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Product listing: Golgin-97 (CDF4) Mouse mAb, UniProt ID Q92805 #97537 to PathScan® Phospho-S6 Ribosomal Protein (Ser235/236) Sandwich ELISA Kit, UniProt ID P62753 #7205

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The Golgi-associated protein golgin A1 (GOLGA1, golgin-97) was first isolated as a Golgi complex autoantigen associated with the autoimmune disorder Sjogren's syndrome (1). The golgin-97 protein contains a carboxy-terminal GRIP domain and is a commonly used trans-Golgi network (TGN) marker. All four known mammalian GRIP domain-containing proteins (golgin-97, golgin-245, GCC88 and GCC185) are found in the TGN, share extensive alpha-helical structure, and form homodimers (2). While all four golgin proteins localize to the TGN, they exhibit different membrane-binding abilities and are found in distinct TGN regions (3). Golgin-97 and golgin-245 are targeted to the trans-Golgi network through an interaction between their GRIP domains and the Arl1 protein switch II region (4). Overexpression studies and siRNA assays with GRIP domain-containing proteins suggest that these proteins help to maintain trans-Golgi network integrity and function by controlling localization of TGN resident proteins (5). By using a Shiga toxin B fragment (STxB)-based in vitro transport assay and an E-cadherin transport model system, golgin-97 and its effector Arl1-GTP were shown to play a role in trans-Golgi endosomal trafficking (6,7). Research studies also suggest that golgin-97 may play a role in poxvirus morphogenesis and maturation (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Tyk2 is a member of the Jak family of protein tyrosine kinases. It associates with and is activated by receptors for many cytokines including IL-13, the IL-6 family, IL-10, and IFN-α and β (1-3). Following ligand binding, Tyk2 is activated by phosphorylation of Tyr1054 and/or Tyr1055 (4). Tyk2 is required for the tyrosine phosphorylation of Stat3 in the IFN-β signaling cascade (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: 4F2hc is a transmembrane protein that belongs to the solute carrier family. 4F2hc forms heterodimeric complexes with various amino acid transporters such as LAT1 and LAT2 and regulates uptake of amino acids (1-5). 4F2hc is one of the earliest expressed antigens on the surface of activated human lymphocytes (6), hence it is also named CD98. 4F2hc is expressed in all cell types with the exception of platelets, and is expressed at highest levels in the tubules of the kidney and the gastrointestinal tract (7,8). It is localized at the plasma membrane when associated with LAT1 or LAT2 (9) and at the apical membrane of placenta (10). Research studies have shown that 4F2hc is highly expressed in various tumors including glioma (11), ovarian cancer (12), and astrocytomas (13), and it has been implicated in tumor progression and correlated with poor outcome in patients with pulmonary neuroendocrine tumors (14). 4F2hc is also involved in integrin trafficking through association with β1 and β4 integrins, and regulates keratinocyte adhesion and differentiation (15).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Cystathionine beta-synthase (CBS) is a key enzyme involved in sulfur amino acid metabolism because it catalyzes the formation of cystathionine from serine and homocysteine (1,2). The CBS protein contains a heme-binding domain that modulates enzyme activity by sensing redox changes or carbon monoxide binding (1). S-adenosylmethionine binds the carboxyl-terminal CBS domain to allosterically regulate CBS catalytic activity (3,4). In addition to catalyzing cystathionine formation, CBS also catalyzes the generation of hydrogen sulfide, a neuromodulator in the brain, through alternative reactions (5,6). Mutations in the corresponding CBS gene result in homocystinuria, an autosomal recessive disorder characterized by abnormal sulfur metabolism, mental retardation, eye anomalies, and vascular disease (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: BCL11A is a zinc finger-containing transcriptional repressor that is important for normal hematopoiesis (1). Alternative splicing of the BCL11A transcript results in several isoforms of the protein (2). BCL11A is required for the early stages of B lineage commitment and mice lacking BCL11A fail to develop B cells (1). Mice deficient in BCL11A also fail to develop plasmacytoid dendritic cells (3). In addition, BCL11A regulates the switch from fetal to adult hemoglobin by repressing expression of fetal hemoglobin in adult erythroid cells (4). Since expression of fetal hemoglobin can decrease the severity of hemoglobin disorders in adults, BCL11A is a potential therapeutic target for these diseases (4). BCL11A was also recently identified as a component of the mammalian SWI/SNF complex (5). BCL11A is required for morphogenesis and terminal differentiation of dorsal spinal neurons (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: TRAFs (TNF receptor-associated factors) are a family of multifunctional adaptor proteins that bind to surface receptors and recruit additional proteins to form multiprotein signaling complexes capable of promoting cellular responses (1-3). Members of the TRAF family share a common carboxy-terminal "TRAF domain", which mediates interactions with associated proteins; many also contain amino-terminal Zinc/RING finger motifs. The first TRAFs identified, TRAF1 and TRAF2, were found by virtue of their interactions with the cytoplasmic domain of TNF-receptor 2 (TNFRII) (4). The six known TRAFs (TRAF1-6) act as adaptor proteins for a wide range of cell surface receptors and participate in the regulation of cell survival, proliferation, differentiation, and stress responses.