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Product listing: IRAP (D7C5) XP® Rabbit mAb, UniProt ID Q9UIQ6 #6918 to LSD1 (1E5-H2) Mouse mAb, UniProt ID O60341 #4218

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

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

Background: IRAP (also known as LNPEP) was originally described as an insulin-responsive aminopeptidase found in Glut4-containing vesicles (1). It is essentially always in the same compartments as Glut4 and has identical insulin-stimulated translocation patterns as Glut4 (2). IRAP is therefore considered to be a surrogate marker for Glut4 (2). IRAP was later found to be a critical enzyme that regulates the expression and activity of several essential hormones and regulatory proteins, including the Glut4 transporter (3,4). This membrane associated, zinc-dependent cystinyl aminopeptidase acts as both a receptor for angiotensin IV as well as the enzyme that catalyzes the synthesis of this essential hormone from its angiotensinogen precursor (5). IRAP catalyzes the hydrolysis of several peptide hormones, including oxytocin and vasopressin (4). Abnormal IRAP expression or activity is associated with several forms of cancer in humans, including renal and endometrial cancers (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The protein phosphatase (PTP) receptor CD45 is a type I transmembrane protein comprised of a pair of intracellular tyrosine phosphatase domains and a variable extracellular domain generated by alternative splicing (1). The catalytic activity of CD45 is a function of the first phosphatase domain (D1) while the second phosphatase domain (D2) may interact with and stabilize the first domain, or recruit/bind substrates (2,3). CD45 interacts directly with antigen receptor complex proteins or activates Src family kinases involved in the regulation of T- and B-cell antigen receptor signaling (1). Specifically, CD45 dephosphorylates Src-family kinases Lck and Fyn at their conserved negative regulatory carboxy-terminal tyrosine residues and upregulates kinase activity. Conversely, studies indicate that CD45 can also inhibit Lck and Fyn by dephosphorylating their positive regulatory autophosphorylation site. CD45 appears to be both a positive and a negative regulator that conducts signals depending on specific stimuli and cell type (1). Human leukocytes including lymphocytes, eosinophils, monocytes, basophils, and neutrophils express CD45, while erythrocytes and platelets are negative for CD45 expression (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Erlin-1 and erlin-2 (SPFH1 and SPFH2) are SPFH domain-containing proteins that belong to the prohibitin family (1,2). The N-termal domain of erlin proteins contains ER-targeting sequences responsible for their translocation to the endoplasmic reticulum (ER) (3). In the ER, erlin-1 and erlin-2 specifically associate with the detergent resistant lipid raft microdomain of the membrane (3). Erlin-1 may be involved in dentritic cell activation (4) and erlin-2 has been shown to regulate the ER-associated degradation (ERAD) pathway by interacting with endogenous substrates and resulting in their polyubiquitination and degradation (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. Originally thought to function as a static scaffold for DNA packaging, histones have now been shown to be dynamic proteins, undergoing multiple types of post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (1,2). The p300/CBP histone acetyltransferases acetylate multiple lysine residues in the amino terminal tail of histone H2B (Lys5, 12, 15, and 20) at gene promoters during transcriptional activation (1-3). Hyper-acetylation of the histone tails neutralizes the positive charge of these domains and is believed to weaken histone-DNA and nucleosome-nucleosome interactions, thereby destabilizing chromatin structure and increasing the access of DNA to various DNA-binding proteins (4,5). In addition, acetylation of specific lysine residues creates docking sites that facilitate recruitment of many transcription and chromatin regulatory proteins that contain a bromodomain, which binds to acetylated lysine residues (6). Histone H2B is mono-ubiquitinated at Lys120 during transcriptional activation by the RAD6 E2 protein in conjunction with the BRE1A/BRE1B E3 ligase (also known as RNF20/RNF40) (7). Mono-ubiquitinated histone H2B Lys120 is associated with the transcribed region of active genes and stimulates transcriptional elongation by facilitating FACT-dependent chromatin remodeling (7-9). In addition, it is essential for subsequent methylation of histone H3 Lys4 and Lys79, two additional histone modifications that regulate transcriptional initiation and elongation (10). In response to metabolic stress, AMPK is recruited to responsive genes and phosphorylates histone H2B at Lys36, both at promoters and in transcribed regions of genes, and may regulate transcriptional elongation (11). In response to multiple apoptotic stimuli, histone H2B is phosphorylated at Ser14 by the Mst1 kinase (12). Upon induction of apoptosis, Mst1 is cleaved and activated by caspase-3, leading to global phosphorylation of histone H2B during chromatin condensation. Interestingly, histone H2B is rapidly phosphorylated at irradiation-induced DNA damage foci in mouse embryonic fibroblasts (13). In this case, phosphorylation at Ser14 is rapid, depends on prior phosphorylation of H2AX Ser139, and occurs in the absence of apoptosis, suggesting that Ser14 phosphorylation may have distinct roles in DNA-damage repair and apoptosis.

