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Product listing: Tom20 (D8T4N) Rabbit mAb (HRP Conjugate), UniProt ID Q15388 #72610 to FEN-1 Antibody, UniProt ID P39748 #2746

$305
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Tom20 (D8T4N) Rabbit mAb #42406.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Mitochondria play a central role in cellular energy metabolism and are essential organelles in eukaryotes. In humans, 13 proteins are encoded by the mitochondrial genome while the vast majority of mitochondrial proteins are encoded by the nuclear genome. As a result, most mitochondrial proteins are synthesized as precursors in the cytoplasm and imported across mitochondrial membranes by one or more translocase protein complexes (1). The translocase of the outer mitochondrial membrane (TOM complex) facilitates the import of proteins through the outer mitochondrial membrane, while the complementary translocase of the inner membrane (TIM complex) is responsible for protein transport to the mitochondrial matrix. The TOM complex consists of the receptors Tom20, Tom22, and Tom70, and the channel-forming protein Tom40 (1). Tom20 is localized in the outer mitochondrial membrane and initially recognizes precursors with a presequence to facilitate protein import across the outer mitochondrial membrane (2). In a sequential process, recognition of the presequence by Tom20 is followed by tethering of the presequence to the Tom40 protein complex for efficient protein import (3).

The Jak Isoform Antibody Sampler Kit provides an economical means to examine several Jak isoforms. The kit contains enough primary and secondary antibodies to perform two Western blot experiments per primary antibody.

Background: Members of the Janus family of tyrosine kinases (Jak1, Jak2, Jak3, and Tyk2) are activated by ligands binding to a number of associated cytokine receptors (1). Upon cytokine receptor activation, Jak proteins become autophosphorylated and phosphorylate their associated receptors to provide multiple binding sites for signaling proteins. These associated signaling proteins, such as Stats (2), Shc (3), insulin receptor substrates (4), and focal adhesion kinase (FAK) (5), typically contain SH2 or other phospho-tyrosine-binding domains.

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: p53-binding protein 1 (53BP1) was originally identified as a p53 binding partner that could enhance the transcriptional activity of p53 (1,2). 53BP1 consists of two BRCA1 carboxy terminal (BRCT) domains that allow for binding to p53 and a separate domain responsible for binding to phosphorylated histone H2A.X (3). 53BP1 rapidly translocates to nuclear foci following treatment of cells with ionizing radiation (IR) or radiomimetic agents that cause DNA double strand breaks (DSBs) (4,5). Because of this localization to DSBs and homology to the yeast protein Rad9, a role for 53BP1 in DSB repair has been proposed. Recruitment of 53BP1 to sites of DNA damage has been demonstrated to be independent of ATM, NBS1, and DNA-PK (4) and retention of 53BP1 at DNA breaks requires phosphorylated H2A.X (6). In cells lacking 53BP1, phosphorylation of ATM substrates is reduced, suggesting that 53BP1 is upstream of ATM (7). In response to IR, phosphorylation of 53BP1 at serines 6, 25, 29, and 784 by ATM has been demonstrated, but phosphorylation at these sites is not required for localization of 53BP1 to sites of DSBs (6). Phosphorylation of 53BP1 at Ser1618 has been reported to be enriched in human cells arrested in mitosis (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: CDX2, a homeobox domain-containing transcription factor, is a master regulator of the trophoectoderm, the layer that gives rise to extra-embryonic tissues in mammalian development (1). CDX2 is also involved in intestinal development (2), and gain of expression or loss of expression has been associated with various human malignancies such as Barret Esophagus (3) and colorectal cancer (4,5). Mouse embryonic stem cells deficient in CDX2 display limited hematopoietic progenitor development and altered Hox gene expression (6), pointing to a role for CDX2 in Hox gene regulation. CDX2 is also implicated in the aberrant expression of Hox genes in human AML cell lines (7).

