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Product listing: Toll-like Receptor 9 Antibody, UniProt ID Q9NR96 #2254 to α/β-Synuclein (Syn205) Mouse mAb, UniProt ID P37840 #2644

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Members of the Toll-like receptor (TLR) family, named for the closely related Toll receptor in Drosophila, play a pivotal role in innate immune responses (1-4). TLRs recognize conserved motifs found in various pathogens and mediate defense responses (5-7). Triggering of the TLR pathway leads to the activation of NF-κB and subsequent regulation of immune and inflammatory genes (4). The TLRs and members of the IL-1 receptor family share a conserved stretch of approximately 200 amino acids known as the Toll/Interleukin-1 receptor (TIR) domain (1). Upon activation, TLRs associate with a number of cytoplasmic adaptor proteins containing TIR domains, including myeloid differentiation factor 88 (MyD88), MyD88-adaptor-like/TIR-associated protein (MAL/TIRAP), Toll-receptor-associated activator of interferon (TRIF), and Toll-receptor-associated molecule (TRAM) (8-10). This association leads to the recruitment and activation of IRAK1 and IRAK4, which form a complex with TRAF6 to activate TAK1 and IKK (8,11-14). Activation of IKK leads to the degradation of IκB, which normally maintains NF-κB in an inactive state by sequestering it in the cytoplasm.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Integrins are α/β heterodimeric cell surface receptors that play a pivotal role in cell adhesion and migration, as well as in growth and survival (1,2). The integrin family contains at least 18 α and 8 β subunits that form 24 known integrins with distinct tissue distribution and overlapping ligand specificities (3). Integrins not only transmit signals to cells in response to the extracellular environment (outside-in signaling), but also sense intracellular cues to alter their interaction with the extracellular environment (inside-out signaling) (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The 25 kDa synaptosome-associated protein (SNAP25) is a target membrane soluble, N-ethylmaleimide-sensitive factor attachment protein receptor (t-SNARE) that is found on neuronal presynaptic membranes. SNAP25 forms a core complex with the SNARE proteins syntaxin and synaptobrevin to mediate synaptic vesicle fusion with the plasma membrane during Ca2+-dependent exocytosis (1). This complex is responsible for exocytosis of the neurotransmitter γ-aminobutyric acid (GABA). Neurotransmitter release is inhibited by proteolysis of SNAP25 by botulinum toxins A and E (2). SNAP25 plays a secondary role as a Q-SNARE involved in endosome fusion; the protein is associated with genetic susceptibility to attention-deficit hyperactivity disorder (ADHD) (3).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: CCT2 is one of eight largely unrelated subunit proteins found in a protein chaperone complex known as the chaperonin-containing TCP-1 (CCT) or TRiC complex. The CCT complex is an abundanct cytoslic component that is credited with helping newly synthesized polypeptides adopt the correct conformation (1). Proteins that fold and assemble with the help of CCT include the cytoskeletal proteins actin and tubulin as well as up to 15% of newly synthesized eukaryotic proteins (2). CCT2 is the β-subunit of the chaperone complex and is one of several CCT proteins that exhibit increased expression in response to stress. This implies that the CCT complex helps cells recover from protein damage by assisting in protein folding and assembly (3). CCT subunit levels also change throughout the cell cycle, with lower proteins levels (and reduced chaperone activity) found during induced cell cycle arrest during at M phase (4). Each CCT subunit is thought to perform a specific function during protein folding and assembly (5); CCT2 exhibits both actin and tubulin binding activities (6,3) but the exact molecular function on this subunit remains uncertain.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Homer1, Homer2 and Homer3 are scaffolding proteins, composed of an EVH protein–binding domain, a coiled-coil domain and a leucine zipper domain. The EVH domain is a protein-protein binding module that binds to the proline-rich motifs PPXXF, PPXF, and LPSSP of G protein–coupled receptors (GPCRs), inositol 1,4,5-triphosphate (IP3) receptors (IP3Rs), ryanodine receptors, and TRP channels (1-2). The coiled-coil and the leucine zipper domains cause multimerization of Homers and assemble signaling proteins complexes. The Homer1 gene encodes a short isoform (Homer1a, aa 1-186) and two long isoforms (Homer1b, aa 1-354; Homer1c, aa 1-366). Homer1a lacks the coiled-coil domain and leucine zipper, antagonizing multimerization of Homers and thus disassembling signaling proteins complexes (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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
Human