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

Application Methods: Western Blotting

Background: KSR1 (kinase supressor of Ras) was identified from a genetic screen in Drosophila and C. elegans as a component of the Ras signaling pathway (1). KSR1 has a putative carboxy-terminal kinase domain that lacks a key Lys residue for phospho-group transfer. Although reports indicate that ceramide and EGF activate KSR1 (2,3), other evidence demonstrates that KSR1 regulates Raf in a kinase-independent manner (4,5). It is now widely accepted that KSR1 functions as a scaffold that binds MEK1/2 and 14-3-3 protein constitutively and binds ERK1/2 in a Ras activation-dependent manner (1,5,6). HSP70/HSP90 and p50 Cdc37 associate with the KSR1 complex to ensure its stability (5). Multiple phosphorylation sites have been identified: Ser297 and Ser392 mediate 14-3-3 binding, and putative MAPK phosphorylation sites include Thr260, Thr274 and Ser443 (6). C-TAK1 (Cdc25C-associated kinase 1) binds and phosphorylates KSR1 at Ser392 in quiescent cells (7). In response to stimuli, Ser392 is dephosphorylated by PP2A, which leads to ERK1/2 association and allows the KSR1 complex to translocate from cytosol to membrane, where the MAPK pathway is activated (8). IMP, a Ras-responsive E3 ubiquitin ligase, is also involved in interaction with KSR1 and may regulate its localization and stability (9). Very high expression levels of KSR1 inhibit MAPK signaling, whereas physiological levels promote MAPK signaling, indicating that the scaffold protein can turn signaling "on" or "off" depending on the scaffold concentration (10).

$293
100 µl
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), 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.

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Glycogen synthase kinase-3 (GSK-3) was initially identified as an enzyme that regulates glycogen synthesis in response to insulin (1). GSK-3 is a ubiquitously expressed serine/threonine protein kinase that phosphorylates and inactivates glycogen synthase. GSK-3 is a critical downstream element of the PI3K/Akt cell survival pathway whose activity can be inhibited by Akt-mediated phosphorylation at Ser21 of GSK-3α and Ser9 of GSK-3β (2,3). GSK-3 has been implicated in the regulation of cell fate in Dictyostelium and is a component of the Wnt signaling pathway required for Drosophila, Xenopus, and mammalian development (4). GSK-3 has been shown to regulate cyclin D1 proteolysis and subcellular localization (5).

