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Product listing: JunB (P169) Antibody, UniProt ID P17275 #3755 to RBAP46/RBAP48 Antibody, UniProt ID Q09028 #4633

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: JunB is a basic region, leucine zipper (bZIP) transcription factor belonging to the Jun family that includes c-Jun and JunD. Jun family members homodimerize or heterodimerize with Fos and ATF proteins to form a functional transcription factor AP-1 (activator protein 1), whose activity is regulated by a variety of physiological and pathological stimuli such as growth factors, infections, and stress signals (1-4). While JunB sometimes antagonizes c-Jun transcriptional activity, it may functionally substitute for c-Jun during development in mice (5-7). JunB regulates hematopoietic stem cell number and plays an important role in the pathogenesis of chronic myelogenous leukemia (CML) and acute myeloid leukemia (AML) (8,9).

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

Application Methods: Western Blotting

Background: The methylation of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP) is an essential step in the formation of thymine nucleotides (1,2, reviewed in 3). This process is catalyzed by thymidylate synthase (TS or TYMS), a homodimer composed of two 30 kDa subunits. TS is an intracellular enzyme that provides the sole de novo source of thymidylate, making it a required enzyme in DNA biosynthesis with activity highest in proliferating cells (1). Being the exclusive source of dTMP, investigators have concluded that TS is also an important target for anticancer agents such as 5-fluorouracil (5-FU) (1-5). 5-FU acts as a TS inhibitor and is active against solid tumors such as colon, breast, head, and neck. Research studies have demonstrated that patients with metastases expressing lower levels of TS have a higher response rate to treatment with 5-FU than patients with tumors that have increased levels of TS (5). Researchers continue to investigate TS expression in different types of cancers (6-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: The centrosome is an organelle that plays an important role in the mammalian cell cycle. Prior to the onset of mitosis, the single interphase centrosome duplicates only once, creating a pair of daughter centrosomes that will form the two spindle poles after breakdown of the nuclear envelope. Failure to duplicate or overduplication of the centrosome can result in polyploidy and genomic instability (reviewed in 1). Centrosomal protein of 110 kDa (CP110) is a cyclin-dependent kinase (CDK) substrate that plays a critical role in promoting the duplication of centrosomes and correct spindle formation (2). In addition, CP110 has been shown to interact with calmodulin (CaM) and centrin to regulate the progression through cytokinesis (3), and with Cep97 and Cep290 to regulate the formation of primary cilia (4,5). CP110 expression is induced in G1/S with peak expression during S-phase. Degradation of CP110 is mediated by cyclin F in G2-phase and is required for normal progression into M-phase (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human, Mouse, Rat

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

Background: PZR (Protein zero related) is an immunoglobulin superfamily protein that specifically binds the tyrosine phosphatase SHP-2 through its intracellular immunoreceptor tyrosine-based inhibitory motifs (ITIMs) (1,2). PZR is phosphorylated by c-Src, c-Fyn, c-Lyn, Csk, and c-Abl (3). PP1, a Src family kinase inhibitor, inhibits PZR phosphorylation (4,5). There are three alternatively spliced isoforms, designated as PZR, PZRa, and PZRb; both PZRa and PZRb lack ITIMs (6,7). PZR is the main receptor of ConA and has an important role in cell signaling via c-Src (4). PZR is expressed in many cell types and is localized to cell contacts and intracellular granules in BAECs and mesothelioma (REN) cells. PZR has been implicated as a cell adhesion protein that may be involved in SHP-2-dependent signaling at interendothelial cell contacts (3). Hypertyrosine phosphorylation of PZR was observed during embryogenesis in a mouse model of Noonan syndrome (8).