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

Background: DSS-AHC critical region on the X chromosome protein 1 (DAX1) is an orphan nuclear receptor encoded by the nuclear receptor subfamily 0 group B member 1 (NR0B1) gene. DAX1 possesses an atypical DNA binding domain that allows it to form heterodimeric complexes with DNA binding partners and repress transcriptional activity (1,2). During development, DAX1 is important for establishment of the hypothalamic-pituitary-adrenal gonadal axis. The receptor is essential for development of several important hormone-producing organs that determine this axis, including the adrenal glands, pituitary, hypothalamus, and the male and female reproductive organs (3,4). Research studies suggest that DAX1 plays a role in maintenance of pluripotency in embryonic stem cells (5,6). Loss of DAX1 function through deletion or mutation results in adrenal insufficiency and hypogonadotropic hypogonadism (7), while duplication of the NR0B1 gene on the X-chromosome causes dosage-sensitive sex reversal (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Coat Protein Complex II (COPII) is composed of five cytosolic proteins: Sec23/24 complex, Sec13/31 complex, and Sar1. COPII coat is located at the ER/Golgi interface and is involved in transport of newly synthesized proteins from the ER to the Golgi apparatus (1). COPII formation is initiated through the binding of the activated G protein, Sar1, to the Sec23/24 complex, thereby forming a prebudding complex that directly binds target molecules (1-3). The prebudding complex further recruits Sec13/31 to form mature COPII coat (4,5). The Sec24 subunit of COPII coat is thought to play a critical role in cargo selection (2,6). It binds directly to cargo proteins at the ER and brings them to COPII vesicles through interaction with Sec23. There are four Sec24 isoforms in human cells: Sec24A, Sec24B, Sec24C, and Sec24D (7). In mice, mutations in Sec24B have been linked to developmental defects (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