$262
3 nmol
300 µl
SignalSilence® Atg7 siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit Atg7 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: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). Autophagy is generally activated by conditions of nutrient deprivation but has also been associated with a number of physiological processes including development, differentiation, neurodegeneration, infection, and cancer (3). The molecular machinery of autophagy was largely discovered in yeast and referred to as autophagy-related (Atg) genes. Formation of the autophagosome involves a ubiquitin-like conjugation system in which Atg12 is covalently bound to Atg5 and targeted to autophagosome vesicles (4-6). This conjugation reaction is mediated by the ubiquitin E1-like enzyme Atg7 and the E2-like enzyme Atg10 (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: PCK2 (PEPCK2 or PEPCK-M) encodes an isoform of phosphoenolpyruvate carboxykinase (PEPCK) that is found in the mitochondria of renal and hepatic tissues (1). PEPCK is involved in gluconeogenesis, the process of generating glucose from non-carbohydrate substrates such as lactate and glycerol (2). PEPCK catalyzes the reaction whereby oxaloacetate becomes phosphoenolpyruvate, a rate limiting step in the metabolic process (2). The predominant function of PCK2 is to process the lactate that is continually produced by red blood cells in the liver and kidney (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The placenta-specific gene 8 (Plac8) encodes a chromatin-binding protein that was first identified from placenta and that is highly expressed in plasmacytoid dendritic cells (1,2). Research studies indicate that Plac8 plays a role in immune function and is essential in the differentiation of brown fat (3,4). During brown fat differentiation, Plac8 interacts with the transcription factor C/EBPβ at its promoter sequence to activate the transcription of C/EBPβ (4). Experimental deletion of Plac8 in mice leads to impaired innate immune function, abnormal brown fat function, cold intolerance, and obesity (3,4). Additional studies examining the spread of colorectal carcinoma suggest a possible role for Plac8 in cancer invasion, possibly through promoting the epithelial-to-mesenchymal transition seen during tumor progression (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Nucleotide excision repair (NER) is a process by which cells identify and repair DNA lesions that result from chemical and radiation exposure (1). The DNA binding protein XPA is an essential part of a pre-incision complex that forms at sites of damage, and is necessary for the initiation of nucleotide excision repair (2). XPA is one of eight NER proteins (XPA-G, XPV) encoded by genes that are defective in cases of xeroderma pigmentosum, a disorder characterized by sensitivity to sunlight, predisposition to exposed tissue cancers, and neurological defects in some patients (3). Activation of XPA follows phosphorylation at Ser196 and results in increased NER activity. Phosphorylation of XPA at Ser196 is induced by UV exposure in an ATR-dependant fashion (4) and promotes nuclear accumulation of XPA (5). Research studies suggest that XPA may be a direct substrate of the serine/threonine kinase ATR (4) and that NER activity may be negatively regulated through dephosphorylation of Ser196 by the phosphatase WIP1 (6).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Modulation of chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of DNA wound around eight core histone proteins (two each of H2A, H2B, H3, and H4), is the primary building block of chromatin (1). The amino-terminal tails of core histones undergo various post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (2-5). These modifications occur in response to various stimuli and have a direct effect on the accessibility of chromatin to transcription factors and, therefore, gene expression (6). In most species, histone H2B is primarily acetylated at Lys5, 12, 15, and 20 (4,7). Histone H3 is primarily acetylated at Lys9, 14, 18, 23, 27, and 56. Acetylation of H3 at Lys9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms (2,3). Phosphorylation at Ser10, Ser28, and Thr11 of histone H3 is tightly correlated with chromosome condensation during both mitosis and meiosis (8-10). Phosphorylation at Thr3 of histone H3 is highly conserved among many species and is catalyzed by the kinase haspin. Immunostaining with phospho-specific antibodies in mammalian cells reveals mitotic phosphorylation at Thr3 of H3 in prophase and its dephosphorylation during anaphase (11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: p38 MAP kinase (MAPK), also called RK (1) or CSBP (2), is the mammalian orthologue of the yeast HOG kinase that participates in a signaling cascade controlling cellular responses to cytokines and stress (1-4). Four isoforms of p38 MAPK, p38α, β, γ (also known as Erk6 or SAPK3), and δ (also known as SAPK4) have been identified. Similar to the SAPK/JNK pathway, p38 MAPK is activated by a variety of cellular stresses including osmotic shock, inflammatory cytokines, lipopolysaccharide (LPS), UV light, and growth factors (1-5). MKK3, MKK6, and SEK activate p38 MAPK by phosphorylation at Thr180 and Tyr182. Activated p38 MAPK has been shown to phosphorylate and activate MAPKAP kinase 2 (3) and to phosphorylate the transcription factors ATF-2 (5), Max (6), and MEF2 (5-8). SB203580 (4-(4-fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(4-pyridyl)-imidazole) is a selective inhibitor of p38 MAPK. This compound inhibits the activation of MAPKAPK-2 by p38 MAPK and subsequent phosphorylation of HSP27 (9). SB203580 inhibits p38 MAPK catalytic activity by binding to the ATP-binding pocket, but does not inhibit phosphorylation of p38 MAPK by upstream kinases (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Abi1, Abi2 and Abi3 are members of the Abl1 interactor family, which function as adaptor signaling molecules down stream of the receptor tyrosine kinase Ab1 (1-3). In addition to Abl, Abi1 has been shown to interact with the important signaling transducers WAVE and p85PI3K to regulate cytoskeletal and growth signaling (4,5). Along its sequences, Abi1 has multiple modules for carrying on these interactions. It has a WAVE binding domain, which allows it to interact with WAVE, a homeo-domain/PEST domain, which, when phosphorylated can acts as a docking site for SH2 binding, a PXXP sequence to interact with the SH3 domain of Abl, and a C-terminal SH3 domain for interaction with the proline rich region of Ab1 (4,5). Abl can phosphorylate Abi1 on Y213 (6), the phosphorylated sequence serves as a docking site for both the SH2 domain of Abl and the SH2 domain of p85PI3K (7). Another important phosphorylation site for Abi1 is Y435. Phosphorylation of Abi1 at Y435 promotes tumor cell adhesion and invasion (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: 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
Human

