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Product listing: TAZ (V386) Antibody, UniProt ID Q9GZV5 #4883 to Thioredoxin 1 Antibody (Mouse/Rat Preferred), UniProt ID P10599 #2298

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Chromatin IP, Western Blotting

Background: TAZ is a transcriptional co-activator with a PDZ-binding motif that is regulated by its interaction with 14-3-3 proteins (1). TAZ shares homology with the WW domain of Yes-associated protein (YAP) (1). TAZ is proposed to modulate the switch between proliferation and differentiation of mesenchymal stem cells (MSC) via interaction with transcription factors Runx2 and PPARγ. This process is critical to normal tissue development and the prevention of tumor formation. Due to its role in determination of MSC fate, TAZ may have clinical relevance to several human diseases caused by an imbalance of MSC differentiation (2,3). TAZ is negatively regulated via phosphorylation by LATS1/2, core kinases in the Hippo signaling pathway that controls stem cell development, tissue growth and tumor development (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: TBC1D1 is a paralog of AS160 (1) and both proteins share about 50% identity (2). TBC1D1 was shown to be a candidate gene for severe obesity (3). It plays a role in Glut4 translocation through its GAP activity (2,4). Studies indicate that TBC1D1 is highly expressed in skeletal muscle (1). Insulin, AICAR, and contraction directly regulate TBC1D1 phosphorylation in this tissue (1). Three AMPK phosphorylation sites (Ser231, Ser660, and Ser700) and one Akt phosphorylation site (Thr590) were identified in skeletal muscle (5). Muscle contraction or AICAR treatment increases phosphorylation on Ser231, Ser660, and Ser700 but not on Thr590; insulin increases phosphorylation on Thr590 only (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: TBC1D1 is a paralog of AS160 (1) and both proteins share about 50% identity (2). TBC1D1 was shown to be a candidate gene for severe obesity (3). It plays a role in Glut4 translocation through its GAP activity (2,4). Studies indicate that TBC1D1 is highly expressed in skeletal muscle (1). Insulin, AICAR, and contraction directly regulate TBC1D1 phosphorylation in this tissue (1). Three AMPK phosphorylation sites (Ser231, Ser660, and Ser700) and one Akt phosphorylation site (Thr590) were identified in skeletal muscle (5). Muscle contraction or AICAR treatment increases phosphorylation on Ser231, Ser660, and Ser700 but not on Thr590; insulin increases phosphorylation on Thr590 only (5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: TBK1 (TANK-binding kinase 1)/NAK (NF-κB activating kinase) is an IκB kinase (IKK)-activating kinase and can activate IKK through direct phosphorylation (1). TBK1 was identified through association with the TRAF binding protein, TANK, and found to function upstream of NIK and IKK in the activation of NF-κB (2). TBK1 induces IκB degradation and NF-κB activity through IKKβ. TBK1 may mediate IKK and NF-κB activation in response to growth factors that stimulate PKCε activity (1). TBK1 plays a pivotal role in the activation of IRF3 in the innate immune response (3).