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 is also 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 is directed by a number of autophagy-related (Atg) genes. These proteins are involved in the formation of autophagosomes, which are cytoplasmic vacuoles that are delivered to lysosomes for degradation. The class III type phosphoinositide 3-kinase (PI3K) Vps34 regulates vacuolar trafficking and autophagy (4,5). Multiple proteins associate with Vps34, including p105/Vps15, Beclin-1, UVRAG, Atg14, and Rubicon (6-12). Atg14 and Rubicon were identified based on their ability to bind to Beclin-1 and participate in unique complexes with opposing functions (9-12). Rubicon, which localizes to the endosome and lysosome, inhibits Vps34 lipid kinase activity; knockdown of Rubicon enhances autophagy and endocytic trafficking (11,12). In contrast, Atg14 localizes to autophagosomes, isolation membranes, and ER and can enhance Vps34 activity. Knockdown of Atg14 inhibits starvation-induced autophagy (11,12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Hypoxia-inducible factor 1 (HIF1) is a heterodimeric transcription factor that plays a critical role in the cellular response to hypoxia (1). The HIF1 complex consists of two subunits, HIF-1α and HIF-1β, which are basic helix-loop-helix proteins of the PAS (Per, ARNT, Sim) family (2). HIF1 regulates the transcription of a broad range of genes that facilitate responses to the hypoxic environment, including genes regulating angiogenesis, erythropoiesis, cell cycle, metabolism, and apoptosis. The widely expressed HIF-1α is typically degraded rapidly in normoxic cells by the ubiquitin/proteasomal pathway. Under normoxic conditions, HIF-1α is proline hydroxylated leading to a conformational change that promotes binding to the von Hippel Lindau protein (VHL) E3 ligase complex; ubiquitination and proteasomal degradation follows (3,4). Both hypoxic conditions and chemical hydroxylase inhibitors (such as desferrioxamine and cobalt) inhibit HIF-1α degradation and lead to its stabilization. In addition, HIF-1α can be induced in an oxygen-independent manner by various cytokines through the PI3K-AKT-mTOR pathway (5-7).HIF-1β is also known as AhR nuclear translocator (ARNT) due to its ability to partner with the aryl hydrocarbon receptor (AhR) to form a heterodimeric transcription factor complex (8). Together with AhR, HIF-1β plays an important role in xenobiotics metabolism (8). In addition, a chromosomal translocation leading to a TEL-ARNT fusion protein is associated with acute myeloblastic leukemia (9). Studies also found that ARNT/HIF-1β expression levels decrease significantly in pancreatic islets from patients with type 2 diabetes, suggesting that HIF-1β plays an important role in pancreatic β-cell function (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein tyrosine kinase Pyk2, also called CAKβ, RAFTK and CADTK, is a nonreceptor tyrosine kinase structurally related to focal adhesion kinase (FAK) (1-4). Pyk2 is predominantly expressed in cells derived from hematopoietic lineages and in the central nervous system. Pyk2 is one of the signaling mediators for the G-protein-coupled receptors and MAP kinase signaling pathway. It plays an important role in cell spreading and migration (5-7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Dynamin is a family of large GTPases that has been implicated in the formation of vesicles of both the endocytotic and secretory processes (1). Dynamin plays an important role in the internalization of cell surface receptors, a process that attenuates the response to extracellular signals. It has been illustrated that dynamin interacts with signaling proteins such as Src, PLCγ, PKC and G-proteins. PKC and Src phosphorylate dynamin, and its phosphorylation may regulate the endocytosis of cell surface receptors (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: The transcription factor Th-inducing POZ/Krüppel-like factor (ThPOK, ZBTB7B, cKROX, ZFP67) is a transcriptional repressor belonging to the POK/ZBTB family of lymphoid