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Product listing: SIRPα/SHPS1 (D6I3M) Rabbit mAb, UniProt ID P78324 #13379 to SAV1 (D6M6X) Rabbit mAb, UniProt ID Q9H4B6 #13301

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

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

Background: SHP-substrate 1 (SHPS1, SIRPα) is a single-pass membrane protein and member of both the immunoglobulin superfamily and the signal regulatory protein (SIRP) family. Following growth hormone stimulation or integrin binding, SHPS1 is phosphorylated at several tyrosine residues within its cytoplasmic tail. These phosphorylation events promote association between SHPS1 and multiple signaling proteins, including SHP-1, SHP-2, Grb2 and Shc via their SH2 domains (1-4). Recruitment of SHP-1 and SHP-2 results in SHPS1 dephosphorylation and suppression of tyrosine kinase signaling (1-3,5). The tyrosine kinase JAK2 associates with SHPS1 via its carboxy terminus and phosphorylates SHPS1 in response to extracellular stimuli (5). Research studies show that Src associates with and may phosphorylate SHPS1 in response to insulin (4). In macrophages, SHPS1 can form a complex with the Src pathway adaptor protein SKAP2, Fyn-binding protein FYB, and the tyrosine kinase PYK2 (6). The SHPS1 extracellular domain contains at least three IgG-like domains that interact with CD47, a ubiquitously expressed, integrin-associated protein that acts as a repressive cue in both immune and neuronal cells (7,8). The interaction between CD47 and SHPS1 on opposing cells can inhibit cellular migration (9), promote "tethering" between macrophages and target cells during engulfment (10), facilitate self versus non-self recognition (11), and maintain immune homeostasis (12). SHPS1 plays a critical role in modulating the immune response and inflammation, and may play a role in neuronal development (13,14). The interaction between SHPS1 and CD47 may be an exploitable target in cancer therapy (15-17).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

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

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: TNF-α is an important cytokine produced by numerous cell types including neutrophils, activated lymphoctyes, macrophages and NK cells. It plays a critical role in inflammatory responses and in apoptosis (1). TNF-α exists as a membrane-anchored and soluble form, both of which show biological activity. Response to TNF-α is mediated through two receptors, TNF-R1, which is widely expressed, and TNF-R2, which is expressed mainly in immune and endothelial cells (2). Antagonists to TNF-α have been validated as therapeutic targets for rheumatoid arthritis and other immune disorders (3).

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

Application Methods: Western Blotting

Background: Transcription initiation factor IIE subunit alpha (TFIIE-α) is part of TFIIE, a general transcription factor made up of paired α and β subunits. These general transcription factors include TFIIA, TFIIB, TFIID, TFIIE, TFIIF, and TFIIH (1-4). Binding of RNA polymerase II (RNAPII) to promoter sequences as part of the pre-initiation complex (PIC) is facilitated by these general transcription factors. These factors also help in selection of the proper transcription start site, DNA unwinding, and RNAPII promoter escape during transcription (1). During the transition from transcription initiation to elongation, TFIIE stimulates the TFIIH kinase and DNA helicase activities, responsible for phosphorylation of the carboxy-terminal domain of the largest RNAPII subunit (POL2RA) and unwinding of promoter DNA for RNAPII promoter escape (1,5-9).

$262
3 nmol
300 µl
SignalSilence® TNF-R1 siRNA I (Mouse Specific) from Cell Signaling Technology (CST) allows the researcher to specifically inhibit TNF-R1 expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Mouse

Background: TNF-α is an important cytokine produced by numerous cell types including neutrophils, activated lymphoctyes, macrophages and NK cells. It plays a critical role in inflammatory responses and in apoptosis (1). TNF-α exists as a membrane-anchored and soluble form, both of which show biological activity. Response to TNF-α is mediated through two receptors, TNF-R1, which is widely expressed, and TNF-R2, which is expressed mainly in immune and endothelial cells (2). Antagonists to TNF-α have been validated as therapeutic targets for rheumatoid arthritis and other immune disorders (3).

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

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

Background: Fatty acid binding proteins (FABPs) bind to fatty acids and other lipids to function as cytoplasmic lipid chaperones (1,2). They participate in the transport of fatty acids and other lipids to various cellular pathways (2). Research studies have shown that common variants of the human liver fatty acid binding protein gene FABP1 play a role in the development of type 2 diabetes and insulin resistance (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Apolipoproteins are plasma lipoproteins that function as transporters of lipids and cholesterol in the circulatory system. Chylomicrons are a fundamental class of apolipoproteins containing very low-density lipoproteins (VLDL), intermediate-density lipoproteins (IDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) (1,2).