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Neural precursor expressed, developmentally down-regulated protein 4 (NEDD4) was originally identified as a gene that is highly expressed in the early mouse embryonic central nervous system (1). Subsequently, a family of NEDD4-like proteins have been defined that includes seven members in humans (2). NEDD4 and NEDD4-like (NEDD4L) proteins contain multiple functional domains including a calcium-dependent phospholipid and membrane binding domain (C2 domain), two to four protein binding domains (WW domains), and an E3 ubiquitin-protein ligase domain (HECT domain). NEDD4 and NEDD4L have been shown to downregulate both neuronal voltage-gated Na+ channels (NaVs) and epithelial Na+ channels (ENaCs) in response to increased intracellular Na+ concentrations (3,4). The WW domains of NEDD4 bind to PY motifs (amino acid sequence PPXY) found in multiple NaV and ENaC proteins; ubiquitination of these proteins is mediated by the HECT domain of NEDD4 and results in their internalization and removal from the plasma membrane. Research studies have shown that mutation of the PY motifs in ENaC proteins is associated with Liddle's syndrome, an autosomal dominant form of hypertension (5). In addition to targeting sodium channels, NEDD4L has also been shown to negatively regulate TGF-β signaling by targeting Smad2 for degradation (6). Mouse and human NEDD4 are rapidly cleaved by caspase proteins during apoptosis, although the significance of this cleavage is not clear (7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Carcinoembryonic antigen (CEA), also known as CD66e or CEACAM5, is a 180-200 kDa cell surface glycoprotein whose expression is elevated in intestinal carcinomas and other tumors. CEA mediates cell adhesion, though little more is known about its biological activity. Expression of CEA is correlated with tumerogenicity (1), and it has been shown to play a role in cell migration, adhesion and invasion in culture cells, as well as in metastasis in vivo (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Metabotropic glutamate receptor 1 (mGluR1) is a G protein-coupled receptor (GPCR) for the neurotransmitter glutamate in the mammalian brain. Unlike ionotropic receptors, metabotropic receptors do not form an ion channel pore themselves but are indirectly linked to ion channels (1). Both mGluR1 and mGluR5 are coupled to phospholipase C and activate inositol phospholipid metabolism via G protein-mediated mechanisms. Upon phosphatidylinositol activation, the second messenger calcium is released and generates a calcium-activated chloride current. Metabotropic glutamate receptors other than mGluR1 and mGluR5 inhibit adenylate cyclase (1-3). mGluR1 does not share sequence homology with conventional GPCRs (1). mGluR1 forms a homodimer and is linked to synaptic plasticity, as well as long-term potentiation and long-term depression. Furthermore, mGluR1 is a potential therapeutic target for various psychiatric and neurological diseases, including schizophrenia, epilepsy, and Parkinson and Alzheimer diseases (4-6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Survivin is a 16 kDa anti-apoptotic protein highly expressed during fetal development and cancer cell malignancy (1). Survivin binds and inhibits caspase-3, controlling the checkpoint in the G2/M-phase of the cell cycle by inhibiting apoptosis and promoting cell division (2,3). This regulatory process requires the phosphorylation of survivin at Thr34 by p34 cdc2 kinase (4). Gene targeting using a Thr34 phosphorylation-defective survivin mutant, as well as antisense survivin, have been shown to inhibit tumor growth (5,6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: RNA polymerase II (RNAPII) is a large multi-protein complex that functions as a DNA-dependent RNA polymerase, catalyzing the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (1). The largest subunit, RNAPII subunit B1 (Rpb1), also known as RNAPII subunit A (POLR2A), contains a unique heptapeptide sequence (Tyr1,Ser2,Pro3,Thr4,Ser5,Pro6,Ser7), which is repeated up to 52 times in the carboxy-terminal domain (CTD) of the protein (1). This CTD heptapeptide repeat is subject to multiple post-translational modifications, which dictate the functional state of the polymerase complex. Phosphorylation