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

Application Methods: Western Blotting

Background: TATA-binding protein (TBP) is a ubiquitously expressed nuclear protein that functions at the core of the general transcription factor protein complex TFIID (1-3). TFIID, which contains TBP and 13 TBP-associated factors (TAFs), contributes to the formation of the transcription pre-initiation complex, an assembly of multiple protein complexes (TFIIA, TFIIB, TFIIE, TFIIF, TFIIH, and RNA polymerase II) that bind to a gene promoter during the initiation of transcription (1-3). Once the pre-initiation complex is formed, RNA polymerase II becomes competent for elongation and transcribes the body of a gene. TBP functions in the recruitment of TFIID by binding to the TATA-box sequence found approximately 25 base pairs upstream of the transcription start site of many protein-coding genes. In addition, many transcriptional activator proteins interact with TBP and various TAF proteins to facilitate recruitment of TFIID and formation of the pre-initiation complex.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: The Elongin complex is a heterotrimer composed of TCEB3/Elongin A, Elongin B (TCEB2), and Elongin C (TCEB1) subunits (1-3). The Elongin complex regulates the rate of RNA polymerase II (RNAPII) transcription elongation by releasing the transient pausing of RNAPII at multiple sites along the DNA. TCEB3/Elongin A is the transcriptionally active subunit, while Elongin B and C subunits play a regulatory role (3,4). TCEB3/Elongin A may be required for expression of a subset of cell cycle regulated genes, and embryonic stem (ES) cells lacking TCEB3/Elongin A show abnormalities in cell size, growth, and cell cycle distribution (5). In addition, the Elongin complex has been shown to interact with the cullin family and RING finger proteins Cul5/Rbx2 upon UV-induced DNA damage, removing arrested RNAPII at sites of DNA damage by ubiquitination and degradation as part of an E3 ubiquitin ligase (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: TCL1 (T cell leukemia 1), MTCP1 and TCL1b belong to the TCL1 proto-oncogene family, and their products are involved in Akt activation during embryonic development, T cell leukemias, prolymphocytic leukemias and B cell lymphomas (1-3). The Akt association domain of TCL1 binds with the PH domain of Akt. The formation of an oligomeric TCL-Akt complex is required for TCL1 coactivator function and results in phosphorylation and activation of Akt . Furthermore, functional analysis indicates that the interaction between TCL1 and Akt promotes translocation of Akt to the nucleus (4-6). These findings are supported by the crystal structure of TCL1, which suggests that TCL1 may participate in molecular transport (7).