$262
3 nmol
300 µl
SignalSilence® PI3 Kinase p110β siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit PI3 Kinase p110β expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All CST™ SignalSilence® siRNA products are rigorously tested in-house and have been shown to reduce protein expression by western analysis.
REACTIVITY
Human

Background: Phosphoinositide 3-kinase (PI3K) catalyzes the production of phosphatidylinositol-3,4,5-triphosphate by phosphorylating phosphatidylinositol (PI), phosphatidylinositol-4-phosphate (PIP), and phosphatidylinositol-4,5-bisphosphate (PIP2). Growth factors and hormones trigger this phosphorylation event, which in turn coordinates cell growth, cell cycle entry, cell migration, and cell survival (1). PTEN reverses this process, and research studies have shown that the PI3K signaling pathway is constitutively activated in human cancers that have loss of function of PTEN (2). PI3Ks are composed of a catalytic subunit (p110) and a regulatory subunit. Various isoforms of the catalytic subunit (p110α, p110β, p110γ, and p110δ) have been isolated, and the regulatory subunits that associate with p110α, p110β, and p110δ are p85α and p85β (3). In contrast, p110γ associates with a p101 regulatory subunit that is unrelated to p85. Furthermore, p110γ is activated by βγ subunits of heterotrimeric G proteins (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Chloride channel 3 (CLCN3) is a voltage-gated chloride channel (CIC) family protein that mediates H+/Cl- exchange across cell membranes. This 818 amino acid, multi-pass membrane protein is highly expressed in the brain and is especially abundant in the olfactory bulb, hippocampus, and cerebellum (1). CLCN3 protein localizes to endosomal compartments and synaptic vesicles where it contributes to vesicle acidification and proper synaptic vesicle neurotransmitter loading for GABAergic synaptic transmission (2,3). CAMKII-mediated phosphorylation of CLCN3 regulates chloride channel activity by regulating cell surface targeting of the CLCN3 chloride channel (4). Research studies show abnormally high CLCN3 expression at the cell surface of human glioma cells, and that CAMKII-dependent regulation of these channels contributes to glioma invasion (5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein acetylation is a common modification that occurs both at lysine residues within proteins (ε-amino acetylation) and multiple amino acid residues at the amino terminus of proteins (α-amino acetylation). The N-α-acetyltransferase ARD1 homolog A protein (ARD1A, also known as NAA10) and the highly homologous N-α-acetyltransferase ARD1 homolog B protein (ARD1B, also known as ARD2 or NAA11) are mutually exclusive catalytic subunits of the amino-terminal acetyltransferase complex (NatA) (1-3). This complex, which consists of either ARD1A or ARD1B and the N-α-acetyltransferase 15 (NAA15) auxiliary protein, localizes to ribosomes where it functions to acetylate Ser-, Ala-, Gly-, Thr-, Cys-, Pro-, and Val- amino termini after initiator methionine cleavage during protein translation (1-5). Like ε-amino acetylation, amino-terminal α-amino acetylation functions to regulate protein stability, activity, cellular localization, and protein-protein interactions (4,5). Defects in ARD1A have been shown to cause amino-terminal acetyltransferase deficiency (NATD), which results in severe delays and defects in postnatal growth (6).In addition to functioning as amino-terminal acetyltransferases in the NatA complex, free ARD1A and ARD1B proteins regulate cell growth and differentiation through ε-amino acetylation of lysine residues in multiple target proteins, including the HIF-1α, β-catenin, and AP-1 transcription factors (7-9). ARD1A-mediated acetylation of HIF-1α at Lys532 under normoxic conditions enhances binding of VHL, leading to increased ubiquitination and degradation of HIF-1α and down-regulation of HIF-1α target genes involved in angiogenesis, apoptosis, cellular proliferation, and glucose metabolism (7). Decreased expression of ARD1A under hypoxic conditions contributes to the stabilization of HIF-1α and upregulation of target genes (7). ARD1A also promotes cell proliferation and tumorigenesis by acetylating and activating β-catenin and AP-1 transcription factors, leading to the stimulation of cyclin D1 expression (8,9). Interestingly, the acetyltransferase activity of ARD1A is regulated by autoacetylation at Lys136, which is required for the ability of ARD1A to promote proliferation and tumorigenesis (9). Research studies have shown that ARD1 proteins are over-expressed in multiple cancers, including breast, prostate, lung, and colorectal cancers (10-13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Intercellular cell adhesion molecule-2 (CD102/ICAM-2) is a cell surface glycoprotein that belongs to the immunoglobulin superfamily (IgSF) of adhesion molecules. Like CD54/ICAM-1, CD102/ICAM-2 is a ligand that binds the leukocyte adhesion molecule LFA-1 (leukocyte function-associated antigen-1), which mediates intercellular interactions between immune cells and other cell types (1).Expression of CD102/ICAM-2 has been shown to affect angiogenesis (2), cellular radioresistance (3) and anti-tumor immune response (4). Along with CD54/ICAM-1, CD102/ICAM-2 mediates T cell crawling and diapedesis across the blood-brain barrier (5), as well as T cell migration across the bronchial epithelium (6). CD102/ICAM-2 interaction with the actin cytoskeleton through α-actinin has been shown to limit the mobility on neuroblastoma cells (7), and this effect is dependent on glycosylation of CD102/ICAM-2 (8).

