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Product listing: Pro-Apoptosis Bcl-2 Family Antibody Sampler Kit, UniProt ID O43521 #9942 to AMPKα1 Antibody, UniProt ID Q13131 #2795

The Pro-Apoptosis Bcl-2 Family Antibody Sampler Kit provides an economical means to examine several members of the Bcl-2 family and their activation status. The kit contains enough primary and secondary antibodies to perform two Western blot experiments per primary antibody.

Background: The Bcl-2 family consists of a number of evolutionarily conserved proteins containing Bcl-2 homology domains (BH) that regulate apoptosis through control of mitochondrial membrane permeability and release of cytochrome c (1-3). Four BH domains have been identified (BH1-4) that mediate protein interactions. The family can be separated into three groups based upon function and sequence homology: pro-survival members include Bcl-2, Bcl-xL, Mcl-1, A1 and Bcl-w; pro-apoptotic proteins include Bax, Bak and Bok; and "BH3 only" proteins Bad, Bik, Bid, Puma, Bim, Bmf, Noxa and Hrk. Interactions between death-promoting and death-suppressing Bcl-2 family members has led to a rheostat model in which the ratio of pro-apoptotic and anti-apoptotic proteins controls cell fate (4). Thus, pro-survival members exert their behavior by binding to and antagonizing death-promoting members. In general, the "BH3-only members" can bind to and antagonize the pro-survival proteins leading to increased apoptosis (5). While some redundancy of this system likely exists, tissue specificity, transcriptional and post-translational regulation of many of these family members can account for distinct physiological roles.

$364
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometric analysis of human cells. The unconjugated antibody #4060 reacts with human, mouse and rat Phospho-Akt protein. CST expects that Phospho-Akt (Ser473) (D9E) XP® Rabbit mAb (Alexa Fluor® 488 Conjugate) will also recognize Phospho-Akt in these species.
APPLICATIONS
REACTIVITY
Bovine, D. melanogaster, Hamster, Human, Monkey, Mouse, Rat, Zebrafish

Application Methods: Flow Cytometry

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).

$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. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated FoxO1 (C29H4) Rabbit mAb #2880.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: The Forkhead family of transcription factors is involved in tumorigenesis of rhabdomyosarcoma and acute leukemias (1-3). Within the family, three members (FoxO1, FoxO4, and FoxO3a) have sequence similarity to the nematode orthologue DAF-16, which mediates signaling via a pathway involving IGFR1, PI3K, and Akt (4-6). Active forkhead members act as tumor suppressors by promoting cell cycle arrest and apoptosis. Increased expression of any FoxO member results in the activation of the cell cycle inhibitor p27 Kip1. Forkhead transcription factors also play a part in TGF-β-mediated upregulation of p21 Cip1, a process negatively regulated through PI3K (7). Increased proliferation results when forkhead transcription factors are inactivated through phosphorylation by Akt at Thr24, Ser256, and Ser319, which results in nuclear export and inhibition of transcription factor activity (8). Forkhead transcription factors can also be inhibited by the deacetylase sirtuin (SirT1) (9).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (8).

$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 antibody (α-Tubulin (11H10) Rabbit mAb #2125).
APPLICATIONS
REACTIVITY
Bovine, D. melanogaster, Human, Monkey, Mouse, Pig, Rat, Zebrafish

