaments are present at early developmental stages, while GFAP filaments are characteristic of differentiated and mature brain astrocytes. Thus, GFAP is commonly used as a marker for intracranial and intraspinal tumors arising from astrocytes (2). Vimentin is present in sarcomas, but not carcinomas, and its expression is examined relative to other markers to distinguish between the two forms of neoplasm (3). Desmin is a myogenic marker expressed in early development that forms a network of filaments that extends across the myofibril and surrounds Z discs. The desmin cytoskeleton provides a connection among myofibrils, organelles and the cytoskeleton (4). Desmin knockout mice develop cardiomyopathy, skeletal and smooth muscle defects (5). In humans, desmin related myopathies might be caused by mutations in the corresponding desmin gene or in proteins with which desmin interacts, including αB-crystallin and synemin. Disorganized desmin filaments and the accumulation of protein aggregates comprised predominantly of desmin characterize desmin-related myopathies (reviewed in 6,7).

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

Application Methods: Western Blotting

Background: The Src family of protein tyrosine kinases, which includes Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, are important in the regulation of growth and differentiation of eukaryotic cells (1). Src activity is regulated by tyrosine phosphorylation at two sites, but with opposing effects. While phosphorylation at Tyr416 in the activation loop of the kinase domain upregulates enzyme activity, phosphorylation at Tyr527 in the carboxy-terminal tail by Csk renders the enzyme less active (2).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Rat

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).

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

Application Methods: Western Blotting

Background: High mobility group protein B2 (HMGB2) belongs to a family of highly conserved proteins that contain HMG box domains (1,2). All three family members (HMGB1, HMGB2, and HMGB3) contain two HMG box domains and a C-terminal acidic domain. HMGB1 is a widely expressed and highly abundant protein (2). HMGB2 is widely expressed during embryonic development, but it is restricted to lymphoid organs and testis in adult animals (3). HMGB3 is only expressed during embryogenesis (4). While expression varies, the biochemical properties of the different family members may be indistinguishable. The HMG box domains facilitate the binding of HMGB proteins to the minor groove of DNA, which results in local bending of the DNA double helix (1,2). HMGB proteins are recruited by and help facilitate the assembly of site-specific DNA binding proteins to their cognate binding sites in chromatin. For example, HMGB1 and HMGB2 facilitate the binding of Hox proteins, Oct proteins, p53, Rel proteins, and steroid hormone receptor proteins to their target gene promoters (1,2). Furthermore, HMGB2 interacts with RAG1 to facilitate RAG complex binding to the recombinant signal sequence (RSS) and stimulate DNA-bending and subsequent VDJ cleavage at antigen receptor genes (5,6). In addition to their functions in the nucleus, HMGB proteins play a significant role in extracellular signaling associated with inflammation. HMGB2 is secreted by myeloid cells and promotes proliferation and migration of endothelial cells by binding to the receptor for advanced glycation endproducts (RAGE) (7). Research studies have shown that HMGB2 overexpression in hepatocellular carcinoma is associated with poor prognosis and shorter survival time (8).

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

Application Methods: Western Blotting

Background: Glucose homeostasis is regulated by hormones and cellular energy status. Elevations of blood glucose during feeding stimulate insulin release from pancreatic β-cells through a glucose sensing pathway. Feeding also stimulates release of gut hormones such as glucagon-like peptide-1 (GLP-1), which further induces insulin release, inhibits glucagon release and promotes β-cell viability. CREB-dependent transcription likely plays a role in both glucose sensing and GLP-1 signaling (1). The protein CRTC2 (CREB-regulated transcription coactivator 2)/TORC2 (transducer of regulated CREB activity 2) functions as a CREB co-activator (2,3) and is implicated in mediating the effects of these two pathways (4). In quiescent cells, CRTC2/TORC2 is phosphorylated at Ser171 and becomes sequestered in the cytoplasm via an interaction with 14-3-3 proteins. Glucose and gut hormones lead to the dephosphorylation of CRTC2/TORC2 and its dissociation from 14-3-3 proteins. Dephosphorylated CRTC2/TORC2 enters the nucleus to promote CREB-dependent transcription. CRTC2/TORC2 plays a key role in the regulation of hepatic gluconeogenic gene transcription in response to hormonal and energy signals during fasting (5).CRTC2/TORC2-related proteins CRTC1/TORC1 and CRTC3/TORC3 also act as CREB co-activators (2,3). CRTC1/TORC1, CRTC2/TORC2 and CRTC3/TORC3 associate with the HTLV Tax protein to promote Tax-dependent transcription of HTLV-1 long terminal repeats (6,7). CRTC1/TORC1 is highly phosphorylated at Ser151 in mouse hypothalamic cells under basal conditions (8). When these cells are exposed to cAMP or a calcium activator, CRTC1/TORC1 is dephosphorylated and translocates into the nucleus (8). CRTC1/TORC1 is essential for energy balance and fertility (8).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Clusterin (CLU, apolipoprotein J) is a multifunctional glycoprotein that is expressed ubiquitously in most tissues. Clusterin functions as a secreted chaperone protein that interacts with and stabilizes stress-induced proteins to prevent their precipitation (1,2). Research studies show that clusterin plays a protective role in Alzheimer’s disease by sequestering amyloid β(1-40) peptides to form long-lived, stable complexes, which prevents amyloid fibril formation (3-5).In addition to the secreted protein, several intracellular isoforms are localized to the nucleus, mitochondria, cytoplasm, and ER. The subcellular distribution of these multiple isoforms leads to the diversity of clusterin functions. Additional studies report that clusterin is involved in membrane recycling, cell adhesion, cell proliferation, apoptosis, and tumor survival (6-9). The clusterin precursor is post-translationally cleaved into the mature clusterin α and clusterin β forms. Clusterin α and β chains create a heterodimer through formation of disulfide bonds (10).