$305
400 µl
This Cell Signaling Technology antibody is immobilized via covalent binding of primary amino groups to N-hydroxysuccinimide (NHS)-activated Sepharose® beads. EGF Receptor (EGFR1) Mouse mAb (IP Specific) (Sepharose® Bead Conjugate) is useful for immunoprecipitation assays. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated EGF Receptor (EGFR1) Mouse mAb (IP Specific) #2256.
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation

Background: The epidermal growth factor (EGF) receptor is a transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization, and lysosomal degradation (1,2). Phosphorylation of EGF receptor (EGFR) at Tyr845 in the kinase domain is implicated in stabilizing the activation loop, maintaining the active state enzyme, and providing a binding surface for substrate proteins (3,4). c-Src is involved in phosphorylation of EGFR at Tyr845 (5). The SH2 domain of PLCγ binds at phospho-Tyr992, resulting in activation of PLCγ-mediated downstream signaling (6). Phosphorylation of EGFR at Tyr1045 creates a major docking site for the adaptor protein c-Cbl, leading to receptor ubiquitination and degradation following EGFR activation (7,8). The GRB2 adaptor protein binds activated EGFR at phospho-Tyr1068 (9). A pair of phosphorylated EGFR residues (Tyr1148 and Tyr1173) provide a docking site for the Shc scaffold protein, with both sites involved in MAP kinase signaling activation (2). Phosphorylation of EGFR at specific serine and threonine residues attenuates EGFR kinase activity. EGFR carboxy-terminal residues Ser1046 and Ser1047 are phosphorylated by CaM kinase II; mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation (10).

$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Mitogen- and stress-activated protein kinase 1 (MSK1) and MSK2 are serine/threonine kinases that promote immediate early gene transcription in stress- or mitogen-induced cells (1-4,7, 8) and LPS-stimulated macrophages (9). MSK2, also known as RSKB, contains two catalytic domains and has been shown to interact directly with p38 MAP kinase (10). MSK2 is phosphorylated and activated in response to tumor necrosis factor, epidermal growth factor or phorbol ester in HeLa cells or murine embryonic fibroblasts (MEFs) in a p38- and ERK-dependent manner (8,11). Phosphorylation on residues Ser196 and Thr568 within the activation loop of both catalytic domains is required for full kinase activation (11). Both MSK1 and MSK2 contain a functional nuclear localization sequence that is sufficient and required for nuclear targeting (10). Consistent with their nuclear localization, these kinases play an important role in regulating transcriptional responses to stress and mitogens. Activation of MSK2 in HeLa cells or MEFs results in rapid phosphorylation of histone H3, HMG-14, CREB and ATF1 and acetylation of histone H3 associated with immediate early gene transcription (3,4,6,7).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Secretory proteins translocate into the endoplasmic reticulum (ER) after their synthesis where they are post-translationally modified and properly folded. To reach their native conformation, many secretory proteins require the formation of intra- or inter-molecular disulfide bonds (1). This process is called oxidative protein folding. Disulfide isomerase (PDI) has two thioredoxin homology domains and catalyzes the formation and isomerization of these disulfide bonds (2). Other ER resident proteins that possess the thioredoxin homology domains, including endoplasmic reticulum resident protein 44 (ERp44), constitute the PDI family (2). ERp44 is induced upon ER stress and is linked to Ero1-Lα and Ero1-Lβ through mixed disulfide bonds (3). ERp44 was shown to mediate the ER localization of Ero1-Lα (4).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Tau is a heterogeneous microtubule-associated protein that promotes and stabilizes microtubule assembly, especially in axons. Six isoforms with different amino-terminal inserts and different numbers of tandem repeats near the carboxy terminus have been identified, and tau is hyperphosphorylated at approximately 25 sites by Erk, GSK-3, and CDK5 (1,2). Phosphorylation decreases the ability of tau to bind to microtubules. Neurofibrillary tangles are a major hallmark of Alzheimer's disease; these tangles are bundles of paired helical filaments composed of hyperphosphorylated tau. In particular, phosphorylation at Ser396 by GSK-3 or CDK5 destabilizes microtubules. Furthermore, research studies have shown that inclusions of tau are found in a number of other neurodegenerative diseases, collectively known as tauopathies (1,3).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 700 fluorescent dye and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated DYKDDDDK Tag (D6W5B) Rabbit mAb #14793.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Flow Cytometry

Background: Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation, and immunostaining techniques. Because of their small size, they are unlikely to affect the tagged protein’s biochemical properties.

