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Product listing: PEX5 (D7V4D) Rabbit mAb, UniProt ID P50542 #83020 to EGF Receptor (D38B1) XP® Rabbit mAb (Biotinylated), UniProt ID P00533 #6627

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Peroxin-5 (PEX5) is the shuttle receptor that delivers proteins to peroxisomes (1). In the cytosol, PEX5 binds to the peroxisomal targeting signal 1 (PTS1), a short peptide sequence present at the extreme C termini of newly synthesized peroxisomal matrix proteins. The PEX5-cargo complex interacts with the peroxisomal docking/translocation machinery on the peroxisomal membrane, where the cargo is released into the organelle matrix. During this process, PEX5 is monoubiquitinated at a conserved cysteine residue, and the ubiquitin-PEX5 conjugate is released from the organelle into the cytosol, where PEX5 is deubiquitinated and ready the next round of targeting (2,3).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Etk, also known as BMX, is a member of the Bruton's tyrosine kinase (Btk) family (1). It is expressed in a variety of hematopoietic, epithelial and endothelial cells. Etk, like other Btk family members, contains a pleckstrin homology (PH) domain and Src homology SH3 and SH2 domains. It participates in multiple signal transduction pathways (2). Phosphorylation of Tyr566 by Src kinase is required for activation of Etk in vivo (3). In endothelial and epithelial cells, Etk is regulated by FAK through phosphorylation at Tyr40 (4).

$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).

$489
96 assays
1 Kit
The PathScan® Total PTEN Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenously expressed PTEN. A PTEN rabbit antibody has been coated onto the microwells. After incubation with cell lysates, PTEN is captured by the coated antibody. Following extensive washing, a PTEN mouse detection antibody is added to detect the captured PTEN. 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 the absorbance for this developed color is proportional to the quantity of PTEN.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Monkey, Mouse, Rat

Background: PTEN (phosphatase and tensin homologue deleted on chromosome ten), also referred to as MMAC (mutated in multiple advanced cancers) phosphatase, is a tumor suppressor implicated in a wide variety of human cancers (1). PTEN encodes a 403 amino acid polypeptide originally described as a dual-specificity protein phosphatase (2). The main substrates of PTEN are inositol phospholipids generated by the activation of the phosphoinositide 3-kinase (PI3K) (3). PTEN is a major negative regulator of the PI3K/Akt signaling pathway (1,4,5). PTEN possesses a carboxy-terminal, noncatalytic regulatory domain with three phosphorylation sites (Ser380, Thr382, and Thr383) that regulate PTEN stability and may affect its biological activity (6,7). PTEN regulates p53 protein levels and activity (8) and is involved in G protein-coupled signaling during chemotaxis (9,10).

$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).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct flow cytometric and immunofluorescent analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated COX IV (3E11) Rabbit mAb #4850.
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Pig, Rat, Zebrafish

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Cytochrome c oxidase (COX) is a hetero-oligomeric enzyme consisting of 13 subunits localized to the inner mitochondrial membrane (1-3). It is the terminal enzyme complex in the respiratory chain, catalyzing the reduction of molecular oxygen to water coupled to the translocation of protons across the mitochondrial inner membrane to drive ATP synthesis. The 3 largest subunits forming the catalytic core are encoded by mitochondrial DNA, while the other smaller subunits, including COX IV, are nuclear-encoded. Research studies have shown that deficiency in COX activity correlates with a number of human diseases (4). The COX IV antibody can be used effectively as a mitochondrial loading control in cell-based research assays.

$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).