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

Application Methods: Western Blotting

Background: The RalA binding protein 1 (RalBP1 or RLIP76) was originally identified as a GTP-RalA associated protein that acted as a downstream RalA effector in regulating Ral-Ras signaling (1). RalBP1 interacts with RalA and the endocytosis protein REPS2 (POB1) through its carboxy-terminal Ral binding domain. RalBP1 has an intrinsic GTPase activating function and interacts with Cdc42 through its centrally located Rho-GAP domain (1-3). A protein complex containing RalBP1/POB1/RalA regulates endocytosis of membrane receptors (4). RalBP1 also functions as a non-ABC transporter that catalyzes the ATP-dependent transport of numerous xenobiotics, including glutathione conjugates and some chemotherapeutic agents. RalBP1 transporter activity may play an important role in detoxification, drug resistance and the stress response (5-7). Increased expression of RalBP1 protein is associated with some forms of cancer and regression of cancer xenografts results from RalBP1 inhibition (8,9). Evidence to date suggests that RalBP1 may be a promising therapeutic target for cancer therapy.

$262
3 nmol
300 µl
SignalSilence® KEAP1 siRNA II from Cell Signaling Technology (CST) allows the researcher to specifically inhibit KEAP1 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: The nuclear factor-like 2 (NRF2) transcriptional activator binds antioxidant response elements (ARE) of target gene promoter regions to regulate expression of oxidative stress response genes. Under basal conditions, the NRF2 inhibitor INrf2 (also called KEAP1) binds and retains NRF2 in the cytoplasm where it can be targeted for ubiquitin-mediated degradation (1). Small amounts of constitutive nuclear NRF2 maintain cellular homeostasis through regulation of basal expression of antioxidant response genes. Following oxidative or electrophilic stress, KEAP1 releases NRF2, thereby allowing the activator to translocate to the nucleus and bind to ARE-containing genes (2). The coordinated action of NRF2 and other transcription factors mediates the response to oxidative stress (3). Altered expression of NRF2 is associated with chronic obstructive pulmonary disease (COPD) (4). NRF2 activity in lung cancer cell lines directly correlates with cell proliferation rates, and inhibition of NRF2 expression by siRNA enhances anti-cancer drug-induced apoptosis (5).

$260
200 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Met, a high affinity tyrosine kinase receptor for hepatocyte growth factor (HGF, also known as scatter factor) is a disulfide-linked heterodimer made of 45 kDa α- and 145 kDa β-subunits (1,2). The α-subunit and the amino-terminal region of the β-subunit form the extracellular domain. The remainder of the β-chain spans the plasma membrane and contains a cytoplasmic region with tyrosine kinase activity. Interaction of Met with HGF results in autophosphorylation at multiple tyrosines, which recruit several downstream signaling components, including Gab1, c-Cbl, and PI3 kinase (3). These fundamental events are important for all of the biological functions involving Met kinase activity. The addition of a phosphate at cytoplasmic Tyr1003 is essential for Met protein ubiquitination and degradation (4). Phosphorylation at Tyr1234/1235 in the Met kinase domain is critical for kinase activation. Phosphorylation at Tyr1349 in the Met cytoplasmic domain provides a direct binding site for Gab1 (5). Research studies have shown that altered Met levels and/or tyrosine kinase activities are found in several types of tumors, including renal, colon, and breast. Thus, investigators have concluded that Met is an attractive potential cancer therapeutic and diagnostic target (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunohistochemistry (Paraffin)