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

Application Methods: Western Blotting

Background: Translationally controlled tumor protein (TCTP/p23/HRF) is a ubiquitously expressed and highly conserved protein involved in various cellular processes, such as its role as a histamine releasing factor in chronic allergic disease (1). TCTP binds tubulin in a cell cycle dependent manner and is associated with the mitotic spindle (2). In addition, TCTP interacts with the actin cytoskeleton to regulate cell shape (3). In mitosis, TCTP is phosphorylated by PLK at Ser46, decreasing microtubule stability (4,5). TCTP interacts with the small GTPase Rheb, possibly acting as a GEF, thereby activating the TORC1 pathway and controlling cell growth and proliferation (6,7). TCTP has also been shown to be involved in apoptosis and cell stress (8-11). In cultured cells, reduction in TCTP expression can cause loss of the malignant phenotype (12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: TDP43 (TAR DNA-binding protein 43) is involved in transcriptional regulation and exon splicing (1,2). While normal TDP43 is a nuclear protein, pathological TDP43 is a component of insoluble aggregates in patients with frontotemporal lobar degeneration (FTLD) and amyotrophic lateral sclerosis (ALS). In these disorders, TDP43 is abnormally ubiquitinated, phosphorylated and cleaved to generate carboxy-terminal fragments that are sequestered as insoluble aggregates in neuronal nuclei, perikarya, and neurites (3,4). Additionally, TDP43 inhibits the expression of the HIV-1 gene and regulates CFTR gene splicing (1,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: TDP43 (TAR DNA-binding protein 43) is involved in transcriptional regulation and exon splicing (1,2). While normal TDP43 is a nuclear protein, pathological TDP43 is a component of insoluble aggregates in patients with frontotemporal lobar degeneration (FTLD) and amyotrophic lateral sclerosis (ALS). In these disorders, TDP43 is abnormally ubiquitinated, phosphorylated and cleaved to generate carboxy-terminal fragments that are sequestered as insoluble aggregates in neuronal nuclei, perikarya, and neurites (3,4). Additionally, TDP43 inhibits the expression of the HIV-1 gene and regulates CFTR gene splicing (1,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The Hippo pathway is an important evolutionarily conserved signaling pathway that controls organ size and tumor suppression by inhibiting cell proliferation and promoting apoptosis (1,2). An integral function of the Hippo pathway is to repress the activity of Yes-associated protein (YAP), a proposed oncogene whose activity is regulated by phosphorylation and subcellular localization (3,4). When the Hippo pathway is turned off, YAP is phosphorylated and translocates to the nucleus where it associates with various transcription factors including members of the transcriptional enhancer factor (TEF) family, also known as the TEA domain (TEAD) family (TEAD1-4) (5,6). Although widely expressed in tissues, the TEAD family proteins have specific tissue and developmental distributions. YAP/TEAD complexes regulate the expression of genes involved in cell proliferation and apoptosis (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Tec kinase belongs to a structurally related subfamily of protein tyrosine kinases (PTKs) that includes Btk, Itk (also known as Emt or Tsk), Bmx, and Txk (or Rlk) (1). With the exception of Txk, the members of this subfamily possess a long amino-terminal region consisting of a pleckstrin homology (PH) domain and a Tec homology (TH) domain . Because PH domains bind phosphoinositides with high affinity, the Tec family kinases have been proposed to act downstream of phosphatidylinositol 3-kinase (PI3-kinase) in signaling pathways. Binding of the PH domain with phosphoinositides is probably required for targeting of Tec family kinases to the cell membrane (2). Tec kinase is activated in response to many upstream signaling events including antigen receptor, RTK, GPCR, and integrin stimulation (3,4). Activated Tec kinase directly phosphorylates substrates such as PLC-gamma 2 and BRDG1 docking protein (5) and mediates downstream signaling.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Tensin 2 belongs to the Tensin family of cytoskeletal proteins that includes Tensin 1-3 and Cten, which couple integrins to the actin cytoskeleton (1). Tensin proteins contain SH2 and phosphotyrosine binding (PTB) domains, which enable interaction with diverse signaling molecules and proteins. Tensin family proteins play important roles in signal transduction, cell proliferation, and motility (2-5).Tensin 2 is localized to focal adhesions of various tissues with highest expression in the heart, kidney, and liver (6,7). Tensin 2 inhibits Akt/PKB signaling via a phosphatase tensin-type domain (8). However, Tensin 2 also mediates thrombopoietin/c-Mpl signaling, which promotes Akt signaling (9). Interaction with Tensin 2 is essential for the tumor suppressor function of Deleted in Cancer 1 (DLC1) (10-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Methylation of DNA at cytosine residues is a heritable, epigenetic modification that is critical for proper regulation of gene expression, genomic imprinting, and mammalian development (1,2). 