The Phototope-HRP Western Blot Detection System is designed for the chemiluminescent detection of proteins in standard Western blotting applications. Proteins and biotinylated molecular weight markers (provided) are separated by SDS-PAGE and transferred onto membrane. Following incubation with your primary anti-serum, horseradish peroxidase (HRP) linked secondary antibody and HRP-linked anti-biotin antibody are bound and then allowed to react with LumiGLO® reagent. The light emitted by destabilized LumiGLO® reagent is subsequently captured on X-ray film.

Background: Chemiluminescence systems have emerged as the best all-around method for western blot detection. They eliminate the hazards associated with radioactive materials and toxic chromogenic substrates. The speed and sensitivity of these methods are unequalled by traditional alternatives, and because results are generated on film, it is possible to record and store data permanently. Blots detected with chemiluminescent methods are easily stripped for subsequent reprobing with additional antibodies. HRP-conjugated secondary antibodies are utilized in conjunction with specific chemiluminescent substrates to generate the light signal. HRP conjugates have a very high turnover rate, yielding good sensitivity with short reaction times.

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Cyclins are a family of proteins that activate specific cyclin-dependent kinases required for progression through the cell cycle. The entry of all eukaryotic cells into mitosis is regulated by activation of cdc2/cdk1 at the G2/M transition. This activation is a multi-step process that begins with the binding of the regulatory subunit, cyclin B1, to cdc2/cdk1 to form the mitosis-promoting factor (MPF). MPF remains in the inactive state until phosphorylation of cdc2/cdk1 at Thr161 by cdk activating kinase (CAK) (1,2) and dephosphorylation of cdc2/cdk1 at Thr14/Tyr15 by cdc25C (3-5). Five cyclin B1 phosphorylation sites (Ser116, 126, 128, 133, and 147) are located in the cytoplasmic retention signal (CRS) domain and are thought to regulate the translocation of cyclin B1 to the nucleus at the G2/M checkpoint, promoting nuclear accumulation and initiation of mitosis (6-9). While MPF itself can phosphorylate Ser126 and Ser128, polo-like kinase 1 (PLK1) phosphorylates cyclin B1 preferentially at Ser133 and possibly at Ser147 (6,10). At the end of mitosis, cyclin B1 is targeted for degradation by the anaphase-promoting complex (APC), allowing for cell cycle progression (11). Research studies have shown that cyclin B1 is overexpressed in breast, prostate, and non-small cell lung cancers (12-14).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated 4E-BP1 (53H11) Rabbit mAb #9644.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: Translation repressor protein 4E-BP1 (also known as PHAS-1) inhibits cap-dependent translation by binding to the translation initiation factor eIF4E. Hyperphosphorylation of 4E-BP1 disrupts this interaction and results in activation of cap-dependent translation (1). Both the PI3 kinase/Akt pathway and FRAP/mTOR kinase regulate 4E-BP1 activity (2,3). Multiple 4E-BP1 residues are phosphorylated in vivo (4). While phosphorylation by FRAP/mTOR at Thr37 and Thr46 does not prevent the binding of 4E-BP1 to eIF4E, it is thought to prime 4E-BP1 for subsequent phosphorylation at Ser65 and Thr70 (5).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometry and immunofluorescent analysis in human and monkey cells, respectively. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated β-Actin (13E5) Rabbit mAb #4970.