Application Methods: 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).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mink, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Transcription factors of the nuclear factor κB (NF-κB)/Rel family play a pivotal role in inflammatory and immune responses (1,2). There are five family members in mammals: RelA, c-Rel, RelB, NF-κB1 (p105/p50), and NF-κB2 (p100/p52). Both p105 and p100 are proteolytically processed by the proteasome to produce p50 and p52, respectively. Rel proteins bind p50 and p52 to form dimeric complexes that bind DNA and regulate transcription. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins (3-5). NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKKα (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which translocates to the nucleus (9-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Tuberous sclerosis complex (TSC) is an autosomal dominant disorder that causes symptoms including hamartomas in brain, kidney, heart, lung and skin (1). The tumor suppressor genes TSC1 and TSC2 encode hamartin and tuberin, respectively (2,3). Hamartin and tuberin form a functional complex and are involved in numerous cellular activities such as vesicular trafficking, regulation of the G1 phase of the cell cycle, steroid hormone regulation, Rho activation and anchoring neuronal intermediate filaments to the actin cytoskeleton (4-9). The combination of genetic, biochemical and cell-biological studies demonstrate that the tuberin/hamartin complex functions as a GTPase-activating protein for the Ras-related small G protein Rheb and thus inhibits targets of rapamycin including mTOR. Cells lacking hamartin or tuberin fail to inhibit phosphorylation of S6 kinase resulting in the activation of S6 ribosomal protein's translation of 5'TOP mRNA transcripts (10). Hamartin is phosphorylated by CDK1 (cdc2) at Thr417, Ser584 and Thr1047 in cells in G2/M phase of the cell cycle (11).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The aldehyde dehydrogenase family is a large group of enzymes that oxidize aldehydes formed through metabolic processes to their carboxylic acids (1). ALDH1A1 is a liver cytosolic isoform of acetaldehyde dehydrogenase and is involved in the major pathway of alcohol metabolism along with alcohol dehydrogenase (2). ALDH1A1 is also known as retinal dehydrogenase 1 and is involved in retinol metabolism, converting retinol to retinoic acid (3). Recent studies suggest that control of retinoid signaling through ALDH1A1 may influence hematopoietic stem cell differentiation (4). There has been recent interest in ALDH1 isoforms as predictive biomarkers in disease. Several studies have suggested that ALDH1A1 is a potential marker for cancer stem cells and chemoresistance in several tumor types, such as melanoma (5), lung cancer (6), and glioblastoma (7).

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

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

Background: Wiskott-Aldrich syndrome proteins (WASPs) mediate actin dynamics by activating the Arp2/3 actin nucleation complex in response to activated Rho family GTPases. In mammals, five WASP family members have been described. Hematopoietic WASP and ubiquitously expressed N-WASP are autoinhibited in unstimulated cells. Upon stimulation they are activated by cdc42, which relieves the autoinhibition in conjunction with phosphatidyl inositol 4,5-bisphosphate. Three WAVE (Wasf, SCAR) family proteins are similar in sequence to WASP and N-WASP but lack the WASP/N-WASP autoinhibition domains and are indirectly activated by Rac (reviewed in 1). Both WASP and WAVE functions appear to be essential, as knockout of either N-WASP or Scar-2 in mice results in cardiac and neuronal defects and embryonic lethality (2,3). Loss of WASP results in immune system defects and fewer immune cells (4). WAVE-2 (WASF2) is widely distributed, while WAVE-1 and WAVE-3 are strongly expressed in brain (5). WAVE-3 may act as a tumor suppressor in neuroblastoma, a childhood disease of the sympathetic nervous system (6). Increased expression of WAVE-3 is seen in breast cancer, and studies in breast adenocarcinoma cells indicate that WAVE-3 regulates breast cancer progression, invasion and metastasis through the p38 mitogen-activated protein kinase (MAPK) pathway (7,8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Synaptophysin (SYP) is a neuronal synaptic vesicle glycoprotein that is expressed in neuroendocrine cells and neoplasms (1). Synaptophysin contains four transmembrane domains that form a hexameric channel or gap junction-like pore (2). Synaptophysin binds to the SNARE protein synaptobrevin/VAMP, which prevents the inclusion of synaptobrevin in the synaptic vesicle fusion complex and creates a pool of synaptobrevin for exocytosis when synapse activity increases (3). Synaptophysin is also responsible for targeting synaptobrevin 2/VAMP2 to synaptic vesicles, a critical component of the fusion complex (4).

Molecular Weight: 792.3 g/mol(Average based on isomer content)

Background: During oxidative phosphorylation in mitochondria, the electron transport system pumps H+ from the matrix into the intermembrane compartment. This process generates a H+ gradient across the mitochondrial inner membrane. This H+ gradient is used to drive mitochondrial FoF1 ATPase to convert ADP to ATP. Oligomycin, an antibiotic from Streptomyces diastatochromogenes, blocks oxidative phosphorylation by binding to the Fo part of the ATPase to inhibit its activity (1-3).