of the CTD during the active transcription cycle integrates transcription with chromatin remodeling and nascent RNA processing by regulating the recruitment of chromatin modifying enzymes and RNA processing proteins to the transcribed gene (1). During transcription initiation, RNAPII contains a hypophosphorylated CTD and is recruited to gene promoters through interactions with DNA-bound transcription factors and the Mediator complex (1). The escape of RNAPII from gene promoters requires phosphorylation at Ser5 by CDK7, the catalytic subunit of transcription factor IIH (TFIIH) (2). Phosphorylation at Ser5 mediates the recruitment of RNA capping enzymes, in addition to histone H3 Lys4 methyltransferases, which function to regulate transcription initiation and chromatin structure (3,4). After promoter escape, RNAPII proceeds down the gene to an intrinsic pause site, where it is halted by the negative elongation factors NELF and DSIF (5). At this point, RNAPII is unstable and frequently aborts transcription and dissociates from the gene. Productive transcription elongation requires phosphorylation at Ser2 by CDK9, the catalytic subunit of the positive transcription elongation factor P-TEFb (6). Phosphorylation at Ser2 creates a stable transcription elongation complex and facilitates recruitment of RNA splicing and polyadenylation factors, in addition to histone H3 Lys36 methyltransferases, which function to promote elongation-compatible chromatin (7,8). Ser2/Ser5-phosphorylated RNAPII then transcribes the entire length of the gene to the 3' end, where transcription is terminated. RNAPII dissociates from the DNA and is recycled to the hypophosphorylated form by various CTD phosphatases (1).In addition to Ser2/Ser5 phosphorylation, Ser7 of the CTD heptapeptide repeat is also phosphorylated during the active transcription cycle. Phosphorylation at Ser7 is required for efficient transcription of small nuclear (sn) RNA genes (9,10). snRNA genes, which are neither spliced nor poly-adenylated, are structurally different from protein-coding genes. Instead of a poly(A) signal found in protein-coding RNAs, snRNAs contain a conserved 3'-box RNA processing element, which is recognized by the Integrator snRNA 3' end processing complex (11,12). Phosphorylation at Ser7 by CDK7 during the early stages of transcription facilitates recruitment of RPAP2, which dephosphorylates Ser5, creating a dual Ser2/Ser7 phosphorylation mark that facilitates recruitment of the Integrator complex and efficient processing of nascent snRNA transcripts (13-15).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Ribosomal protein L7a is a highly conserved ribosome protein localized to 60S ribosomal subunit (1). The protein has distinct domains that target the newly synthesized polypeptide to nucleus and the nucleoli, the site of ribosome biosynthesis (2). Ribosomal protein L7a can also interact with RNA in vitro through two distinct RNA-binding domains in the protein (3). Taken together, nucleolar localization and the ability to bind RNA suggests that ribosomal protein L7a may act as an important component for ribosome biosynthesis and function.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Paxillin is a multidomain protein that localizes primarily to focal adhesion sites in the extracellular matrix (1). Paxillin is one of the key components of integrin signaling, and tyrosine phosphorylation of paxillin is required for integrin-mediated cytoskeletal reorganization (2). Paxillin is phosphorylated by another focal adhesion component, focal adhesion kinase (FAK), at Tyr118 (3,4). Phospho-Paxillin (Tyr118) may provide a docking site for recruitment of other signaling molecules to focal adhesions. It has been shown that the SH2 domain of Crk binds to the phosphorylated Tyr118 of paxillin (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: The IL-17 family of cytokines consists of IL-17A-F, and their receptors include IL-17RA-RE (1). IL-17 cytokines are produced by a variety of cell types including the Th17 subset of CD4+ T cells, as well as subsets of γδ T cells, NK cells, and NKT cells (2). IL-17A and IL-17F, the most well-studied of the IL-17 cytokines, contribute to fungal and bacterial immunity by inducing expression of proinflammatory cytokines, chemokines, and antimicrobial peptides (2). In addition, IL-17A contributes to the pathogenesis of several autoimmune diseases (3). IL-17E promotes Th2 cell responses (4). The roles of IL-17B, IL-17C, and IL-17D are less clear, however these family members also appear to have the capacity to induce proinflammatory cytokines (1,5,6). IL-17 receptors have an extracellular domain, a transmembrane domain, and a SEFIR domain. They are believed to signal as homodimers, heterodimers, or multimers through their SEFIR domain by recruiting the SEFIR domain-containing adaptor Act1 (7). Unlike most cytokines that signal through Jak/STAT pathways, IL-17 signaling results in NF-κB activation (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry, Western Blotting