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Mouse, Pig, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Actin, a ubiquitous eukaryotic protein, is the major component of the cytoskeleton. At least six isoforms are known in mammals. Nonmuscle β- and γ-actin, also known as cytoplasmic actin, are predominantly expressed in nonmuscle cells, controlling cell structure and motility (1). α-cardiac and α-skeletal actin are expressed in striated cardiac and skeletal muscles, respectively; two smooth muscle actins, α- and γ-actin, are found primarily in vascular smooth muscle and enteric smooth muscle, respectively. These actin isoforms regulate the contractile potential of muscle cells (1). Actin exists mainly as a fibrous polymer, F-actin. In response to cytoskeletal reorganizing signals during processes such as cytokinesis, endocytosis, or stress, cofilin promotes fragmentation and depolymerization of F-actin, resulting in an increase in the monomeric globular form, G-actin (2). The ARP2/3 complex stabilizes F-actin fragments and promotes formation of new actin filaments (2). Research studies have shown that actin is hyperphosphorylated in primary breast tumors (3). Cleavage of actin under apoptotic conditions has been observed in vitro and in cardiac and skeletal muscle, as shown in research studies (4-6). Actin cleavage by caspase-3 may accelerate ubiquitin/proteasome-dependent muscle proteolysis (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: T-cell intracellular antibody 1 (TIA-1) is a member of the RNA-recognition motif (RRM) family of RNA-binding proteins that was originally found to induce DNA fragmentation in digitonin-permeabilized thymocytes (1). TIA-1 protein has about 80% identity to the related TIAR protein, both of which possess three amino-terminal RRM domains and a glutamine-rich carboxyl terminus (1,2). Alternative splicing is responsible for generating at least two isoforms of TIA-1 and TIAR (3,4). Several research studies indicate that TIA-1 and TIAR play a role in apoptosis, cellular stress, and inflammation. Importantly, TIA-1 and TIAR translocate from the nucleus to stress granules in response to a variety of environmental stresses (5-8). Stress granules function as sites of translational repression in response to potentially damaging conditions. mRNA transcripts targeted by TIA-1 and TIAR include TNF-α, COX-2, cytochrome c, GADD45α, and HIF-1α (8-13).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The NDRG (N-Myc downstream-regulated gene) family consisting of NDRG1, NDRG2, NDRG3, and NDRG4 are structurally related proteins with roles in cell proliferation, differentiation, apoptosis, stress responses, and cell migration/metastasis (1-3). NDRG1 was originally identified as a protein that was upregulated in N-Myc knockout mice (1). Proteins in the NDRG family, particularly NDRG1 and NDRG2, have been reported to be down-regulated in various cancer tissues and have been suggested to function as a tumor suppressors (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: SNARK was identified as an SNF1/AMPK-related kinase and member of the AMPK catalytic subunit family (1,2). This enzyme was separately identified as a TNFα-induced SNF1-like kinase 2 (NUAK2) (3). The kinase activity of SNARK/NUAK2 is increased by AMP and AICAR (1). SNARK/NUAK2 activity is regulated by a variety of cellular stresses such as endoplasmic reticulum (ER) stress and oxidative stresses (4), suggesting that SNARK/NUAK2 is a signaling molecule involved in the cell stress response (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: β1-Adrenergic Receptor (β1AR) is a G protein-coupled receptor (GPCR) involved in the regulation of cardiovascular functions (1). Together with β2AR, β1AR is a major βAR in the heart. β1AR is activated by catecholamines and couples to Gαs protein, activating adenylate cyclase and increasing intracellular cAMP levels (2). Beta-blockers (βAR antagonists), one of the major class of therapeutics in cardiovascular medicine, act mostly by preventing catecholamine binding to β1AR (3).