5-methylcytosine is a repressive epigenetic mark established de novo by two enzymes, DNMT3a and DNMT3b, and is maintained by DNMT1 (3, 4). 5-methylcytosine was originally thought to be passively depleted during DNA replication. However, subsequent studies have shown that Ten-Eleven Translocation (TET) proteins TET1, TET2, and TET3 can catalyze the oxidation of methylated cytosine to 5-hydroxymethylcytosine (5-hmC) (5). Additionally, TET proteins can further oxidize 5-hmC to form 5-formylcytosine (5-fC) and 5-carboxylcytosine (5-caC), both of which are excised by thymine-DNA glycosylase (TDG), effectively linking cytosine oxidation to the base excision repair pathway and supporting active cytosine demethylation (6,7). TET2 is the most frequently mutated gene in myeloid dysplastic syndrome (MDS), a dysplasia of myeloid, megakaryocytic, and/or erythroid cell lineages, of which 30% progress to acute myeloid leukemia (AML) (8, 9). It is also mutated in diffuse large B-cell lymphoma (10). TET2 protein expression is often reduced in solid tumors such as prostate cancer, melanoma, and oral squamous cell carcinoma (11-13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: TFAM (Transcription Factor A, Mitochondrial; aka TCF6) is a member of the high-mobility group (HMG) proteins because it contains two HMG boxes. TFAM is a transcription factor for mitochondrial DNA (mtDNA), and enhances mtDNA transcription in a promoter-specific fashion in the presence of mitochondrial RNA polymerase and transcription factor B (1). Because the majority of ATP production depends on the mitochondrial respiratory chain, maintenance of the mitochondrial genome is critical for normal health. TFAM plays an essential role in the maintenance of mtDNA and thus, ATP production (2). TFAM binds to mtDNA both nonspecifically and in a sequence-specific manner. It is known to have a dual effect on mtDNA: protection of mtDNA and initiation of transcription from mtDNA (3). TFAM attenuates age-dependent impairment of the brain by preventing oxidative stress and mitochondrial dysfunctions in microglia (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Transcription factor E3 (TFE3) is a member of a family of basic helix-loop-helix leucine zipper transcription factors that includes MITF, TFEB, TFE3, and TFEC. Members of this family form heterodimers with each other, bind the same DNA sequences, and undergo the same types of post-translational modifications, including sumoylation (1). Research studies indicate that TFE3 and other family members play roles in development, organelle biogenesis, nutrient sensing, autophagy, and energy metabolism (2,3). Additional studies report that TFE3 controls the gate for pluripotent cells to exit the state of pluripotency prior to differentiation (4). Translocations involving the TFE3 gene region have been identified in a number of tumors, including sporadic renal cell tumors. Several specific translocations that result in kidney cancer and involve the TFE3 gene have been described and characterized in detail (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Transcription factor EB (TFEB) is a member of the Myc-related, bHLH leucine-zipper family of transcription factors that drives the expression of a network of genes known as the Coordinated Lysosomal Expression and Regulation (CLEAR) network (1,2). TFEB specifically recognizes and binds regulatory sequences within the CLEAR box (GTCACGTGAC) of lysosomal and autophagy genes, resulting in the up-regulated expression of genes involved in lysosome biogenesis and function, and regulation of autophagy (1,2). TFEB is activated in response to nutrient deprivation, stimulating translocation to the nucleus where it forms homo- or heterooligomers with other members of the microphthalmia transcription factor (MiTF) subfamily and resulting in up-regulation of autophagosomes and lysosomes (3-5). Recently, it has been shown that TFEB is a component of mammalian target of rapamycin (mTOR) complex 1 (mTORC1), which regulates the phosphorylation and nuclear translocation of TFEB in response to cellular starvation and stress (6-9). During normal growth conditions, TFEB is phosphorylated at Ser211 in an mTORC1-dependent manner. Phosphorylation promotes association of TFEB with 14-3-3 family proteins and retention in the cytosol. Inhibition of mTORC1 results in a loss of TFEB phosphorylation, dissociation of the TFEB/14-3-3 complex, and rapid transport of TFEB to the nucleus where it increases transcription of CLEAR and autophagy genes (10). TFEB has also been shown to be activated in a nutrient-dependent manner by p42 MAP kinase (Erk2). TFEB is phosphorylated at Ser142 by Erk2 in response to nutrient deprivation, resulting in nuclear localization and activation, and indicating that pathways other than mTOR contribute to nutrient sensing via TFEB (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