$303
100 µl
$717
300 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: CrkL, a 39 kDa adaptor protein, has a key regulatory role in hematopoietic cells. CrkL has one SH2 and two SH3 domains, with 60% homology to CrkII (1). The amino-terminal SH3 domain of CrkL binds proteins such as C3G, SOS, PI3K, c-Abl and BCR/Abl. The SH2 domain of CrkL can bind to tyrosine-phosphorylated proteins such as Cbl, HEF1, CAS and paxillin (2,3). CrkL is involved in various signaling cascades initiated by different cytokines and growth factors. The biological outcomes of the Crk-activated signal transduction include the modulation of cell adhesion, cell migration and immune cell responses (4). CrkL is a prominent substrate of the BCR/Abl oncoprotein in chronic myelogenous leukemia and binds to both BCR/Abl and c-Abl (5). CrkL is prominently and constitutively tyrosine phosphorylated in CML neutrophils and is not phosphorylated in normal neutrophils. Moreover, stimulation of normal neutrophils with cytokines and agonists does not induce tyrosine phosphorylation of this protein (6), indicating that it may be a useful target for therapeutic intervention or as a disease marker. Tyr207 in CrkL is the BCR/Abl phosphorylation site (7).

$305
400 µl
This Cell Signaling Technology antibody is immobilized by the covalent reaction of hydrazinonicotinamide-modifed antibody with formylbenzamide-modified magnetic bead. Myc-Tag (9B11) Mouse mAb (Magnetic Bead Conjugate) is useful for immunoprecipitation assays of Myc epitope-tagged proteins.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Immunoprecipitation

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.

$303
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Western Blotting

Background: Dynamin-related protein 1 (DRP1) is a member of the dynamin superfamily of GTPases. Members of this family have diverse cellular functions including vesicle scission, organelle fission, viral resistance, and intracellular trafficking (reviewed in 1). DRP1 affects mitochondrial morphology and is important in mitochondrial and peroxisomal fission in mammalian cells (2-5). The yeast ortholog of DRP1 clusters into a spiral-shaped structure on the mitochondrial membrane at the site of fission (reviewed in 6), and this structure is likely conserved in mammalian cells (3). The division of the mitochondria, which is required for apoptosis, as well as normal cell growth and development is controlled, in part, by the phosphorylation of DRP1 at Ser616 by Cdk1/cyclin B and at Ser637 by protein kinase A (PKA) (reviewed in 6). When phosphorylated at Ser616, DRP1 stimulates mitochondrial fission during mitosis. Conversely, fission is inhibited when DRP1 is phosphorylated at Ser637 (reviewed in 6). Dephosphorylation at Ser637 by calcineurin reverses this inhibition (7). In addition to phosphorylation, sumoylation of DRP1 is also an enhancer of mitochondrial fission (8). Balancing fission and fusion events is essential for proper mitochondrial function. Research studies have demonstrated mitochondrial defects in a variety of neurodegenerative diseases including Alzheimer’s disease, Parkinson’s disease, and Huntington’s disease (reviewed in 6).