cell development regulators (1). ThPOK is best known as a signature CD4+ Th cell transcription factor that is upregulated during the differentiation of CD4+ Th but not CD8+ cytotoxic T cells (1). Expression of ThPOK in developing T cells represses expression of CD8 and cytotoxic T cell effector genes, and indirectly promotes expression of CD4 by antagonizing RUNX-mediated CD4 repression (2-4). ThPOK expression has also been observed in NKT cells and γδ T cells (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: TKS5 (SH3PXD2A, FISH) is a scaffold protein expressed on invadosomes of both normal and transformed cell lines. Research studies suggest that TKS5 is functionally required for both the formation and invasive behavior of invadosomes (1, 2). TKS5 has an N-terminal PX domain that mediates invadosome initiation and localization of MMP-rich vesicles to the invadosome (3). TKS5 also has five SH3 domains, which recruit ADAM family proteinases to the invadosome to degrade extracellular matrix. These SH3 domains interact with adaptor proteins to facilitate F-actin polymerization during invadosome formation (4-6). Src tyrosine kinase has been shown to phosphorylate TKS5 at Tyr557 and Tyr619, which was shown to be necessary and sufficient for TKS5-mediated invadopia formation and invasion (7). Elevated TKS5 expression is positively associated with invasive behavior of cancer cells, suggesting TKS5 may have prognostic potential in cancer (8, 9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: The process of SUMO conjugation to target proteins is similar to the molecular chain of events observed with ubiquitin (1). SUMO is conjugated to target proteins through the coordinated action of the cellular SUMO conjugation machinery, which consists of the E1, E2, and E3 enzymes (2). The canonical SUMO E1 activating enzyme is a heterodimer consisting of Ubiquitin-like 1-activating enzyme E1A (UBLE1A, SAE1) and UBLE1B (SAE2, UBA2) subunits. Mature SUMO is activated by E1 in an ATP-dependent reaction that generates adenylated SUMO, which functions as a high-energy intermediate in the formation of a thioester linkage between SUMO and Cys173 of SAE2 (3,4). SUMO is subsequently transferred from SAE2 to the SUMO E2 conjugating enzyme UBE2I (5). Research studies indicate that UBLE1A (SAE1) is a nuclear protein and c-Myc transcriptional target whose expression is required for Myc-driven tumorigenesis (6-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: First identified as a pro-apoptotic protein that binds the cytoplasmic tail of the TNF receptor superfamily member CD27 (1), Siva-1 also binds several other TNFR family members including glucocorticoid-induced tumor necrosis factor receptor (GITR) and OX40 (1-3), as well as anti-apoptotic Bcl-2 family members Bcl-xL and Bcl-2 (4,5). Siva-1 is composed of a central death domain homology region, a C-terminal box-B-like ring finger followed by a zinc finger-like domain, and a unique N-terminal amphipathic helical region (SAH) (1,4). Studies have demonstrated that Siva-1 has the ability to induce cell death via both the extrinsic and intrinsic apoptotic pathways (1-8). The SAH domain of Siva-1 is responsible for the inhibition of the pro-survival activities of Bcl-xL and Bcl-2, leading to caspase-mediated cell death (4,5,8). Siva-1 plays a role in T cell signaling and homeostasis by inhibiting NF-κB activity, also resulting in apoptotic cell death (7,9). An alternative splice variant of Siva-1, Siva-2, lacks part of the SAH and death domains and is less effective at inducing apoptosis (1,2,5,8). Studies in xenografts have shown that down-regulation of Siva-1 inhibits tumorigenesis in response to p53 activation (10). Down-regulation of Siva-1 may also play a role in tumor metastasis through its regulation of the epithelial-mesenchymal transition (EMT) and cell migration (11). Overexpression of Siva-1 is implicated in several pathological conditions including acute ischemic injury (12) and Coxsackievirus infection (13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

