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Product listing: SignalSilence® Vitamin D3 Receptor siRNA I, UniProt ID P11473 #12719 to TCF1/TCF7 Blocking Peptide, UniProt ID P36402 #1007

$262
3 nmol
300 µl
SignalSilence® Vitamin D3 Receptor siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit vitamin D3 receptor 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: Although originally identified based on their roles in calcium and bone homeostasis, the vitamin D3 receptor (VDR/NR1I1) and its ligand 1-α, 25-dihydroxycholecalciferol [1α, 25(OH)2D3] are now recognized to exert biological effects in almost every tissue of the human body. Targets for vitamin D signaling include the central nervous system, skin, immune system, endocrine glands, kidney, and colon. At the cellular level, vitamin D signaling affects proliferation, differentiation, and apoptosis of both normal and transformed cells. Within the steroid receptor gene family, VDR belongs to the NR1I subfamily that also includes NR1I2/PXR and NR1I3/CAR. The human VDR gene is composed of 11 exons that encode six domains (A-F) of the full length VDR protein, which includes an N-terminal dual zinc finger DNA binding domain, a C-terminal ligand-binding activity domain, and an extensive unstructured region that links the two functional domains together (1). Upon 1α, 25(OH)2D3 binding to the hormone ligand-binding domain, VDR is stabilized by the phosphorylation of Ser51 in the DNA-binding domain by PKC (2), and Ser208 in the hinge region by casein kinase II (3). VDR associates with the retinoic acid receptor (RXR) through dimerization domains. The 1α, 25(OH)2D3-VDR-RXR complex binds to the vitamin D response elements (VDREs) in the promoters of target genes through the DNA-binding domain. Ligand-induced conformation changes in VDR results in the dissociation of the co-repressor, silencing-mediator for retinoid and thyroid hormone receptors (SMRT), and allows interaction of the VDR activation function (AF2) transactivation domain with transcriptional coactivators (1).Studies have shown that variable VDR expression is associated with different forms or stages of cancer and likely results from tissue-type variation in 1α, 25(OH)2D3 signaling. In the case of colon cancer, research indicates that VDR expression is relatively higher in hyperplastic colon polyps and during early tumorigenesis but diminishes in later stage, poorly differentiated tumors. Multiple studies suggest that 1α, 25(OH)2D3 may be an attractive target for development as a therapeutic anticancer agent (4,5) .

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

Background: The HIV-1 viral protein R (Vpr)-binding protein (VPRBP, DCAF1) is a substrate-specific adaptor for the CUL4-based ubiquitin ligase complex that consists of CUL4A, RBX1, and DDB1 (1). VPRBP protein structure contains a central LIS1 homology (LisH) motif responsible for dimerization, and two carboxy-terminal WD-40 motifs involved in Vpr and DDB1 binding (2-4). Research studies demonstrate that VPRBP plays a role in hepatic lipid metabolism by promoting the ubiquitin-dependent proteasomal degradation of the TR4 nuclear receptor, which is involved in lipid homeostasis (5). The VPRBP protein plays a role in mammalian germ cell development through regulation of TET methylcytosine dioxygenase activation (6). Additional studies show that VPRBP exhibits kinase activity and phosphorylates histone H2A at Ser120, which blocks tumor suppressor gene transcription (7). The tumor suppressor Merlin/NF2 inhibits tumorigenesis through interaction with and suppression of the CUL4A-RBX1-DDB1-VPRBP complex (8).

$262
50-100 transfections
300 µl
SignalSilence® XIAP siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit XIAP expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Human

Background: The inhibitor of apoptosis protein (IAP) family consists of an evolutionarily conserved group of apoptosis inhibitors containing a conserved 70 amino acid BIR (baculovirus inhibitor repeat) domain (1,2). Human members of this family include c-IAP1, c-IAP2, XIAP, survivin, livin, and NAIP. Overexpression of IAP family members, particularly survivin and livin, in cancer cell lines and primary tumors suggests an important role for these proteins in cancer progression (3-5). In general, the IAP proteins function through direct interactions to inhibit the activity of several caspases, including caspase-3, caspase-7, and caspase-9 (5,6). In addition, binding of IAP family members to the mitochondrial protein Smac blocks their interaction with caspase-9, thereby allowing the processing and activation of the caspase (2).