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

Background: The coxsackie virus and adenovirus receptor (CXADR, CAR) is a highly conserved, single-transmembrane glycoprotein and the primary receptor to mediate cellular attachment and infection of coxsackie B viruses and most adenoviruses (1,2). The CAR protein contains a pair of Ig-like domains within the amino-terminal extracellular domain and a carboxyl-terminal PDZ motif (1). Research studies indicate that CAR is a tight junction protein that associates with the ZO-1 scaffold protein and promotes both cell adhesion and restriction of solute and ion movement between cells (2). Endogenous CAR is targeted to the basolateral plasma membrane by a tyrosine-based basolateral sorting signal and clathrin adaptors AP-1A and AP-1B (3). CAR binds junctional adhesion molecule L (JAML) on epithelial cells and neutrophils where it activates PI3K and downstream MAPK kinases to stimulate epithelial γδ T cell proliferation and increase production of TNFα and keratinocyte growth factor (4-6). As a result, the CAR protein plays a potentially critical role in adenoviral gene therapy, immunity, wound repair, inflammation, and cancer therapy (4-6). Additional studies demonstrate that CAR is essential in regulating squamous carcinoma cell growth (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunohistochemistry (Paraffin)

Background: The family of Trk receptor tyrosine kinases consists of TrkA, TrkB, and TrkC. While the sequence of these family members is highly conserved, they are activated by different neurotrophins: TrkA by NGF, TrkB by BDNF or NT4, and TrkC by NT3 (1). Neurotrophin signaling through these receptors regulates a number of physiological processes, such as cell survival, proliferation, neural development, and axon and dendrite growth and patterning (1). In the adult nervous system, the Trk receptors regulate synaptic strength and plasticity. TrkA regulates proliferation and is important for development and maturation of the nervous system (2). Phosphorylation at Tyr490 is required for Shc association and activation of the Ras-MAP kinase cascade (3,4). Residues Tyr674/675 lie within the catalytic domain, and phosphorylation at these sites reflects TrkA kinase activity (3-6). Point mutations, deletions, and chromosomal rearrangements (chimeras) cause ligand-independent receptor dimerization and activation of TrkA (7-10). TrkA is activated in many malignancies including breast, ovarian, prostate, and thyroid carcinomas (8-13). Research studies suggest that expression of TrkA in neuroblastomas may be a good prognostic marker as TrkA signals growth arrest and differentiation of cells originating from the neural crest (10).

$262
3 nmol
300 µl
SignalSilence® Atg5 siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit Atg5 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: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). Autophagy is generally activated by conditions of nutrient deprivation but has also been associated with a number of physiological processes including development, differentiation, neurodegeneration, infection, and cancer (3). The molecular machinery of autophagy was largely discovered in yeast and referred to as autophagy-related (Atg) genes. Formation of the autophagosome involves a ubiquitin-like conjugation system in which Atg12 is covalently bound to Atg5 and targeted to autophagosome vesicles (4-6). This conjugation reaction is mediated by the ubiquitin E1-like enzyme Atg7 and the E2-like enzyme Atg10 (7,8).