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

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

Application Methods: Western Blotting

Background: CCAAT/enhancer-binding proteins (C/EBPs) are a family of transcription factors that are critical for cellular differentiation, terminal function, and inflammatory response (1). Six members of the family have been characterized (C/EBPα, β, δ, γ, ε, and ζ) and are distributed in a variety of tissues (1). Translation from alternative start codons results in two isoforms of C/EBPα (p42 and p30), which are both strong transcriptional activators (2). It has been reported that insulin and insulin-like growth factor-I stimulate the dephosphorylation of C/EBPα, which may play a key role in insulin-induced repression of GLUT4 transcription (3). Phosphorylation of C/EBPα at Thr222, Thr226, and Ser230 by GSK-3 seems to be required for adipogenesis (4).

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

Application Methods: Immunofluorescence (Frozen)

Background: The electroneutral cation-chloride-coupled co-transporter (SLC12) gene family comprises bumetanide-sensitive Na+/K+/Cl- (NKCC), thiazide-sensitive Na+/Cl-, and K+/Cl- (KCC) co-transporters. SLC12A1/NKCC2 and SLC12A2/NKCC1 regulate cell volume and maintain cellular homeostasis in response to osmotic and oxidative stress (1). The broadly expressed NKCC1 is thought to play roles in fluid secretion (i.e. salivary gland function), salt balance (i.e. maintenance of renin and aldosterone levels), and neuronal development and signaling (2-7). During neuronal development, NKCC1 and KCC2 maintain a fine balance between chloride influx (NKCC1) and efflux (KCC2), which regulates γ-aminobutyric acid (GABA)-mediated neurotransmission (3). Increased NKCC1 expression in immature neurons maintains high intracellular chloride levels that result in inhibitory GABAergic signaling; KCC2 maintains low intracellular chloride levels and excitatory GABAergic responses in mature neurons (4,5,8). Deletion of NKCC1 impairs NGF-mediated neurite outgrowth in PC-12D cells while inhibition of NKCC1 with bumetanide inhibits re-growth of axotomized dorsal root ganglion cells (6,7). Defective chloride homeostasis in neurons is linked to seizure disorders that are ameliorated by butemanide treatment, indicating that abnormal NKCC1 and NKCC2 expression or signaling may play a role in neonatal and adult seizures (9-12). NKCC1 is found as a homodimer or within heterooligomers with other SLC12 family members. This transport protein associates with a number of oxidative- and osmotic-responsive kinases that bind, phosphorylate, and activate NKCC1 co-transporter activity (13-16). In response to decreased intracellular chloride concentrations, Ste20-related proline-alanine-rich kinase (SPAK) phosphorylates NKCC1 to increase co-transporter activity and promote chloride influx (16-19). Oxidative stress response kinase 1 (OSR1) also phosphorylates and activates NKCC1 in response to oxidative stress (14).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: The Drosophila piwi gene was identified as being required for the self-renewal of germ-line stem cells (1). Piwi homologs are well conserved among various species including Arabidopsis, C. elegans, and human (1). Miwi and Mili proteins are both mouse homologs of Piwi and contain a C-terminal Piwi domain (2). Miwi and Mili bind to Piwi-interacting RNAs (piRNAs) in male germ cells and are essential for spermatogenesis in mouse (3-5).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Members of the Toll-like receptor (TLR) family, named for the closely related Toll receptor in Drosophila, play a pivotal role in innate immune responses (1-4). TLRs recognize conserved motifs found in various pathogens and mediate defense responses (5-7). Triggering of the TLR pathway leads to the activation of NF-κB and subsequent regulation of immune and inflammatory genes (4). The TLRs and members of the IL-1 receptor family share a conserved stretch of approximately 200 amino acids known as the Toll/Interleukin-1 receptor (TIR) domain (1). Upon activation, TLRs associate with a number of cytoplasmic adaptor proteins containing TIR domains, including myeloid differentiation factor 88 (MyD88), MyD88-adaptor-like/TIR-associated protein (MAL/TIRAP), Toll-receptor-associated activator of interferon (TRIF), and Toll-receptor-associated molecule (TRAM) (8-10). This association leads to the recruitment and activation of IRAK1 and IRAK4, which form a complex with TRAF6 to activate TAK1 and IKK (8,11-14). Activation of IKK leads to the degradation of IκB, which normally maintains NF-κB in an inactive state by sequestering it in the cytoplasm.

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

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

Background: Heterotrimeric guanine nucleotide-binding proteins (G proteins) consist of α, β and γ subunits and mediate the effects of hormones, neurotransmitters, chemokines, and sensory stimuli. To date, over 20 known Gα subunits have been classified into four families, Gα(s), Gα(i/o), Gα(q) and Gα(12), based on structural and functional similarities (1,2). Phosphorylation of Tyr356 of Gα(q)/Gα(11) is essential for activation of the G protein, since phenylalanine substitution for Tyr356 changes the interaction of Gα with receptors and abolishes ligand-induced IP3 formation (3).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: PEA-15 is a 15 kDa phosphoprotein expressed abundantly in astrocytes and fibroblasts as well as in tissues, including the lung and eye (1). The protein has been shown to coordinate cell growth, death, and glucose utilization (2-4). The amino-terminal DED domain of PEA-15 mediates its binding to FADD or Erk and further regulates the Erk and apoptosis signaling pathways. PEA-15 can be phosphorylated at two serine residues, Ser104 and Ser116, located within the carboxy terminus. Phosphorylation at these sites regulates binding to Erk and FADD (2,3).