$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).

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

Application Methods: 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
Bovine

Application Methods: Western Blotting

Background: Bovine serum albumin (BSA) is the most abundant protein in plasma. Albumin is predominantly synthesized in the liver and is a major transportation component for many endogenous and exogenous compounds, including fatty acids, steroid hormones, metabolites and drugs. It is also responsible for maintaining colloid osmotic pressure and may affect microvascular integrity (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

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

Background: PITSLRE, alternatively known as cell division kinase 11 (CDK11), is the result of duplication of the CDK11 gene (1). CDK11A and CDK11B encode nearly identical serine/threonine protein kinases, PITSLREB and PITSLREA respectively, both belonging to the p34CDC2 family of protein kinases (2). Full-length PITSLRE/CDK11 (commonly referred to as CDK11p110) is expressed ubiquitously throughout the cell cycle whereas a smaller, alternate transcript (CDK11p58), the result of internal ribosomal entry, is expressed only during the G2/M transition where it promotes centrosome maturation and spindle formation (3-5). During induction of apoptosis by Fas or TNF, or anoikis, PITSLRE/CDK11 is cleaved by caspases to generate p110C, an approximately 46 kDa protein that contains the catalytically active kinase domain of PITSLRE/CDK11 that interacts with and inhibits p21-activated kinase (PAK1) activity (6-8). Full length PITSLRE/CDK11 (CDK11p110) appears to participate in pre-mRNA splicing events. This is demonstrated by the observation that CDK11p110 interacts with numerous splicing factors including RNPS1, 9G8/SRSF7 and cyclin L and that CDK11p110 can phosphorylate and inhibit the splicing activity of 9G8/SRSF7 (9-11).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The mediator complex consists of about 25-30 proteins and is thought to facilitate transcription activation by acting as a molecular bridge between the RNA polymerase II (RNAPII) machinery and transcription factors (1). Mediator is recruited to target genes by transcription factors and plays an essential role in the recruitment and stabilization of the RNAPII transcription complex at promoters, as well as the activation of transcription post RNAPII recruitment (1-5). The mediator complex also plays an important role in creating ‘chromatin loops’ that occur as a result of interactions between the transcription factor bound at distal enhancers and RNAPII bound at the proximal promoter, and works to sustain proper chromatin architecture during active transcription (6-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: The minichromosome maintenance (MCM) 2-7 proteins are a family of six related proteins required for initiation and elongation of DNA replication. MCM2-7 bind together to form the heterohexameric MCM complex that is thought to act as a replicative helicase at the DNA replication fork (1-5). This complex is a key component of the pre-replication complex (pre-RC) (reviewed in 1). Cdc6 and CDT1 recruit the MCM complex to the origin recognition complex (ORC) during late mitosis/early G1 phase forming the pre-RC and licensing the DNA for replication (reviewed in 2). Licensing of the chromatin permits the DNA to replicate only once per cell cycle, thereby helping to ensure that genetic alterations and malignant cell growth do not occur (reviewed in 3). Phosphorylation of the MCM2, MCM3, MCM4, and MCM6 subunits appears to regulate MCM complex activity and the initiation of DNA synthesis (6-8). CDK1 phosphorylation of MCM3 at Ser112 during late mitosis/early G1 phase has been shown to initiate complex formation and chromatin loading in vitro (8). Phosphorylation of MCM2 at serine 139 by cdc7/dbf4 coincides with the initiation of DNA replication (9). MCM proteins are removed during DNA replication, causing chromatin to become unlicensed through inhibition of pre-RC reformation. Studies have shown that the MCM complex is involved in checkpoint control by protecting the structure of the replication fork and assisting in restarting replication by recruiting checkpoint proteins after arrest (reviewed in 3,10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Eukaryotic initiation factor 6 (eIF6) is reqiured for the 60S ribosomal subunit assembly in the nucleolus (1). In the cytoplasm, this protein is bound to 60S ribosome subunits and prevents them from joining 40S ribosome subunits to form 80S ribosomes (2). eIF6 is also shown to associate with the RNA-induced silencing complex (RISC) (3). Deletion of eIF6 abolishes the miRNA-mediated gene silencing (3). eIF6 may play its essential role in miRNA-mediated silencing by inhibiting translation initiation or ribosome recycling (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Neurite outgrowth inhibition protein (Nogo, RTN4) is a reticulon family protein that was identified as an axonal growth inhibitor of the central nervous system (CNS). Nogo occurs as three major isoforms (Nogo-A, Nogo-B, and Nogo-C) that share a common carboxy terminus of 188 amino acids. Nogo-A is transmembrane protein enriched in the endoplasmic reticulum and expressed at high levels in the CNS, and more weakly in skeletal and