Background: Orexin, also called HCRT or hypocretin, is expressed as a precursor that is processed into two biologically active neuropeptides called orexin-A (HCRT1) and orexin-B (HCRT2) (1). Orexin is expressed in the lateral and posterior hypothalamus and plays a role in feeding behavior (1). The orexin neuropeptides act by stimulating the two orexin receptors that belong to the G Protein-Coupled Receptors family (1). Orexin receptor 1 is mostly found in the hypothalamic region, while orexin receptor 2 is also found in the cerebral cortex and the nucleus accumbent (2). Orexin also plays a role in adipocyte homeostasis and is required for brown adipose tissue development, differentiation, and function (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Retromer is a heteropentameric protein complex that consists of two protein compounds, a sortin-nexin dimer and a trimeric VPS26-VPS29-VPS35 protein subcomplex. The retromer complex associates with endosomes at their cytosolic side to mediate retrograde transport of transmembrane proteins from endosomes to the trans-Golgi network (1-3). Vacuolar protein sorting-associated protein 29 (VPS29) is considered a cryptic metallophosphoesterase, as it contains a conserved metallophosphoesterase-fold that includes a phenylalanine in place of an essential histidine residue within the active site (4). While VPS29 is capable of binding metal ions, it does so with low affinity and exhibits no enzymatic activity. Instead, VPS29 serves as a scaffold protein that interacts with the carboxy-terminal region of VPS35 and is essential for association of the retromer with other endosomal transport proteins (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Human Tid-1 is a human orthologue of the Drosophila tumor suppressor lethal (2) tumorous imaginal discs, l (2) tid and is a member of the DnaJ family of proteins that serve as co-chaperones to Hsp70 proteins (1). These proteins are characterized by a J domain, a highly conserved tetrahelical domain that binds to Hsp70 chaperones and activates their ATPase activity. Hsp70 and their associated chaperones mediate a variety of activities including the folding of newly synthesized polypeptides, the translocation of proteins across membranes and assembly of multimeric protein complexes. Two alternatively spliced variants exist for human Tid-1 ,designated hTID-1s and hTID-1L, both which contain the J domain, localize to the mitochondrial matrix, and co-immunoprecipitate with Hsp70. Expression of Tid-1L increases apoptosis induced by the DNA damaging agent mitomycin c (MMC) and by TNF-alpha, and that activity is dependent on its J domain. In contrast, expression of Tid-1S reduces apoptosis by these agents. Tid-1 orthologues are also found in mouse (mTid-1) and rat (rTid-1) (2,3). The mouse orthologue was originally identified though its interaction with p120 GTPase-activating protein (GAP), raising the possiblity that Tid-1 helps regulates the confirmation, activity, or subcellular localization of GAP (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: ADP-ribosylation factor GTPase activating protein 1 (ARFGAP1) is a Golgi-localized protein that regulates vesicle formation and membrane trafficking (1). ARFGAP1 initiates cargo selection and COP1 vesicle formation by stimulating GTP hydrolysis of ADP-ribosylation factor ARF1 (2). This GTPase activating protein initiates vesicle transport by coupling vesicle formation with cargo sorting (3). ARFGAP1 plays an active role in the Golgi-to-ER retrograde, intra-Golgi, and trans-Golgi trafficking networks (1). Research studies indicate that ARFGAP1 can act as a GTPase activating protein for LRRK2, a large multifunction protein whose genetic mutations are associated with Parkinson’s disease (4). ARFGAP1 regulates GTPase activity and promotes the kinase activity of LRRK2, which suggests some potential as a promising target for study of LRRK2 mediated neurodegeneration (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: Modulation of chromatin structure plays a critical role in the regulation of transcription and replication of the eukaryotic genome. The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. In addition to the growing number of post-translational histone modifications regulating chromatin structure, cells can also exchange