Background: The type I interferon (IFN) family includes IFN-β1 and IFN-α1 through IFN-α13 in humans and IFN-α1 through IFN-α14 in mice. Type I IFN is produced following detection of pathogen-associated molecular patterns (PAMPs) and is important for induction of antiviral genes, activation of dendritic cells, and initiation of adaptive immunity (1, 2). Type I IFNs signal through the IFN alpha receptor (IFNAR), which is a heterodimer composed of IFNAR1 and IFNAR2. Activation of IFNAR leads to formation of the nuclear complex IFN-stimulated gene factor 3 (ISGF3), which consists of STAT1, STAT2, and IRF-9 (3, 4). ISGF3 binds to IFN-stimulated response elements (ISREs) to initiate transcription of interferon-stimulated genes (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Ubiquitinating enzymes (UBEs) catalyze protein ubiquitination, a reversible process countered by deubiquitinating enzyme (DUB) action (1,2). Five DUB subfamilies are recognized, including the USP, UCH, OTU, MJD, and JAMM enzymes. In humans, there are three proteasomal DUBs: PSMD14 (POH1/RPN11), UCH37 (UCH-L5), and Ubiquitin-Specific Protease 14, which is also known as the 60 kDa subunit of tRNA-guanine transglycosylase (USP14/TGT60 kDa). USP14 is recruited to the proteasome through its reversible association with the PSMD2 (S2/hRPN1) subunit of the 19S regulatory particle. Whereas PSMD14 appears to promote substrate degradation (3,4), USP14 is thought to antagonize substrate degradation (5-8). While the underlying mechanism for the opposing roles of these two proteasomal DUBs is still uncertain, it is thought that USP14 removes ubiquitin from substrate upon docking of the substrate with the 26S proteasome. Furthermore, USP14 trims ubiquitin residues from the distal end of the polyubiquitin chain, thus decreasing the affinity of the chain for the ubiquitin receptors of the proteasome, and allowing for enhanced substrate stability (6,9,10). Studies have elucidated a physiologic role for USP14 in regulating synaptic activity in mammals (11). Research studies have shown that targeting this activity with small molecule inhibitors has potential benefits for the treatment of neurodegenerative diseases and cancer (5,12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Ectonucleotide pyrophosphatase-phosphodiesterase 1 (ENPP1) is a single-pass, type II transmembrane protein primarily involved in ATP hydrolysis at the plasma membrane. Targeting of ENPP1 to the basolateral cell surface relies on the presence of a carboxy-terminal di-leucine-based signal (1). ENPP1 plays important roles in bone mineralization and soft tissue calcification (2-5). Mutations in the corresponding ENPP1 gene cause generalized arterial calcification in infancy (GACI) and idiopathic infantile arterial calcification (IIAC) (6,7). ENPP1 inhibits insulin receptor function and overexpression of this enzyme causes insulin resistance and glucose intolerance in mice (8,9). Genetic variants of ENPP1 have been associated with obesity and type 2 diabetes (10-12).