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

Background: TFII-I (also known as SPIN and BAP-135) is a mutifunctional transcription factor that facilitates basal transcriptional machinery assembly at the core promotor region, as well as the assembly of the transcriptional activator complex at upstream regulatory sites (1). Four isoforms of TFII-I (alpha, beta, gamma, and delta) form homo- or heteromeric complexes, which may perform different functions on different promoters (1). In B cells, cross-linking of BCR (B cell receptors) leads to TFII-I phosphorylation at Tyr248 by Btk (2). This phosphorylation disrupts the association of Btk and TFII-I and enhances TFII-I transcriptional activity and nuclear localization (2). In nonlymphoid cells, TFII-I is phosphorylated at Tyr248 by Src dependent kinase or JAK2 (3,4). PKG (cGMP-dependent kinase) interacts with and phosphorylates TFII-I at Ser371 and 743, which also promotes TFII-I transcription activity (5). TFII-I activity is also modulated by HDAC3 (Histone Deacetylase 3) through a physical interaction between the two proteins (6).

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

Application Methods: Western Blotting

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: TFIIF is a member of the group of general transcription factors that facilitate the binding of RNA polymerase II (Pol II) to promoter sequences as part of the pre-initiation complex (PIC) (1). TFIIF consists of subunits TFIIF-α (RAP74) and TFIIF-β (RAP30). It is involved in the stabilization of Pol II association with the PIC and selection of the transcription start site during transcription initiation (1,2). In addition to its role in transcription initiation, TFIIF has been shown to stimulate the transcription elongation activity of Pol II as well as dephosphorylation and recycling of Pol II during transcription termination (3-5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Transforming growth factor-β (TGF-β) superfamily members are critical regulators of cell proliferation and differentiation, developmental patterning and morphogenesis, and disease pathogenesis (1-4). TGF-β elicits signaling through three cell surface receptors: type I (RI), type II (RII), and type III (RIII). Type I and type II receptors are serine/threonine kinases that form a heteromeric complex. In response to ligand binding, the type II receptors form a stable complex with the type I receptors allowing phosphorylation and activation of type I receptor kinases (5). The type III receptor, also known as betaglycan, is a transmembrane proteoglycan with a large extracellular domain that binds TGF-β with high affinity but lacks a cytoplasmic signaling domain (6,7). Expression of the type III receptor can regulate TGF-β signaling through presentation of the ligand to the signaling complex. The only known direct TGF-β signaling effectors are the Smad family proteins, which transduce signals from the cell surface directly to the nucleus to regulate target gene transcription (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mink, Rat