canonical histones with variant histones that can directly or indirectly modulate chromatin structure (1). CENP-A, also known as the chromatin-associated protein CSE4 (capping-enzyme suppressor 4-p), is an essential histone H3 variant that replaces canonical histone H3 in centromeric heterochromatin (2). The greatest divergence between CENP-A and canonical histone H3 occurs in the amino-terminal tail of the protein, which binds linker DNA between nucleosomes and facilitates proper folding of centromeric heterochromatin (3). The amino-terminal tail of CENP-A is also required for recruitment of other centromeric proteins (CENP-C, hSMC1, hZW10), proper kinetochore assembly, and chromosome segregation during mitosis (4).CENP-A is regarded as the epigenetic mark of the centromere that persists through cell generations (5). Although its presence is necessary, it is not sufficient for formation of functional kinetochores (6). CENP-T, in complex with CENP-W, has recently been shown to form a histone fold, a structure that is capable of association with DNA, and target DNA to the kinetochore (7). Kinetochore attachment is mediated by a long flexible N-terminal region that has been shown to interact with outer proteins of the kinetochore complex (reviewed in 8). Moreover, the CENP-T-W complex has also been shown to interact with the CENP-S-X dimer, to form a heterotetrameric complex that has structural and potentially functional similarity to canonical histones (8). Since CENP-S-X are conserved kinetochore localized proteins, this new complex has been suggested to be a novel centromeric histone.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: Carboxyl-terminal modulator protein (CTMP) is a negative regulator of Akt and was identified as an Akt binding protein. Akt, also referred to as PKB or Rac, plays a critical role in controlling the balance between survival and apoptosis (1-3). This protein kinase, activated by insulin and various growth and survival factors, functions in a wortmannin-sensitive pathway involving PI3 kinase (2,3). Akt is activated by phospholipid binding and activation loop phosphorylation at Thr308 by PDK1 (4), and by phosphorylation within the carboxy-terminus at Ser473. CTMP binds to the regulatory domain of Akt at the carboxy terminus of the protein and inhibits phosphorylation on Thr308 and Ser473 (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: PTPN18 is a member of the PEST family of nonreceptor protein tyrosine phosphatases, a group that also includes PTP-PEST and PEP (1-3). Members of this protein family contain an N-terminal catalytic domain and a noncatalytic C-terminal domain with a PEST motif that mediates protein-protein interactions (4). PTPN18 was first identified in hematopoietic stem cells (HSCs), where it was suggested to play a role in HSC differentiation (1-3). Subsequently, PTPN18 was shown to bind to c-Src kinase, forming a protein complex that functions to inhibit Src-family kinase signaling (4,5). More recently, PTPN18 expression has been shown to correlate with HER2 receptor expression in breast cancer cell lines (6,7), where it has been suggested to repress HER2 signaling (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: TNFRSF8/CD30 is a type-I transmembrane glycoprotein that is a member of the TNFR superfamily. CD30 is synthesized as a precursor protein that undergoes extensive posttranslational modification before becoming embedded in the plasma membrane as a 120-kDa transmembrane protein (1,2). The expression of CD30 is upregulated in activated T-cells and may trigger costimulatory signaling pathways upon its engagement (3,4). While its expression is normally restricted to subsets of activated T-cells and B-cells, CD30 expression is robustly upregulated in hematologic malignancies, such as Hodgkin’s lymphoma (HL), anaplastic large cell lymphoma (ALCL), and adult T-cell leukemia, thus making it an attractive target for therapeutic intervention (5,6). Research studies have suggested that in certain disease contexts, CD30 recruits TRAF2 and TRAF5 adaptor proteins to drive NF-kappa B activation, aberrant cell growth, and cytokine production (7-9). CD30 signaling is also regulated by TACE-dependent proteolytic cleavage of its ectodomain, which results in reduced CD30L-dependent activation of CD30+ cells (10, 11).