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

Application Methods: Western Blotting

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

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

Application Methods: Western Blotting

Background: A variety of factors contribute to the important biological event of initiation of translation. The eIF4F complex of translation initiation factors binds to the 5' m7 GTP cap to open up the mRNA secondary structure and allow small ribosome subunit binding (1). eIF4A, an eIF4 complex component that acts as an ATP-dependent RNA helicase, unwinds the secondary structure of the 5' mRNA untranslated region to mediate ribosome binding (2,3). In addition, eIF4A has recently been shown to repress Dpp/BMP signalling in a translation-independent manner in Drosophila (4,5).

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

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

Background: Pyruvate kinase is a glycolytic enzyme that catalyses the conversion of phosphoenolpyruvate to pyruvate. In mammals, the M1 isoform (PKM1) is expressed in most adult tissues (1). The M2 isoform (PKM2) is an alternatively spliced variant of M1 that is expressed during embryonic development (1). Research studies found that cancer cells exclusively express PKM2 (1-3). PKM2 is shown to be essential for aerobic glycolysis in tumors, known as the Warburg effect (1). When cancer cells switch from the M2 isoform to the M1 isoform, aerobic glycolysis is reduced and oxidative phosphorylation is increased (1). These cells also show decreased tumorigenicity in mouse xenografts (1). Recent studies showed that PKM2 is not essential for all tumor cells (4). In the tumor model studied, PKM2 was found to be active in the non-proliferative tumor cell population and inactive in the proliferative tumor cell population (4).

$115
5.19 mg
Molecular Weight:519.28 g/mol
APPLICATIONS

Application Methods: Western Blotting

Background: H-89 is a potent selective inhibitor of cAMP dependent protein kinase (PKA). The in vitro IC50 of H-89 for PKA is approximately 50 nM and in vivo the inhibitiory effect on PKA substrate phosphorylation and related cellular functions range from 10 μM to 30 μM (1,2). In addition to PKA, H-89 also exhibits a moderate inhibitory effect on PKG and PKCμ, with IC50 in the 500 nM range (1,3). The inhibitory effect of H-89 is due to its competitive binding to the ATP pocket on the kinase catalytic subunit (4).

Molecular Weight:853.92 g/mol

Background: Paclitaxel belongs to the taxane family of antitumor and antileukemic agents (3). By binding to β-tubulin and promoting the assembly of microtubules, paclitaxel prevents microtubual depolymerization and blocks normal cell division (1-3). The microtubule dysfunction induced by paclitaxel results in aberrant cell mitosis and sometimes apoptosis. The IC50 of paclitaxel-induced mitotic block is 4 nM (4).

The Pro-Survival Bcl-2 Family Antibody Sampler Kit II provides an economical means to examine several members of the Bcl-2 family. The kit contains enough primary antibody to perform two western blot experiments.

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.

$489
96 assays
1 Kit
The PathScan® Phospho-S6 Ribosomal Protein (Ser235/236) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of phospho-S6 ribosomal protein (Ser235/236). A Phospho-S6 Ribosomal Protein (Ser235/236) Antibody has been coated onto the microwells. After incubation with cell lysates, only phospho-S6 ribosomal protein is captured by the coated antibody. Following extensive washing, a Total S6 Ribosomal Protein Mouse mAb is added to detect the captured phospho-S6 ribosomal protein (Ser235/236). Anti-Mouse IgG, HRP-linked Antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of phospho-S6 ribosomal protein (Ser235/236).Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse

Background: One way that growth factors and mitogens effectively promote sustained cell growth and proliferation is by upregulating mRNA translation (1,2). Growth factors and mitogens induce the activation of p70 S6 kinase and the subsequent phosphorylation of the S6 ribosomal protein. Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions (2). These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation (2,3). Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy-terminal region of the S6 protein (4,5).