Application Methods: Western Blotting

Background: Transforming growth factor-β (TGF-β) superfamily members are critical regulators of cell proliferation and differentiation, developmental patterning and morphogenesis, and disease pathogenesis (1-4). TGF-β elicits signaling through three cell surface receptors: type I (RI), type II (RII), and type III (RIII). Type I and type II receptors are serine/threonine kinases that form a heteromeric complex. In response to ligand binding, the type II receptors form a stable complex with the type I receptors allowing phosphorylation and activation of type I receptor kinases (5). The type III receptor, also known as betaglycan, is a transmembrane proteoglycan with a large extracellular domain that binds TGF-β with high affinity but lacks a cytoplasmic signaling domain (6,7). Expression of the type III receptor can regulate TGF-β signaling through presentation of the ligand to the signaling complex. The only known direct TGF-β signaling effectors are the Smad family proteins, which transduce signals from the cell surface directly to the nucleus to regulate target gene transcription (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Transforming growth factor-β (TGF-β) superfamily members are critical regulators of cell proliferation and differentiation, developmental patterning and morphogenesis, and disease pathogenesis (1-4). TGF-β elicits signaling through three cell surface receptors: type I (RI), type II (RII), and type III (RIII). Type I and type II receptors are serine/threonine kinases that form a heteromeric complex. In response to ligand binding, the type II receptors form a stable complex with the type I receptors allowing phosphorylation and activation of type I receptor kinases (5). The type III receptor, also known as betaglycan, is a transmembrane proteoglycan with a large extracellular domain that binds TGF-β with high affinity but lacks a cytoplasmic signaling domain (6,7). Expression of the type III receptor can regulate TGF-β signaling through presentation of the ligand to the signaling complex. The only known direct TGF-β signaling effectors are the Smad family proteins, which transduce signals from the cell surface directly to the nucleus to regulate target gene transcription (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Transforming growth factor-β (TGF-β) superfamily members are critical regulators of cell proliferation and differentiation, developmental patterning and morphogenesis, and disease pathogenesis (1-4). TGF-β elicits signaling through three cell surface receptors: type I (RI), type II (RII), and type III (RIII). Type I and type II receptors are serine/threonine kinases that form a heteromeric complex. In response to ligand binding, the type II receptors form a stable complex with the type I receptors allowing phosphorylation and activation of type I receptor kinases (5). The type III receptor, also known as betaglycan, is a transmembrane proteoglycan with a large extracellular domain that binds TGF-β with high affinity but lacks a cytoplasmic signaling domain (6,7). Expression of the type III receptor can regulate TGF-β signaling through presentation of the ligand to the signaling complex. The only known direct TGF-β signaling effectors are the Smad family proteins, which transduce signals from the cell surface directly to the nucleus to regulate target gene transcription (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Thanatos-associated protein (Thap) proteins are a family of cellular factors that are characterized by an evolutionarily conserved protein motif similar to the DNA-binding domain of Drosophila P element transposase (1). There are 12 known human Thap proteins that all act as site-specific DNA-binding factors involved in transcriptional regulation, cell proliferation, chromatin modification, and apoptosis (2-4). Human Thap11 has been shown to suppress cell growth through transcriptional suppression of c-Myc (5). The mouse homolog of Thap11, Ronin, has been identified as an essential factor underlying embryogenesis in mouse embryonic stem cells (6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: THEM2 is a homotetrameric fatty acyl–CoA thioesterase (1). THEM2 and PC-TP (phosphatidylcholine transfer protein), both enriched in liver, interact to form a complex (1). Cell membrane-bound phosphatidylcholines bind to PC-TP in the complex (1). The complex in turn inhibits IRS-2 and mTORC1, which leads to the suppression of insulin signaling (1). THEM2 has also been shown to regulate adaptive thermogenesis in mice (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: THEMIS is a recently identified protein found to be critical for T cell development (1-5). It contains two amino-terminal globular domains, a nuclear localization signal, and a carboxy-terminal proline-rich sequence with homology to SH3 binding domains (2,3). THEMIS is detected in both the cytoplasm and the nucleus (2). It is expressed at low levels in mature T cells and during thymocyte development, with expression peaking in CD4+CD8+ double positive cells (1-5). THEMIS is tyrosine phosphorylated downstream of TCR signaling and associates with the adaptor GRB2 and possibly other SH3 domain-containing proximal TCR signaling molecules (1-5). Mice lacking THEMIS have a defect in positive selection that results in decreased numbers of both single positive thymocytes and mature T cells (1-5).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: THEX1 (3’hExo) is a 3’ exonuclease that may play a role in the degradation of histone mRNA transcripts (1). A recently identified member of the DEDDh 3' exonuclease family, THEX1 binds the conserved stem-loop structure found at the 3’ end of mRNA in vitro (2). The binding of THEX1 to mRNA requires the presence of a terminal ACCCA sequence and is enhanced by the concurrent binding of stem-loop binding protein (SLBP). Cleavage of histone mRNA by THEX1 exonuclease may help produce the rapid turnover of histone mRNA transcripts associated with the completion of DNA replication (3). Additional evidence suggests that THEX1 may be responsible for excising the remaining few 3’ nucleotides following cleavage by a different enzyme (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Thioredoxin is a small redox protein found in many eukaryotes and prokaryotes. A pair of cysteines within a highly conserved, active site sequence can be oxidized to form a disulfide bond that is then reduced by thioredoxin reductase (1). Multiple forms of thioredoxin have been identified, including cytosolic thioredoxin 1 (TRX1) and mitochondrial thioredoxin 2 (TRX2). Thioredoxin participates in many cellular processes including redox signaling, response to oxidative stress, and protein reduction (1). A potential role of thioredoxin in human disorders such as cancer, aging, and heart disease is currently under investigation (2). Thioredoxin can play a key role in cancer progression, because it acts as a negative regulator of the proapoptotic kinase ASK1 (3). Changes in thioredoxin expression have been associated with meningococcal septic shock and acute lung injury (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: Thioredoxin is a small redox protein found in many eukaryotes and prokaryotes. A pair of cysteines within a highly conserved, active site sequence can be oxidized to form a disulfide bond that is then reduced by thioredoxin reductase (1). Multiple forms of thioredoxin have been identified, including cytosolic thioredoxin 1 (TRX1) and mitochondrial thioredoxin 2 (TRX2). Thioredoxin participates in many cellular processes including redox signaling, response to oxidative stress, and protein reduction (1). A potential role of thioredoxin in human disorders such as cancer, aging, and heart disease is currently under investigation (2). Thioredoxin can play a key role in cancer progression, because it acts as a negative regulator of the proapoptotic kinase ASK1 (3). Changes in thioredoxin expression have been associated with meningococcal septic shock and acute lung injury (4,5).