$262
3 nmol
300 µl
SignalSilence® IKKα siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit IKKα 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: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins (1-3). Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB (3-7). The key regulatory step in this pathway involves activation of a high molecular weight IκB kinase (IKK) complex whose catalysis is generally carried out by three tightly associated IKK subunits. IKKα and IKKβ serve as the catalytic subunits of the kinase and IKKγ serves as the regulatory subunit (8,9). Activation of IKK depends upon phosphorylation at Ser177 and Ser181 in the activation loop of IKKβ (Ser176 and Ser180 in IKKα), which causes conformational changes, resulting in kinase activation (10-13).

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

Application Methods: Western Blotting

Background: The 20S proteasome is the major proteolytic enzyme complex involved in intracellular protein degradation. It consists of four stacked rings, each with seven distinct subunits. The two outer layers are identical rings composed of α subunits (called PSMAs), and the two inner layers are identical rings composed of β subunits. While the catalytic sites are located on the β rings (1-3), the α subunits are important for assembly and as binding sites for regulatory proteins (4). Seven different α and ten different β proteasome genes have been identified in mammals (5). PA700, PA28, and PA200 are three major protein complexes that function as activators of the 20S proteasome. PA700 binds polyubiquitin with high affinity and associates with the 20S proteasome to form the 26S proteasome, which preferentially degrades poly-ubiquitinated proteins (1-3). The proteasome has a broad substrate spectrum that includes cell cycle regulators, signaling molecules, tumor suppressors, and transcription factors. By controlling the degradation of these intracellular proteins, the proteasome functions in cell cycle regulation, cancer development, immune responses, protein folding, and disease progression (6-9).

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

Application Methods: Western Blotting

Background: The protein product of the DEK oncogene is a nuclear phosphoprotein that is highly conserved among higher eukaryotic organisms and preferentially expressed in actively proliferating and/or malignant cells (1,2). DEK is an abundant, non-histone chromosomal protein that establishes and maintains heterochromatin by interacting with HP1a, enhancing HP1a binding to tri-methyl histone H3 Lys9 and stabilizing local tri-methyl histone H3 Lys9 levels (3). DEK localized to euchromatin represses transcription by interacting with transcription factors such as RelA/p65 (4). The DEK protein also associates with mRNA processing factors to regulate splicing and nuclear export (5,6).The DEK proto-oncogene functions as a negative regulator of cellular differentiation, senescence, and apoptosis. DEK is translocated and/or over-expressed in a number of different cancers, including acute myeloid leukemia, breast cancer, cervical cancer, hepatocellular carcinoma, melanoma, and small cell lung cancer (1,2). In addition to the role of DEK in cancer biology, which is mainly related to its intracellular functions, extracellular DEK is implicated in the pathogenesis of autoimmune disorders (1,2). Circulating autoantibodies to DEK have been identified in the serum of patients with autoimmune diseases, including juvenile idiopathic arthritis, sarcoidosis, and systemic lupus erythematosus. DEK is secreted by human monocyte-derived macrophages and apoptotic T-lymphocytes and can act as a chemotactic, pro-inflammatory factor (7,8). Exogenous DEK can penetrate neighboring cells, and translocate to the nucleus to carry out its endogenous nuclear functions (9). IL-8 induced secretion of DEK from macrophages serves as a chemoattractant for peripheral blood leukocytes (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: HS1 (HCLS1, LckBP1, p75) is a protein kinase substrate that is expressed only in tissues and cells of hematopoietic origin (1,2). HS1 contains four cortactin repeats and a single SH3 domain (2). This intracellular protein is phosphorylated following immune receptor activation, which promotes recruitment of HS1 to the immune synapse (3-5). Phosphorylation of HS1 is required to regulate actin dynamics and provide docking sites for many other signaling molecules, such as Vav1 and PLCγ1 (6). HS1 also plays an important role in platelet activation (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: CYP17A1, also known as cytochrome P450C17, is a steroidogenic enzyme belonging to the P450 cytochrome superfamily of monooxygenases (1, 2). In humans, CYP17A1 expression is abundantly expressed in the adrenal cortex, where it plays a central role in the androgen synthesis pathway (2). CYP17A1 is the primary target of abiraterone, a synthetic steroid used in the treatment of castration-resistant prostate cancer (CRPC) (3, 4). Abiraterone is converted to the more active form D4A, which antagonizes androgen receptor signaling by inhibiting CYP17A1 and other steroidogenic enzymes (3, 4). This suppresses the synthesis of 5α-dihydrotestosterone (DHT), which is a driver of castration-resistant prostate cancer cell growth (3, 4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: CD2 is a transmembrane glycoprotein expressed early in thymocyte development and present on most circulating T cells (1, 2). CD2 plays a role in T cell adhesion through binding to its ligand CD58 (LFA-3) (3). Stimulation of CD2 also leads to T cell activation and proliferation (2). T cells from mice deficient in both CD2 and CD28 have severe defects in T cell activation and function, while T cells deficient in either CD2 or CD28 are still capable of mounting a response, suggesting that CD2 and CD28 may have overlapping functions and may be able to compensate for each other (4). In addition, engagement of CD2 and CD58 was recently demonstrated to be the primary costimulatory signal in T cells that lack CD28 (5). CD2 expression also distinguishes a subset of plasmacytoid dendritic cells found in tumors and tonsils that express lysozyme, higher levels of IL-12 p40, and higher levels of CD80 (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: RalA and RalB are members of the Ras family of small GTPases and are highly homologous in protein sequence. The functions of RalA and RalB are distinct yet overlapping. By binding to various effector proteins, RalA and RalB serve as important GTP sensors for exocytosis and membrane trafficking (1-3). RalA is required for Ras-related tumorigenesis (4) and RalB is important for tumor survival (5). In addition to tumor formation, Ral proteins also play a role in cancer cell migration and metastatic tumor invasion (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: PEAK1 (Pseudopodium-enriched atypical kinase 1 or sgk269) is a member of nonreceptor atypical tyrosine kinase family identified by MS analysis of purified psedopodium (1). PEAK1 is a multi-domain protein with a N-terminal Erk binding site, followed by actin-targeting/Src substrate/Erk substrate region, Crk binding site, Shc binding site, and a C-terminal kinase domain (1, 2). By interacting with different adaptors like Shc, Grb2, Src, and others, PEAK1 functions as an important regulator in different signaling pathways, namely the Src/PEAK1/ErbB2 (3), EGFR Shc1/PEAK1/Grb2(4), TGFβ/PEAK1/Src/MAPK (5), and fibronectin/PEAK1/Src (6) pathways. PEAK1 plays an instrumental role in a wide variety of biological processes including epithelial-mesenchymal transition (EMT), dynamics of focal adhesion, cancer metastatic growth and invasion as well as cancer drug resistance (3, 5-8). Phosphorylation of PEAK1 at Tyr665 or Tyr635 by SFK (Src family Kinases) has been shown to be essential for cancer cell migration and invasion as well as the turnover of focal adhesions (7, 9).