$303
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Immunoprecipitation, 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, 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).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: MKK3 and MKK6 are two closely related dual-specificity protein kinases that activate p38 MAP kinase (1-5). MKK3 and MKK6 both phosphorylate and activate p38 MAP kinase at its activation site, Thr-Gly-Tyr, but do not phosphorylate or activate Erk1/2 or SAPK/JNK. Phosphorylation of p38 MAP kinase dramatically stimulates its ability to phosphorylate protein substrates such as ATF-2 and Elk-1. MKK3 and MKK6 are both activated by different forms of cellular stress and inflammatory cytokines (4,5). Activation of MKK3 and MKK6 occurs through phosphorylation at Ser189 and Thr222 on MKK3 (2) and Ser207 and Thr211 on MKK6 (4,5).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated His-Tag (D3I1O) XP® Rabbit mAb #12698.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: 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, 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).

$348
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 Ezh2 (D2C9) XP® Rabbit mAb #5246.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: The polycomb group (PcG) proteins are involved in maintaining the silenced state of several developmentally regulated genes and contribute to the maintenance of cell identity, cell cycle regulation, and oncogenesis (1,2). Enhancer of zeste homolog 2 (Ezh2), a member of this large protein family, contains four conserved regions including domain I, domain II, and a cysteine-rich amino acid stretch that precedes the carboxy-terminal SET domain (3). The SET domain has been linked with histone methyltransferase (HMTase) activity. Moreover, mammalian Ezh2 is a member of a histone deacetylase complex that functions in gene silencing, acting at the level of chromatin structure (4). Ezh2 complexes methylate histone H3 at Lys9 and 27 in vitro, which is thought to be involved in targeting transcriptional regulators to specific loci (5). Ezh2 is deregulated in various tumor types, and its role, both as a primary effector and as a mediator of tumorigenesis, has become a subject of increased interest (6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Class II phosphatidylinositol 3-kinases (PI3K) contain a C-terminal C2 domain that is unique to the class II isoforms of the PI3K family. This C2 domain mediates protein and phospholipid binding acitivities (1,2). PI3K Class II α generates phosphatidylinositol 3-phosphate (PIP3) and phosphatidylinositol 3,4-bisphosphate (PI(3, 4)P2) from phosphatidylinositol and phosphatidylinositol 4-phosphate (3). PI3K Class II α is located in various intracellular locations such as the trans-Golgi network, endocytic compartments, clathrin-coated vesicles, and nuclear speckles (1,4,5). Research studies have indicated that PI3K Class II α regulates the assembly and distribution of clathrin, resulting in the modulation of clathrin-dependent trafficking and sorting within the trans Golgi network (5,6). PI3K Class II α also mediates translocation of the glucose transporter GLUT4 to the plasma membrane in response to insulin (7). PI3K Class II α has also been shown to regulate neurosecretory granule exocytosis (8) and vascular smooth muscle contraction (9). Unlike other PI3K family members, PI3K Class II α is less sensitive to the PI3K inhibitors wortmannin and LY294002 (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Nicotinamide mononucleotide adenylyl transferases (NMNATs) catalyze the reversible reaction of ATP with NaMN (nicotinic acid mononucleotide) or NMN (nicotinamide mononucleotide) to produce NaAD (nicotinic acid adenine dinucleotide) or NAD (nicotinamide adenine dinucleotide). NAD is an essential cofactor or substrates for many enzymes like PARP1 and Sirt1 that regulate diverse cellular processes including oxidative reactions and transcription. NMNATs maintain NAD levels for internal homeostasis (1,2). NMNAT1 is localized to the nucleus and loss-of-function mutant in mice causes embryonic lethality (3). In humans, several different NMNAT1 mutations are associated with Leber congenital amaurosis (LCA), the most common cause of inherited childhood blindness (4-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: MHC class II (MHC-II) proteins play critical roles in cellular immune responses and their expression is mainly regulated by the non-DNA binding transcription factor CIITA (MHC class II transactivator) (1,2). CIITA expression is upregulated by IFN-γ and it in turn enchances MHC-II expression and represses collagen expression (3,4). CIITA has a limited number of transcriptional targets, most of which are involved in MHC-mediated antigen presentation (5). Mutations in the CIITA are associated with the hereditary immunodeficiency disease Bare Lymphocyte Syndrome (BLS) which is characterized by a nearly complete absence of MHC-II expression (also referred to as MHC-II deficiency) (6,7).