$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. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated GATA-1 (D52H6) XP® Rabbit mAb #3535.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: GATA proteins comprise a group of transcription factors that are related by the presence of conserved zinc finger DNA binding domains, which bind directly to the nucleotide sequence core element GATA (1-3). There are six vertebrate GATA proteins, designated GATA-1 to GATA-6 (3).

$262
3 nmol
300 µl
SignalSilence® LRF/Pokemon siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit LRF (pokemon) expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Human

Background: Zinc finger and BTB domain-containing protein 7A (LRF, Pokemon, FBI1) is a transcriptional repressor encoded by the ZBTB7A gene that belongs to the POK (POZ and Kruppel)/ZBTB (zinc finger and BTB) family (1). LRF is broadly expressed with elevated expression in a variety of cancers relative to normal tissues, including non-small cell lung cancer, breast cancer, ovarian cancer, prostate cancer, and hepatocellular carcinoma (1-8). Research studies suggest that LRF acts as an oncogene through various mechanisms including repression of the tumor suppressors ARF and Rb, and repression of the cell cycle arrest factor p21Cip1 (9-11). The LRF transcription factor plays key roles during several stages of hematopoiesis including promoting lymphoid progenitor cells to commit to B cell differentiation by repressing T cell-promoting Notch signals, and promoting cell survival during terminal erythroid differentiation through suppression of the proapoptotic factor Bim (12,13).

$327
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 Phospho-PLCγ1 (Ser1248) (D25A9) Rabbit mAb #8713.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Flow Cytometry

Background: Phosphoinositide-specific phospholipase C (PLC) plays a significant role in transmembrane signaling. In response to extracellular stimuli such as hormones, growth factors, and neurotransmitters, PLC hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to generate two secondary messengers: inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG) (1). At least four families of PLCs have been identified: PLCβ, PLCγ, PLCδ, and PLCε. Phosphorylation is one of the key mechanisms that regulate the activity of PLC. PLCγ is activated by both receptor and non-receptor tyrosine kinases (2). PLCγ forms a complex with EGF and PDGF receptors, which leads to the phosphorylation of PLCγ at Tyr771, 783, and 1248 (3). Phosphorylation by Syk at Tyr783 activates the enzymatic activity of PLCγ1 (4). PLCγ2 is engaged in antigen-dependent signaling in B cells and collagen-dependent signaling in platelets. Phosphorylation by Btk or Lck at Tyr753, 759, 1197, and 1217 is correlated with PLCγ2 activity (5,6).

$262
3 nmol
300 µl
SignalSilence® PTP1B siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit PTP1B expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Human

Background: Protein-tyrosine phosphatase 1B (PTP1B) is the original member of the protein tyrosine phosphatase (PTP) family of proteins (1). PTP1B is highly expressed in insulin-responsive tissues and negatively regulates insulin, as well as integrin, through dephosphorylation of phosphotyrosine residues (2-4). PTP1B knockout mice show resistance to dietary weight gain and enhanced insulin sensitivity, suggesting a possible role in treatment of obesity as well as type 2 diabetes (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Fatty acid binding proteins (FABPs) bind to fatty acids and other lipids to function as cytoplasmic lipid chaperones (1). They participate in the transport of fatty acids and other lipids to various cellular pathways (2). Differential expression of FABPs is found in several types of tumors and their normal-cell counterparts (3). FABP7 is abundantly expressed in fetal brain and may be essential for development (4). Expression is required for the establishment of the radial glial fiber system, a system that is necessary for the development of cortical layers (5). Increased expression of FABP7 is associated with reduced survival in patients with glioblastoma (6), and is also found in glial cells following nerve injury (7). Investigators have found loss of FABP7 may be involved in the development and progression of breast cancer and expression of FABP7 has been shown to induce mammary differentiation and to inhibit growth of breast cancer cells (8,9).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, 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: Western Blotting