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

Application Methods: Western Blotting

Background: Lysine-specific demethylase 1 (LSD1; also known as AOF2 and BHC110) is a nuclear amine oxidase homolog that acts as a histone demethylase and transcription cofactor (1). Gene activation and repression is specifically regulated by the methylation state of distinct histone protein lysine residues. For example, methylation of histone H3 at Lys4 facilitates transcriptional activation by coordinating the recruitment of BPTF, a component of the NURF chromatin remodeling complex, and WDR5, a component of multiple histone methyltransferase complexes (2,3). In contrast, methylation of histone H3 at Lys9 facilitates transcriptional repression by recruiting HP1 (4,5). LSD1 is a component of the CoREST transcriptional co-repressor complex that also contains CoREST, CtBP, HDAC1 and HDAC2. As part of this complex, LSD1 demethylates mono-methyl and di-methyl histone H3 at Lys4 through a FAD-dependent oxidation reaction to facilitate neuronal-specific gene repression in non-neuronal cells (1,6,7). In contrast, LSD1 associates with androgen receptor in human prostate cells to demethylate mono-methyl and di-methyl histone H3 at Lys9 and facilitate androgen receptor-dependent transcriptional activation (8). Therefore, depending on gene context LSD1 can function as either a transcriptional co-repressor or co-activator. LSD1 activity is inhibited by the amine oxidase inhibitors pargyline, deprenyl, clorgyline and tranylcypromine (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Pig