$303
100 µl
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Mouse, Rat

Application Methods: Western Blotting

Background: SAPK/Erk kinase (SEK1), also known as MKK4 or Jun kinase kinase (JNKK), activates the MAP kinase homologues SAPK and JNK in response to various cellular stresses and inflammatory cytokines (1-3). Activation of SEK1 occurs through MEKK phosphorylation of serine and threonine residues at positions 257 and 261, respectively. Like MEK, SEK is a dual-specificity protein kinase that phosphorylates SAPK/JNK at a conserved T*PY* site in its activation loop (4). Phosphorylation by Akt at Ser80 inhibits SEK1 and suppresses stress-activated signal transduction (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). Autophagy is generally activated by conditions of nutrient deprivation but is also 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 is directed by a number of autophagy-related (Atg) genes. These proteins are involved in the formation of autophagosomes, which are cytoplasmic vacuoles that are delivered to lysosomes for degradation. The class III type phosphoinositide 3-kinase (PI3K) Vps34 regulates vacuolar trafficking and autophagy (4,5). Multiple proteins associate with Vps34, including p105/Vps15, Beclin-1, UVRAG, Atg14, and Rubicon (6-12). Atg14 and Rubicon were identified based on their ability to bind to Beclin-1 and participate in unique complexes with opposing functions (9-12). Rubicon, which localizes to the endosome and lysosome, inhibits Vps34 lipid kinase activity; knockdown of Rubicon enhances autophagy and endocytic trafficking (11,12). In contrast, Atg14 localizes to autophagosomes, isolation membranes, and ER and can enhance Vps34 activity. Knockdown of Atg14 inhibits starvation-induced autophagy (11,12).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Postsynaptic Density protein 95 (PSD95) is a member of the membrane-associated guanylate kinase (MAGUK) family of proteins. These family members consist of an amino-terminal variable segment followed by three PDZ domains, a SH3 domain, and an inactive guanylate kinase (GK) domain. PSD95 is a scaffolding protein involved in the assembly and function of the postsynaptic density complex (1-2). PSD95 participates in synaptic targeting of AMPA receptors through an indirect manner involving Stargazin and related transmembrane AMPA receptor regulatory proteins (TARPs) (3). It is implicated in experience-dependent plasticity and plays an indispensable role in learning (4). Mutations in PSD95 are associated with autism (5).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The Na,K-ATPase is an integral membrane heterodimer belonging to the P-type ATPase family. This ion channel uses the energy derived from ATP hydrolysis to maintain membrane potential by driving sodium export and potassium import across the plasma membrane against their electrochemical gradients. It is composed of a catalytic α subunit and a β subunit (reviewed in 1). Several phosphorylation sites have been identified for the α1 subunit. Tyr10 is phosphorylated by an as yet undetermined kinase (2), Ser16 and Ser23 are phosphorylated by PKC, and Ser943 is phosphorylated by PKA (3-5). All of these sites have been implicated in the regulation of enzyme activity in response to hormones and neurotransmitters, altering trafficking and kinetic properties of Na,K-ATPase. Altered phosphorylation in response to angiotensin II stimulates activity in the rat proximal tubule (6). Na,K-ATPase is also involved in other signal transduction pathways. Insulin regulates its localization in differentiated primary human skeletal muscle cells, and this regulation is dependent on ERK1/2 phosphorylation of the α subunit (7). Na,K-ATPase and Src form a signaling receptor complex that affects regulation of Src kinase activity and, subsequently, its downstream effectors (8,9).