Background: Myelin basic protein (MBP) is an abundant central nervous system (CNS) myelin membrane protein that plays an important role in nerve myelination. Myelin sheaths are multi-layered membranes derived from oligodendrocytes that increase the conduction velocity of axonal impulses. MBP helps to adhere the cytoplasmic leaflets of adjacent oligodendrocyte membranes to one another. Several splice variants of MBP are expressed in cells and the protein is modified following translation (i.e. phosphorylation, methylation), which suggests additional membrane adhesion functions (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: MDR1/ABCB1 belongs to the Mdr/Tap subfamily of the ATP-binding cassette transporter superfamily (1). Multidrug resistance 1 (MDR1) serves as an efflux pump for xenobiotic compounds with broad substrate specificity. MDR1 substrates include therapeutic agents such as actinomycin D, etoposide, imatinib, and doxorubicin, as well as endogenous molecules including β-amyloids, steroid hormones, lipids, phospholipids, cholesterol, and cytokines (2). Research studies have shown that MDR1 reduces drug accumulation in cancer cells, allowing the development of drug resistance (3-5). On the other hand, MDR1 expressed in the plasma membrane of cells in the blood-brain, blood-cerebral spinal fluid, or blood-placenta barriers restricts the permeability of drugs into these organs from the apical or serosal side (6,7). MDR1 is also expressed in normal tissues with excretory function such as small intestine, liver, and kidney (7). Intracellular MDR1 has been detected in the ER, vesicles, and nuclear envelope, and has been associated with cell trafficking machinery (8). Other reported functions of MDR1 include viral resistance, cytokine trafficking (9,10), and lipid homeostasis in the peripheral and central nervous system (11-13).

$489
96 assays
1 Kit
PathScan® Phospho-Mer (panTyr) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of tyrosine-phosphorylated Mer protein. A Mer Rabbit mAb has been coated onto the microwells. After incubation with cell lysates, Mer protein (phospho and nonphospho) is captured by the coated antibody. Following extensive washing, a Phospho-Tyrosine Mouse Detection mAb is added to detect the captured phospho-Mer proteins. 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 Mer protein phosphorylated on tyrosine residues.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: Mer tyrosine kinase belongs to a receptor tyrosine kinase family with Axl and Tyro3. This family is characterized by a common NCAM (neural adhesion molecule)-related extracellular domain and a common ligand, GAS6 (growth arrest-specific protein 6). Mer protein has an apparent molecular weight of 170-210 kDa due to different glycosylation patterns generated in different cell types. Mer can be activated by dimerization and autophosphorylation through ligand binding or homophilic cell-cell interaction mediated by its NCAM-like motif (1). The downstream signaling components of activated Mer include PI3 kinase, PLCγ, and MAP kinase (2). Family members are prone to transcriptional regulation and carry out diverse functions including the regulation of cell adhesion, migration, phagocytosis, and survival (3). Mer regulates macrophage activation, promotes apoptotic cell engulfment, and supports platelet aggregation and clot stability in vivo (4). Investigators have found that overexpression of Mer may play a cooperative role in leukemogenesis and may be an effective target for biologically based leukemia/lymphoma therapy (5).