$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).

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

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

Background: Cytoplasmic dynein is a multi-subunit motor complex that regulates microtubule organization as well as the transport and positioning of organelles. Dynactin is a multi-subunit dynein-activating complex, which regulates the interaction of the dynein motor with various cellular cargoes, and enhances dynein’s processivity. p150Glued/DCTN1/Dynactin 1 is the largest subunit of the dynactin complex (1-3). In mitosis, cytoplasmic dynein regulates spindle organization, chromosome movement and centrosome separation (4). The dynactin subunit p150Glued is phosphorylated at serine 19 by the mitotic kinase aurora A during anaphase, and this phosphorylation is required for the appropriate regulation of spindle assembly (5). In neurons, axonal transport is important for cellular function and survival. Dysfunction and mutations in dynein and dynactin subunits, including p150Glued, have been linked to human neurodegenerative diseases such as Alzheimer’s Disease (6-7), Perry Syndrome (8) and ALS (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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The Bcr gene was orginally identified by its presence in the chimeric Bcr-Abl oncogene (1). The amino-terminal region of Bcr contains an oligomerization domain, a serine/threonine kinase domain, and a region that binds SH2 domains. The middle of the protein has a PH domain and a region of sequence similarity to the guanine nucleotide exchange factors for the Rho family of GTP binding proteins. The carboxy-terminal region may be involved in a GTPase activating function for the small GTP-binding protein Rac (2,3). The function of wild type Bcr in cells remains unclear. PDGF receptor may use Bcr as a downstream signaling mediator (4). Research studies have shown that the Bcr-Abl fusion results in production of a constitutively active tyrosine kinase, which causes chronic myelogenous leukemia (CML) (5). Tyr177 of Bcr is phosphorylated in the Bcr-Abl fusion protein, which plays an important role in transforming the activity of Bcr-Abl (6). Phosphorylated Tyr177 provides a docking site for Gab2 and GRB2 (7,8).

$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Ras activity is regulated by GAP (GTPase activating proteins) and GEFs (guanine nucleotide exchange factors). Ras-GRF1 (also known as CDC25Mm) is neuronal RasGEF and is regulated by heterotrimeric G proteins and calcium influx (1,2). Binding to calmodulin and phosphorylation stimulate Ras-GRF1 activity (1,2). Multiple PKA phosphorylation sites on Ras-GRF have been identified. Phosphorylation on the two major sites, Ser54 and Ser822, inhibits Ras-GRF activity (3). Carbachol (a muscarinic agonist)-induced phosphorylation on Ser916 is essential but not sufficient for maximal Ras-GRF activity (4). It has been reported that Ras-GRF1 also shows GEF activity toward Rac after phosphorylation by the tyrosine kinase Src (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

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.

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Chromatin assembly factor 1 (CAF-1) is a histone H3/H4 chaperone complex that functions in de novo assembly of nucleosomes during DNA replication and nucleotide excision repair (1). Nucleosome assembly is a two-step process, involving initial deposition of a histone H3/H4 tetramer onto DNA, followed by the deposition of a pair of histone H2A/H2B dimers (1). CAF-1 interacts with PCNA and localizes to DNA replication and DNA repair foci, where it functions to assemble newly synthesized histone H3/H4 tetramers onto replicating DNA (2-6). Assembly of histone H2A/H2B dimers requires additional assembly factors. The CAF-1 complex consists of three proteins: CHAF1A (p150), CHAF1B (p60) and RBAP48 (p48 or RBBP4). CHAF1A and CHAF1B proteins are specific for the CAF-1 complex, while RBAP48 is a component of multiple chromatin modifying complexes (1). CHAF1A and CHAF1B expression levels correlate with cellular proliferation and both proteins are significantly down-regulated in quiescent cells (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

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

$348
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as unconjugated EGF Receptor (D38B1) XP® Rabbit mAb #4267.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

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).