Application Methods: Immunoprecipitation, Western Blotting

Background: The protein kinase C-related kinases (PRKs) are a subfamily of Ser/Thr-specific kinases with a catalytic domain highly homologous to the PKC family (1-3). They are effectors of Rho family GTPases (4-6) and are activated by fatty acids and phospholipids in vitro (7,8). Activation in vitro and in vivo involves the activation loop phosphorylation of PRK1 (Thr774)/PRK2 (Thr816) by PDK1 (9,10).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: TBP binding protein associated factor 15 (TAF15) is a member of the multifunctional FET (FUS, EWS, and TAF15) family of proteins that bind both DNA and RNA and may be important for transcriptional regulation and RNA processing (1,2). Research studies show that FET family proteins, including TAF15, can be found as oncogenic fusion proteins with transcription factors in a variety of cancers. The fusion protein consists of the FET protein amino-terminal transcription activation domain and the transcription factor DNA binding domain, creating an aberrant transcription factor with potent transactivation potential (1-3). TAF15 can be part of a subset of the transcription factor IID (TFIID) complex, indicating that it may form a transcription pre-initiation complex at active genes, even if it is not considered a canonical TAF (4,5). Additional studies suggest roles for TAF15 in RNA splicing through its association with U1 small nuclear RNA and in regulation of cell cycle regulatory gene expression through a mechanism involving miRNA biosynthesis (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: CD109 is a glycosylphosphatidylinositol (GPI)-linked glycoprotein that belongs to the alpha2-macroglobulin family of thioester containing proteins (1). CD109 is associated with TGF-beta receptor I (TbRI) and inhibits TGF-beta signaling (2,3). Cleavage of CD109 at its Furin cleavage site results in the release of its large amino-terminal domain, which then binds to the TGF-beta receptor I to inhibit TGF-beta signaling (4-7). CD109 is expressed on a subset of CD34+ bone marrow cells and mesenchymal stem cells, activated platelets, activated T-cells, endothelial cells, and a wide variety of tumors (8-10). Elevated CD109 expression has been considered a diagnostic/prognostic marker for several types of cancers (11-14).

$260
100 µl
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Immunoprecipitation, Western Blotting

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Embryonic stem cells (ESC) derived from the inner cell mass of the blastocyst are unique in their pluripotent capacity and potential for self-renewal (1). Research studies demonstrate that a set of transcription factors that includes Oct-4, Sox2, and Nanog forms a transcriptional network that maintains cells in a pluripotent state (2,3). Chromatin immunoprecipitation experiments show that Sox2 and Oct-4 bind to thousands of gene regulatory sites, many of which regulate cell pluripotency and early embryonic development (4,5). siRNA knockdown of either Sox2 or Oct-4 results in loss of pluripotency (6). Induced overexpression of Oct-4 and Sox2, along with additional transcription factors Klf4 and c-Myc, can reprogram both mouse and human somatic cells to a pluripotent state (7,8). Additional evidence demonstrates that Sox2 is also present in adult multipotent progenitors that give rise to some adult epithelial tissues, including several glands, the glandular stomach, testes, and cervix. Sox2 is thought to regulate target gene expression important for survival and regeneration of these tissues (9).

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

Application Methods: Western Blotting

Background: Retinoblastoma-associated proteins 46 and 48 (RBAP46 and RBAP48; also known as RBBP7 and RBBP4) were first characterized in human cells as proteins that bind to the retinoblastoma (Rb) tumor suppressor protein (1). Since then, these proteins have been shown to be components of many protein complexes involved in chromatin regulation, including the chromatin assembly factor 1 (CAF-1) complex and type B histone acetyltransferase complex HAT1, both of which function in chromatin assembly during DNA replication (2,3). RBAP46 and RBAP48 are also found in the nucleosome remodeling factor complex NURF, the nucleosome remodeling and histone de-acetylation complex NuRD, and the Sin3/HDAC histone de-acetylation complex (4-7). More recently, RBAP46 and RBAP48 were identified as components of the polycomb repressor complex PRC2, which also contains EED and Ezh2 (8). RBAP46 and RBAP48 bind to the histone fold region of histone H4 and are believed to target these chromatin remodeling, histone acetylation, and histone de-acetylation complexes to their histone substrates (3).