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

Application Methods: Western Blotting

Background: Erk3, also known as MAPK6 or p97 MAPK, is almost 50% identical to Erk1/2 at the kinase domain located in its amino-terminal region (1). However, Erk3 is distinguished from other MAP kinases in that it lacks the conserved TXY motif in its activation loop, possessing instead an SEG motif (1,2). Phosphorylation at Ser189 in the SEG motif has been reported (2,3). With limited information about its upstream kinases and downstream substrates, the significance of this phosphorylation remains to be elucidated (3,4). Erk3 is an inherently unstable protein, rapidly degraded through amino-terminal ubiquitination and proteasome degradation (3,5). A site-specific cleavage, depending on a short stretch of acidic residues of Erk3, might regulate its translocation from the Golgi/ERGIC to the nucleus during the cell cycle (6). Accumulating evidence suggests that Erk3 is involved in cell differentiation (1,3,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Stem cell factor (SCF) is a growth factor that is essential for hematopoiesis, melanogenesis and fertility. SCF is also known as mast cell growth factor (MCGF), steel factor (SLF), or kit ligand (KL) (1-3). SCF mediates its biological effects by binding to and activating c-Kit (4). SCF induces dimerization of c-Kit followed by trans-autophosphorylation of the cytoplasmic protein tyrosine kinase domain, leading to subsequent recruitment of signaling proteins, tyrosine phosphorylation of substrates and activation of multiple signaling pathways (5,6). SCF/c-Kit may take part in the growth control of human malignancies (7).