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

Application Methods: Chromatin IP, Western Blotting

Background: SIN3 was originally identified as a negative regulator of transcription in budding yeast (1,2). Since then, three isoforms of the SIN3 proteins have been identified in mammalian cells, as products of two different genes, SIN3A and SIN3B (3,4). Both SIN3A and SIN3B are nuclear proteins that function as scaffolding subunits for the multi-subunit SIN3 transcriptional repressor complex, containing SIN3A or SIN3B, HDAC1, HDAC2, SDS3, RBBP4/RBAP48, RBBP7/RBAP46, SAP30, and SAP18 (3,4). SIN3 proteins contain four paired amphipathic alpha-helix (PAH) motifs that function in the recruitment of the SIN3 complex to target genes by binding a multitude of DNA-binding transcriptional repressor proteins, including Mad1, p53, E2F4, HCF-1, AML1, Elk-1, NRSF, CTCF, ERα, and MeCP2 (3,4). In addition, SIN3 proteins contain an HDAC interaction domain (HID), which mediates binding of HDAC1 and HDAC2 via the SDS3 bridging protein, and a highly conserved region (HCR) at the carboxy terminus, which contributes to repressor protein binding (3,4). RBBP4 and RBBP7 proteins also bind to SDS3 and contribute to nucleosome binding of the complex. The SIN3 complex functions to repress transcription, in part, by deacetylating histones at target gene promoters (3,4). In addition, recent studies have shown that SIN3 is recruited to the coding regions of repressed and active genes, where it deacetylates histones and suppresses spurious transcription by RNA polymerase II (3,5). In addition to histone deacetylase activity, the SIN3 complex associates with histone methyltransferase (ESET), histone demethylase (JARID1A/RBP2), ATP-dependent chromatin remodeling (SWI/SNF), methylcytosine dioxygenase (TET1), and O-GlcNAc transferase (OGT) activities, all of which appear to contribute to the regulation of target genes (5-9). The SIN3 complex is critical for proper regulation of embryonic development, cell growth and proliferation, apoptosis, DNA replication, DNA repair, and DNA methylation (imprinting and X-chromosome inactivation) (3,4).

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

Application Methods: Western Blotting

Background: The DNA mismatch repair system (MMR) repairs post-replication DNA, inhibits recombination between nonidentical DNA sequences, and induces both checkpoint and apoptotic responses following certain types of DNA damage (1). MSH2 (MutS homologue 2) forms the hMutS-α dimer with MSH6 and is an essential component of the mismatch repair process. hMutS-α is part of the BRCA1-associated surveillance complex (BASC), a complex that also contains BRCA1, MLH1, ATM, BLM, PMS2 proteins, and the Rad50-Mre11-NBS1 complex (2). Mutations in MSH6 and other MMR proteins have been found in a large proportion of hereditary nonpolyposis colorectal cancer (Lynch Syndrome), the most common form of inherited colorectal cancer in the Western world (3). Mutations in MSH6 have been shown to occur in glioblastoma in response to temozolomide therapy and to promote temozolomide resistance (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: LOX (lysyl oxidase) is a secreted copper-dependent amine oxidase and a member of the lysyl oxidase family (1). It primarily catalyzes the oxidation of lysine (or hydroxylysine) residues in collagen and elastin to form peptidyl aldehyde derivatives (2). These modifications are required for further cross-linking of target proteins to enhance ECM (extracellular matrix) stiffness. LOX plays critical roles in vascular, lung, and skin development, and tissue damage repair (3-5). Upregulation of LOX is associated with various diseases, including cancer progression and tissue fibrosis. Aberrant LOX activity creates a favorable tumor microenvironment to promote tumor metastasis and distal colonization (6-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Interferon-induced transmembrane protein (IFITM) family members are composed of short amino- and carboxy-termini, two transmembrane domains, and a cytoplasmic domain (1). There are four family members in humans: IFITM1, IFITM2, IFITM3, and IFITM5 (2,3). Mice have two additional family members, IFITM6 and IFITM7 (2,3). Basal expression of IFITM proteins is observed in some cells and expression can also be induced by type I and type II interferons (4-6). The primary function of IFITM family proteins appears to be viral restriction, as IFITM proteins inhibit cytosolic entry of viruses by preventing fusion of viral and host membranes (7,8). The mechanism by which IFITM proteins inhibit fusion is unclear. Although IFITM proteins are present on both the plasma membrane and intracellular membranes, they most effectively restrict viral fusion in late endosomes and lysosomes (8,9). In addition, different family members exhibit specific viral preferences (9). For example, IFITM3 is most effective at restricting influenza A infection, while IFITM1 is more successful in controlling filoviruses and SARS (9,10).

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

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

Background: α-Synuclein is a protein of 140-amino acids expressed abundantly in the brain. α-Synuclein is also the main component of pathogenic Lewy bodies and Lewy neurites. Research studies have shown that mutations of the α-synuclein gene are linked to Parkinson's disease (1).