$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Antigen receptors found on the surface of B cells contain a heterodimeric signaling component composed of CD79A and CD79B, also known as Ig α and Ig β, respectively (1,2). Presence of this receptor complex is essential for B-cell development and function (3). Together these two proteins and the associated B cell receptor initiate intracellular signaling following antigen binding (4,5). An immunoreceptor tyrosine-based activation motif (ITAM) found in the CD79A intracellular region appears to be important for its function (6). Antigen binding precedes formation of the CD79A and CD79B heterodimer and subsequent activation of receptor associated kinases (7). Research has shown that CD79A is a marker for B-lineage lymphoblastic leukemia (8). Additionally, investigators have found that mutations in the CD79A (MB1) gene are associated with abnormally low levels of functional B cell receptors in some cases of chronic B cell lymphocytic leukemia (9).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The cyclin-dependent kinases form complexes with their cyclin partners and with CDK inhibitors. CDK6 and CDK4 associate with the D-type cyclins and target the retinoblastoma protein, allowing passage through the G1/S phase restriction point (1). CDK6/cyclin D complexes are sequestered in their inactive form through binding to one of the INK4 CDK inhibitor family members (2,3). Unlike the INK4 family of CDK inhibitors, the CDK inhibitor p21 Waf1/Cip1 may enhance the association of CDK4 and CDK6 with their cyclin D partners (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Eukaryotic cell proliferation depends strictly upon the E3 ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C), whose main function is to trigger the transition of the cell cycle from metaphase to anaphase. The APC/C complex promotes the assembly of polyubiquitin chains on substrate proteins in order to target these proteins for degradation by the 26S proteasome (1,2). The vertebrate APC/C complex consists of as many as 15 subunits, including multiple scaffold proteins, two catalytic subunits (APC2, APC11), and a number of proteins responsible for substrate recognition (3). All E3 enzymes, including APC/C, utilize ubiquitin residues activated by E1 enzymes and transferred to E2 enzymes. Research studies indicate that APC/C interacts with the E2 enzymes UBE2S and UBE2C via the RING-finger domain-containing subunit APC11 (4-6). APC/C function relies on multiple cofactors, including an APC/C coactivator formed by the cell division control protein 20 homolog (CDC20) and Cdh1/FZR1. The CDC20/Cdh1 coactivator is responsible for recognition of APC/C substrates through interaction with specific D-box and KEN-box recognition elements within these substrates (7-9).

$327
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in mouse cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-SHP-2 (Tyr580) (D66F10) Rabbit mAb #5431.
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Flow Cytometry

Background: SHP-2 (PTPN11) is a ubiquitously expressed, nonreceptor protein tyrosine phosphatase (PTP). It participates in signaling events downstream of receptors for growth factors, cytokines, hormones, antigens, and extracellular matrices in the control of cell growth, differentiation, migration, and death (1). Activation of SHP-2 and its association with Gab1 is critical for sustained Erk activation downstream of several growth factor receptors and cytokines (2). In addition to its role in Gab1-mediated Erk activation, SHP-2 attenuates EGF-dependent PI3 kinase activation by dephosphorylating Gab1 at p85 binding sites (3). SHP-2 becomes phosphorylated at Tyr542 and Tyr580 in its carboxy-terminus in response to growth factor receptor activation (4). These phosphorylation events are thought to relieve basal inhibition and stimulate SHP-2 tyrosine phosphatase activity (5). Mutations in the corresponding gene result in a pair of clinically similar disorders (Noonan syndrome and LEOPARD syndrome) that may result from abnormal MAPK regulation (6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: DNA methyltransferase 1 (DNMT1)-associated protein 1 (DMAP1) is a nuclear protein that functions in transcriptional repression and DNA repair. DMAP1 was first identified as an activator of DNMT1 methyltransferase activity (1). Both DMAP1 and DNMT1 are targeted to replication foci during S phase and function to transfer proper methylation patterns to newly synthesized DNA during replication (1). In late S phase, DMAP1-DNMT1 co-operate with a p33ING1-Sin3-HDAC2 complex to maintain pericentric heterochromatin by deacetylating histones, methylating histone H3 at Lys9, and methylating DNA (1,2). The DMAP1 protein is also part of the TIP60-p400 complex, a histone acetyltransferases (HAT) and chromatin-remodeling complex that functions in DNA repair (3,4). Upon DNA damage, the TIP60-p400 complex acetylates histone H4 at Lys16 to induce chromatin relaxation and activation of the ATM kinase. DMAP1 is required for DNA-damage induced TIP60-p400-mediated histone acetylation, and deletion of DMAP1 impairs AMT function (5). DMAP1-DNMT1 may also methylate DNA at sites of DNA damage during homologous recombination, which results in gene silencing (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: B-cell CLL/lymphoma 9-like protein (BCL9L, BL2, Bcl9-2, DLNB11) is a transcriptional activator that was originally identified in silico based on homology to BCL9 (1). BCL9L was subsequently found to play an important role in Wnt/β-catenin signaling by interacting with β-catenin and enhancing the transactivation potential of the β-catenin/TCF complex (2). Research studies show that BCL9L can increase the tumorigenic effect of aberrant Wnt signaling in some cases of colorectal cancer (2). Expression of BCL9L is correlated with tumor progression in colorectal (3) and breast cancer (4). Targeted deletion of BCL9 and BCL9L in the intestinal epithelium resulted in abrogation of Wnt target genes, including those controlling epithelial-mesenchymal transition and stem-cell like properties (5).