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

Application Methods: Chromatin IP, Chromatin IP-seq, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: The polycomb group (PcG) of proteins contributes to the maintenance of cell identity, stem cell self-renewal, cell cycle regulation, and oncogenesis by maintaining the silenced state of genes that promote cell lineage specification, cell death, and cell-cycle arrest (1-4). PcG proteins exist in two complexes that cooperate to maintain long-term gene silencing through epigenetic chromatin modifications. The first complex, EED-EZH2, is recruited to genes by DNA-binding transcription factors and methylates histone H3 on Lys27. This histone methyl-transferase activity requires the Ezh2, Eed, and Suz12 subunits of the complex (5). Histone H3 methylation at Lys27 facilitates the recruitment of the second complex, PRC1, which ubiquitinylates histone H2A on Lys119 (6). Bmi1 is a component of the PRC1 complex, which together with Ring1 strongly enhances the E3 ubiquitin ligase activity of the Ring2 catalytic subunit (7). Bmi1 plays an important role in the regulation of cell proliferation and senescence through repression of the p16 INK4A and p19 ARF genes and is required for maintenance of adult hematopoietic and neural stem cells (3,4,8-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Lysosome-associated membrane protein 1 and 2 (LAMP1 and LAMP2) are two abundant lysosomal membrane proteins (1,2). Both are transmembrane proteins and are heavily glycosylated at the amino-terminal luminal side of the lysosomal inner leaflet, which protects the proteins from proteolysis (3). The carboxy terminus of LAMP1 is exposed to the cytoplasm and contains a tyrosine sorting motif that targets LAMP to lysosomal membranes (4). LAMP1 and LAMP2 are 37% homologous in their protein sequences. Both LAMP1 and LAMP2 are involved in regulating lysosomal motility during lysosome-phagosome fusion and cholesterol trafficking (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: N-methyl-D-aspartate receptor (NMDAR) forms a heterodimer of at least one NR1 and one NR2A-D subunit. Multiple receptor isoforms with distinct brain distributions and functional properties arise by selective splicing of the NR1 transcripts and differential expression of the NR2 subunits. NR1 subunits bind the co-agonist glycine and NR2 subunits bind the neurotransmitter glutamate. Activation of the NMDA receptor or opening of the ion channel allows flow of Na+ and Ca2+ ions into the cell, and K+ out of the cell (1). Each subunit has a cytoplasmic domain that can be directly modified by the protein kinase/phosphatase (2). PKC can phosphorylate the NR1 subunit (NMDAR1) of the receptor at Ser890/Ser896, and PKA can phosphorylate NR1 at Ser897 (3). The phosphorylation of NR1 by PKC decreases its affinity for calmodulin, thus preventing the inhibitory effect of calmodulin on NMDAR (4). The phosphorylation of NR1 by PKA probably counteracts the inhibitory effect of calcineurin on the receptor (5). NMDAR mediates long-term potentiation and slow postsynaptic excitation, which play central roles in learning, neurodevelopment, and neuroplasticity (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The breast cancer susceptibility proteins BRCA1 and BRCA2 are frequently mutated in cases of hereditary breast and ovarian cancers and have roles in multiple processes related to DNA damage, repair, cell cycle progression, transcription, ubiquitination, and apoptosis (1-4). BRCA2 has been shown to be required for localization of Rad51 to sites of double stranded breaks (DSBs) in DNA, and cells lacking BRCA1 and BRCA2 cannot repair DSBs through the Rad51-dependent process of homologous recombination (HR) (5). Numerous DNA damage-induced phosphorylation sites on BRCA1 have been identified, including Ser988, 1189, 1387, 1423, 1457, 1524, and 1542, and kinases activated in a cell cycle-dependent manner, including Aurora A and CDK2, can also phosphorylate BRCA1 at Ser308 and Ser1497, respectively (6-10). Cell cycle-dependent phosphorylation of BRCA2 at Ser3291 by CDKs has been proposed as a mechanism to switch off HR as cells progress beyond S-phase by blocking the carboxy terminal Rad51 binding site (11).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The carboxy terminus of Hsc70-interacting protein (CHIP, STUB1) is a co-chaperone protein and functional E3 ubiquitin ligase that links the polypeptide binding activity of Hsp70 to the ubiquitin proteasome system (1). Cytoplasmic CHIP protein contains three 34-amino acid TPR (tetratricopeptide repeat) domains at its amino terminus and a carboxy-terminal U-box domain. CHIP interacts with the molecular chaperones Hsc70-Hsp70 and Hsp90 through its TPR domain, while E3 ubiquitin ligase activity is confined to the U-box domain (2,3). The binding of CHIP to Hsp70 can stall the folding of Hsp70 client proteins and concomitantly facilitate the U-box dependent ubiquitination of Hsp70-bound substrates (4-6). CHIP appears to play a central role in cell stress protection (7) and is responsible for the degradation of disease-related proteins that include cystic fibrosis transmembrane conductance regulator (4), p53 (8), huntingtin and Ataxin-3 (9), Tau protein (10), and α-synuclein (11).