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

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

Background: DDX6, also known as RCK and p54, was identified as a proto-oncogene product and is a member of the ATP-dependent DEAD box helicase family (1,2). This protein interacts with translation initiation factor eIF4E in the cytoplasmic P-bodies (3) and represses mRNA translation (4). DDX6 is a component of the miRNA induced silencing complex (miRISC) and interacts with Argonaute 1 (Ago1) and Argonaute 2 (Ago2) proteins in vitro and in vivo (5), functioning in miRNA-mediated translational repression (5). Depletion of DDX6 leads to the disruption of cytoplasmic P-bodies indicating that it is required for P-body formation (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Vacuole membrane protein 1 (VMP1, TMEM49) is a transmembrane protein localized to intracellular vacuoles that was originally described as a protein promoting vacuole formation in acinar cells associated with acute pancreatitis (1). Over-expression of VMP1 promotes vacuole formation and subsequent cell death (1). Additional research studies demonstrated that VMP1 expression might be induced by starvation or the mTOR inhibitor rapamycin, which triggers autophagy (2). VMP1 is targeted along with LC3 to autophagosome membranes (2). Knockdown of VMP1 can inhibit autophagosome formation (2). VMP1 interacts with beclin-1, a key autophagy protein that activates the class III PI3 kinase Vps34 (3). VMP1 functions in the degradation and clearance of zymogen-containing vacuoles during experimentally induced pancreatitis (4). During vacuole degradation and clearance, VMP1 interacts with the ubiquitin protease USP9X, suggesting a possible functional link between the molecular machinery of autophagy and the ubiquitin pathway. Orthologs of VMP1 from C. elegans (known as EPG-3), Drosophila (known as TANGO-5), and Dictyostelium, have been shown to play a role in membrane trafficking, organelle organization, and autophagy (5-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The megakaryoblastic leukemia proteins 1 and 2 (MKL1, MKL2) are myocardin-related transcription factors (MRTF-A, MRTF-B) that serve as actin-regulated transcription coactivators for the serum response factor (SRF). Interaction between G-actin and MKL proteins retains the coactivator within the cytoplasm of resting cells. Activated Rho-A promotes F-actin assembly and a reduction of the G-actin pool in serum-stimulated cells. This results in the accumulation of MKL proteins in the nucleus, where the coactivator associates with the SRF to activate target gene transcription and mediate multiple cellular processes (1-4). A number of other signaling pathways, including the TGFβ, BMP, and PDGF pathways, also make use of MKL-mediated activation of target gene transcription (5-9). Chromosomal translocations involving the genes encoding MKL1 and MKL2 have been identified in several cases of acute megakaryoblastic leukemia and chondroid lipoma (10-12).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: TFIIB (also known as GTF2B, TF2B and general transcription factor IIB) is a ubiquitously expressed transcription factor that plays a central role in the assembly of the transcription pre-initiation complex through direct recruitment of RNA polymerase II (1,2). TFIIB functions as a bridge between promoter-bound TFIID and RNA polymerase II. In addition to interacting with promoter-bound TFIID and TFIIA, TFIIB makes extensive contacts with the core promoter via two independent DNA-binding modules. TFIIB may also be a target of transcriptional activator proteins that act to stimulate pre-initiation complex assembly.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Members of the SALL gene family encode putative zinc finger transcription factors highly expressed during development (1). Sall4 is expressed very early in development with other pluripotency regulators, such as Oct-4 and Nanog (2). Recent studies suggest Sall4 works as a master regulator that controls its own expression and the expression of Oct-4 in a transcriptional regulation feedback loop governing stem cell pluripotency and stem cell fate (2,3). Immunohistochemical studies indicate that Sall4 is a sensitive and specific diagnostic marker for primary germ cell tumors and yolk sac tumors (4,5). Research studies have shown that Sall4 is constitutively expressed in acute myeloid leukemia (AML) and is a probable effector of the Wnt/β-catenin signaling pathway in this disease (6). In addition, mutations in Sall4 have been implicated in human malformation syndromes including Duane-radial ray syndrome (Okihiro syndrome) and Acro-renal-ocular syndrome (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: A total of fifteen mammalian DNA polymerase enzymes catalyze the synthesis of nascent DNA during DNA replication and repair (1). DNA polymerase eta (POL η, POLH, Rad30) is one of a specialized type of DNA polymerases that function in DNA repair and translesion synthesis (TLS). POLH can accommodate and read through bulky DNA lesions such as pyrimidine dimers, which allows for continued DNA synthesis past lesions and limited stalling of replication forks (2,3). Damage inducing conditions, such as exposure to UV light or cisplatin, recruit POLH to sites of bulky DNA lesions where the polymerase interacts with PCNA (4,5). Mutations in the human POLH gene can result in a form of xeroderma pigmentosum (XPV), an autosomal recessive disorder characterized by hypersensitivity to light and susceptibility to skin cancer (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Tyrosine-protein phosphatase non-receptor type-14 (PTPN14, Pez, PTPD2 and PTP36) is an evolutionarily conserved non-membrane tyrosine phosphatase with homology to the band 4.1 family of proteins (1-3). The PTPN14 protein contains an amino-terminal FERM (4.1-ezrin-radixin-moesin) domain, which suggests plasma membrane localization of the protein, and a carboxy-terminal protein tyrosine phosphatase (PTP) domain (4). Research studies have identified possible roles for PTPN14 in multiple, diverse signaling pathways, including cell growth and proliferation, cell migration and adhesion, and development. The PTPN14 phosphatase regulates the subcellular localization of YAP in a cell density-dependent manner, indicating a role for PTPN14 in the Hippo signaling pathway (5). The Drosophila PTPN14 homolog Pez localizes to adherens junctions, where it may regulate cell motility through dephosphorylation of β-catenin (3). PTPN14 may play a role in epithelial-mesenchymal transition through effects on the TGF-β signaling pathway (6), and interacts with VEGFR3, a receptor tyrosine kinase involved in lymphangiogenesis (7). Loss-of-function mutations in the PTPN14 gene are associated with colorectal cancer (8), and choanal atresia and lymphedema, an autosomal recessive disorder characterized by defects in both nasal passage development and lymphangiogenesis (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Podoplanin (aggrus, glycoprotein 36) is a single-pass transmembrane protein belonging to the type-1 family of sialomucin-like glycoproteins. Podoplanin was first described in the rat as a surface glycoprotein that regulated podocyte morphology (1). It is now commonly used as a marker of lymphatic endothelial cells, where its expression is associated with the process of lymphangiogenesis (2). Its role in this regard is presumably due to its putative involvement in regulating actin cytoskeleton dynamics (3). Research studies have shown that podoplanin expression is upregulated in a number of tumor types including colorectal cancers (4), oral squamous cell carcinomas (5), and germ cell tumors (6), with higher expression levels often associated with more aggressive tumors (7). Research studies have suggested a functional role for podoplanin in the stromal microenvironment of tumors. For example, it has been reported that podoplanin expression in cancer-associated fibroblasts (CAFs) is positively associated with a stromal environment that promotes cancer progression (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Western Blotting

Background: Troponin, working in conjunction with tropomyosin, functions as a molecular switch that regulates muscle contraction in response to changes in the intracellular Ca2+ concentration. Troponin consists of three subunits: the Ca2+-binding subunit troponin C (TnC), the tropomyosin-binding subunit troponin T (TnT), and the inhibitory subunit troponin I (TnI) (1). In response to β-adrenergic stimulation of the heart, Ser23 and Ser24 of TnI (cardiac) are phosphorylated by PKA and PKC. This phosphorylation stimulates a conformational change of the regulatory domain of TnC, reduces the association between TnI and TnC, and decreases myofilament Ca2+ sensitivity by reducing the Ca2+ binding affinity of TnC (1-3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, 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).