$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 mouse cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Cox2 (D5H5) XP® Rabbit mAb #12282.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: Cyclooxygenase1 (Cox1) and cyclooxygenase2 (Cox2), family members with 60% homology in humans, catalyze prostaglandin production from arachidonic acid (1,2). While Cox1 expression is constitutive in most tissues, Cox2 expression is induced by lipopolysaccharide (LPS) and peptidoglycan (PGN) (3). PGN activates Ras, leading to phosphorylation of Raf at Ser338 and Erk1/2 at Tyr204. The activation of MAP kinase signaling results in subsequent activation of IKKα/β, phosphorylation of IκBα at Ser32/36, and NF-κB activation. Finally, activation of the transcription factor NF-κB is responsible for the induction of Cox2 expression (4). Investigators have shown that LPS and PGN induce the clinical manifestations of arthritis and bacterial infections, such as inflammation, fever, and septic shock (5). Research studies have indicated that Cox1 and Cox2 may also play a role in the neuropathology of Alzheimer's disease by potentiating γ-secretase activity and β-amyloid generation (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: Histone cell cycle regulation defective homolog A (HIRA), also known as TUP1-like enhancer of split protein 1 (TUPLE1), is the mammalian homolog of the yeast HIR1 and HIR2 transcriptional repressor proteins (1). HIRA interacts with UBN1, CABIN, and ASF1A in the cell nucleus to form the evolutionarily conserved HUCA histone chaperone complex that deposits the variant histone H3.3 into chromatin in a DNA-replication independent manner (2). HIRA is required for deposition of histone H3.3 at the transcription start sites of genes, where incorporation of histone H3.3 facilitates nucleosome destabilization and contributes to transcriptional activation (3-5). Histone H3.3 is also linked to gene silencing and is incorporated into regions of the genome thought to be transcriptionally inactive (5-7). While some incorporation of H3.3 into heterochromatin is facilitated by a different histone chaperone complex that contains ATRX and DAXX (ie. telomeric incorporation of H3.3), HIRA is required for incorporation of histone H3.3 and formation of senescence-associated heterochromatin foci (SAHF) during cellular senescence (5-8). HIRA is ubiquitously expressed during mouse embryonic development (9). In the adult mouse, HIRA is expressed at high levels in the kidney, skeletal muscle, and pancreas, but it is expressed at lower levels in the heart, lung, placenta, brain, and liver (9). A missing copy of the HIRA gene on human chromosome region 22q11.2 is a common characteristic of DiGeorge syndrome patients and insufficient production of the HIRA protein may disrupt normal embryonic development (9).

$262
3 nmol
300 µl
SignalSilence® Mitofusin-1 siRNA II from Cell Signaling Technology (CST) allows the researcher to specifically inhibit mitofusin-1 expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Human

Background: Mitofusins are mitochondrial transmembrane GTPases that function to regulate mitochondrial fusion, a process that occurs in concert with mitochondrial division and is necessary for the maintenance of structural and genetic mitochondrial integrity (1,2). Two mitofusins have been described in mammals, mitofusin-1 and -2, which share 60% amino acid identity and appear to function coordinately to regulate mitochondrial fusion (3). Mitochondrial fusion is widely recognized as important for normal cell growth and development (4), and may have evolved as a mechanism to offset the deleterious effects of mtDNA mutations (3). Null mutations in either mitofusin are embryonic lethal in mice, whereas conditional knockout studies have shown that combined deletion of mitofusin-1 and mitofusin-2 in skeletal muscle results in severe mitochondrial dysfunction (3).

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

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

Background: Salvador homolog (SAV1), originally named WW45, was first identified as a 45 kDa protein containing a pair of WW domains and a coiled-coil region (1). SAV1 was subsequently shown to function as a scaffold protein, in a protein complex that includes the kinases MST2 and LATS1, and the transcriptional co-activator YAP (2). This protein complex comprises the core components of the Hippo signaling pathway, which regulates important cellular functions, including contact inhibition and apoptosis, that function to regulate tissue growth and organ size (3,4). A genetic screen in Drosophila identified a role for SAV1 in cell cycle regulation and apoptosis (5), while embryonic mice lacking Sav1 displayed hyperplastic growth and epithelial differentiation effects (6). These findings, together with the observation that SAV1 is mutated a number of human cancer cell lines, suggest that SAV1 functions as a tumor suppressor in the Hippo signaling pathway (5, 7).