$260
100 µl
APPLICATIONS

Application Methods: Immunoprecipitation, Western Blotting

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.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The Hippo pathway is an important evolutionarily conserved signaling pathway that controls organ size and tumor suppression by inhibiting cell proliferation and promoting apoptosis (1,2). An integral function of the Hippo pathway is to repress the activity of Yes-associated protein (YAP), a proposed oncogene whose activity is regulated by phosphorylation and subcellular localization (3,4). When the Hippo pathway is turned off, YAP is phosphorylated and translocates to the nucleus where it associates with various transcription factors including members of the transcriptional enhancer factor (TEF) family, also known as the TEA domain (TEAD) family (TEAD1-4) (5,6). Although widely expressed in tissues, the TEAD family proteins have specific tissue and developmental distributions. YAP/TEAD complexes regulate the expression of genes involved in cell proliferation and apoptosis (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: Lysosome-associated membrane protein 1 and 2 (LAMP1 and LAMP2) are two abundant lysosomal membrane proteins (1,2). Both are transmembrane proteins and are heavily glycosylated at the amino-terminal luminal side of the lysosomal inner leaflet, which protects the proteins from proteolysis (3). The carboxy terminus of LAMP1 is exposed to the cytoplasm and contains a tyrosine sorting motif that targets LAMP to lysosomal membranes (4). LAMP1 and LAMP2 are 37% homologous in their protein sequences. Both LAMP1 and LAMP2 are involved in regulating lysosomal motility during lysosome-phagosome fusion and cholesterol trafficking (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Interleukin-1β (IL-1β) is a proinflammatory cytokine produced predominantly by activated monocytes and epithelial cells (1). Precursor IL-1β is cleaved by caspase-1 and mature IL-1β is then secreted (1-3). Target cells include macrophages and many other cell types. Signaling by IL-1β involves IL-1β binding to IL-1 accessory protein (IL-1-AcP); the complex then binds to IL-1RI (1,2). Signaling occurs through activation of MAP kinase and NF-κB pathways (1,2). IL-1β also binds to IL-1RII, which lacks an intracellular signaling domain and thereby serves as a high affinity decoy receptor. IL-1β binding to IL-1RI is inhibited by the negative regulator, IL-1R antagonist (IL-1Ra). IL-1Ra binding to IL-1RI does not signal and serves to block IL-1β signaling. IL-1β plays critical roles in the acute phase response and sepsis (1-3).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Dog, Human

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

Background: Tight junctions, or zonula 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. Tight junctions are composed of claudin and occludin proteins, which join the junctions to the cytoskeleton (1,2). The claudin family is composed of 23 integral membrane proteins, and their expression, which varies among tissue types, may determine both the strength and properties of the epithelial barrier. Alteration in claudin protein expression pattern is associated with several types of cancer (2,3). Claudin-1 is expressed primarily in keratinocytes (4) and normal mammary epithelial cells, but is absent or reduced in breast carcinomas and breast cancer cell lines (5,6).

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

Application Methods: Western Blotting

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

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

Application Methods: Western Blotting

Background: AMP-activated protein kinase (AMPK) is highly conserved from yeast to plants and animals and plays a key role in the regulation of energy homeostasis (1). AMPK is a heterotrimeric complex composed of a catalytic α subunit and regulatory β and γ subunits, each of which is encoded by two or three distinct genes (α1, 2; β1, 2; γ1, 2, 3) (2). The kinase is activated by an elevated AMP/ATP ratio due to cellular and environmental stress, such as heat shock, hypoxia, and ischemia (1). The tumor suppressor LKB1, in association with accessory proteins STRAD and MO25, phosphorylates AMPKα at Thr172 in the activation loop, and this phosphorylation is required for AMPK activation (3-5). AMPKα is also phosphorylated at Thr258 and Ser485 (for α1; Ser491 for α2). The upstream kinase and the biological significance of these phosphorylation events have yet to be elucidated (6). The β1 subunit is post-translationally modified by myristoylation and multi-site phosphorylation including Ser24/25, Ser96, Ser101, Ser108, and Ser182 (6,7). Phosphorylation at Ser108 of the β1 subunit seems to be required for the activation of AMPK enzyme, while phosphorylation at Ser24/25 and Ser182 affects AMPK localization (7). Several mutations in AMPKγ subunits have been identified, most of which are located in the putative AMP/ATP binding sites (CBS or Bateman domains). Mutations at these sites lead to reduction of AMPK activity and cause glycogen accumulation in heart or skeletal muscle (1,2). Accumulating evidence indicates that AMPK not only regulates the metabolism of fatty acids and glycogen, but also modulates protein synthesis and cell growth through EF2 and TSC2/mTOR pathways, as well as blood flow via eNOS/nNOS (1).