heart muscle (1-3). Expression of Nogo-A decreases with increasing age during brain development. In the adult CNS, negative regulation of neuronal growth leads to stabilization of the CNS wiring at the expense of extensive plastic rearrangements. Nogo-A meditates inhibition of neurite growth together with the nogo receptor 1 (NgR1), the p75 neurotrophin receptor p75NTR, and the transmembrane LINGO1 protein. This Nogo receptor signaling complex activates the RhoA/ROCK pathway, which collapses neuronal growth cones and inhibits axonal growth in the CNS following traumatic brain injury. Research studies suggest that inhibition of Nogo A may be beneficial to patients with traumatic brain injury. Nogo-B and Nogo-C inhibit BACE1 activity and amyloid precursor protein processing, suggesting a role in cell survival (4).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: Eukaryotic initiation factor 4B (eIF4B) is thought to assist the eIF4F complex in translation initiation. In plants, eIF4B is known to interact with the poly-(A) binding protein, increasing its poly-(A) binding activity (1). Heat shock and serum starvation cause dephosphorylation of eIF4B at multiple sites with kinetics similar to those of the corresponding inhibition of translation, while phosphorylation of eIF4B following insulin treatment correlates well with an observed increase in translation (2-5). Multiple kinases, including p70 S6 kinase, can phosphorylate eIF4B in vitro, and at least one serum-inducible eIF4B phosphorylation site is sensitive to rapamycin and LY294002 (6). Recently, Ser406 was identified as a novel phosphorylation site regulated by mitogens (7), and the phosphorylation of this site is dependent on MEK and mTOR activity (7). This phosphorylation is shown to be essential for the translational activity of eIF4B (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: LIN28A and LIN28B are conserved, developmentally regulated RNA binding proteins that inhibit the processing and maturation of the let-7 family of miRNAs (1,2). The let-7 miRNAs have been implicated in repression of oncogenes such as Ras, Myc, and HMGA2 (3). It has recently been shown that upregulation of LIN28A and LIN28B in primary human tumors and human cancer cell lines is correlated with downregulation of let-7 miRNAs (4). LIN28 genes are reported to be involved in primordial germ cell development and germ cell malignancy (5). In addition, allelic variation in LIN28B is associated with regulating the timing of puberty in humans (6). Overexpression of LIN28A, in conjunction with Oct-4, Sox2, and Nanog, can reprogram human fibroblasts to pluripotent, ES-like cells (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: CENP-F (mitosin), is a kinetochore-associated protein whose expression and localization to chromatin is regulated in a cell cycle-dependent manner, with its highest expression in G2/M phases (1, 2). CENP-F is required for appropriate localization of other kinetocore-associated proteins, including CENP-E. CENP-F regulates kinetocore function and maintenance of the mitotic spindle checkpoint. Farnesylation of CENP-F is required for its localization and function (3). CENP-F also interacts with the mitochondrial protein, miro, to direct the distribution of mitochondria to daughter cells as they exit mitosis (4). Researchers have shown that CENP-F drives prostate tumor growth synergistically with FOXM1 in human and mouse (5), and that the gene for CENP-F is among those frequently amplified in hepatocellular, head and neck, and esophageal carcinomas (6-8). CENP-F expression has also been shown in research studies to be associated with poor prognosis in breast cancer (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: Syndecans are a family of type 1 transmembrane heparan sulphate proteoglycans comprising 4 members in mammals (SDC-1 to -4) (1) encoded by four syndecan genes. Syndecans are involved in embryonic development, tumorigenesis, and angiogenesis (2). The extracellular domain harbors attachment sites for heparan sulfate and chondroitin sulfate chains, facilitating interaction with an array of proteins including a plethora of growth factors. In addition, the hydrophobic C-terminal intracellular domain can interact with proteins containing a PDZ domain (2). These interactions place syndecans as important integrators of membrane signaling (3). Syndecans undergo proteolytic cleavage causing the release of their extracellular domain (shedding), converting the membrane-bound proteins into soluble molecular effectors (4).

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

Application Methods: Western Blotting

Background: Flap endonuclease-1 (FEN-1) is a structure-specific nuclease with multiple functions in DNA processing pathways (1,2). The replication and DNA repair activities of FEN-1 are critical for genomic stability in the eukaryotic cell. Through interaction with proliferation cell nuclear antigen (PCNA), FEN-1 helps coordinate Okazaki fragment maturation by removing RNA-DNA primers (3). FEN-1 is also required for non-homologous end joining of double stranded DNA breaks in long patch base excision repair (4,5). The multi-functional activities of FEN-1 are regulated by various mechanisms, including protein partner interactions (6,7), post-translational modifications (8,9), and subcellular re-localization in response to cell cycle or DNA damage (10).