$262
3 nmol
300 µl
SignalSilence® XIAP siRNA II from Cell Signaling Technology (CST) allows the researcher to specifically inhibit XIAP 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 protein expression by western analysis.
REACTIVITY
Human

Background: The inhibitor of apoptosis protein (IAP) family consists of an evolutionarily conserved group of apoptosis inhibitors containing a conserved 70 amino acid BIR (baculovirus inhibitor repeat) domain (1,2). Human members of this family include c-IAP1, c-IAP2, XIAP, survivin, livin, and NAIP. Overexpression of IAP family members, particularly survivin and livin, in cancer cell lines and primary tumors suggests an important role for these proteins in cancer progression (3-5). In general, the IAP proteins function through direct interactions to inhibit the activity of several caspases, including caspase-3, caspase-7, and caspase-9 (5,6). In addition, binding of IAP family members to the mitochondrial protein Smac blocks their interaction with caspase-9, thereby allowing the processing and activation of the caspase (2).

$262
3 nmol
300 µl
SignalSilence® YB1 siRNA from Cell Signaling Technology (CST) allows the researcher to specifically inhibit YB1 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 are rigorously tested in-house and have been shown to reduce target protein expression in specified cell lines.
REACTIVITY
Human

Background: The Y-box binding protein 1 (YB1) belongs to a family of evolutionarily conserved, multifunctional Y-box proteins that bind single-stranded DNA and RNA and function as regulators of transcription, RNA metabolism, and protein synthesis (1). YB1 binds to Y-box sequences (TAACC) found in multiple gene promoters and can positively or negatively regulate transcription. YB1 activates genes associated with proliferation and cancer, such as cyclin A, cyclin B1, matrix metalloproteinase-2 (MMP-2), and the multi-drug resistance 1 (MDR1) gene (2-4). YB1 represses genes associated with cell death, including the Fas cell death-associated receptor and the p53 tumor suppressor gene (5-7). It also interacts with the RNA-splicing factor SRp30c and stabilizes interleukin-2 (IL-2) mRNA upon induction of T lymphocytes by IL-2 (8,9). The majority of YB1 protein localizes to the cytoplasm, with a minor pool found in the nucleus; however, nuclear localization appears to be critical for its role in promoting proliferation. Nuclear translocation is cell cycle regulated, with YB1 protein accumulating in the nucleus during G1/S phase (2). In addition, nuclear translocation is induced in response to extracellular stimuli such as hyperthermia and UV irradiation, or treatment of cells with thrombin, interferons, or insulin-like growth factor (IGF-I) (2,10). Treatment of the MCF7 breast cancer cell line with IGF-I results in Akt-mediated phosphorylation of YB1 at Ser102, which is required for nuclear translocation of YB1 and its ability to promote anchorage-independent growth (10). Research studies have shown that YB1 is overexpressed in many malignant tissues, including breast cancer, non-small cell lung carcinoma, ovarian adenocarcinomas, human osteosarcomas, colorectal carcinomas, and malignant melanomas. Investigators have shown that nuclear YB1 expression correlates with high levels of proliferation, drug resistance, and poor tumor prognosis (2,7,10).

$262
3 nmol
300 µl
SignalSilence® YB1 siRNA from Cell Signaling Technology (CST) allows the researcher to specifically inhibit YB1 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 are rigorously tested in-house and have been shown to reduce target protein expression in specified cell lines.
REACTIVITY
Human

Background: The Y-box binding protein 1 (YB1) belongs to a family of evolutionarily conserved, multifunctional Y-box proteins that bind single-stranded DNA and RNA and function as regulators of transcription, RNA metabolism, and protein synthesis (1). YB1 binds to Y-box sequences (TAACC) found in multiple gene promoters and can positively or negatively regulate transcription. YB1 activates genes associated with proliferation and cancer, such as cyclin A, cyclin B1, matrix metalloproteinase-2 (MMP-2), and the multi-drug resistance 1 (MDR1) gene (2-4). YB1 represses genes associated with cell death, including the Fas cell death-associated receptor and the p53 tumor suppressor gene (5-7). It also interacts with the RNA-splicing factor SRp30c and stabilizes interleukin-2 (IL-2) mRNA upon induction of T lymphocytes by IL-2 (8,9). The majority of YB1 protein localizes to the cytoplasm, with a minor pool found in the nucleus; however, nuclear localization appears to be critical for its role in promoting proliferation. Nuclear translocation is cell cycle regulated, with YB1 protein accumulating in the nucleus during G1/S phase (2). In addition, nuclear translocation is induced in response to extracellular stimuli such as hyperthermia and UV irradiation, or treatment of cells with thrombin, interferons, or insulin-like growth factor (IGF-I) (2,10). Treatment of the MCF7 breast cancer cell line with IGF-I results in Akt-mediated phosphorylation of YB1 at Ser102, which is required for nuclear translocation of YB1 and its ability to promote anchorage-independent growth (10). Research studies have shown that YB1 is overexpressed in many malignant tissues, including breast cancer, non-small cell lung carcinoma, ovarian adenocarcinomas, human osteosarcomas, colorectal carcinomas, and malignant melanomas. Investigators have shown that nuclear YB1 expression correlates with high levels of proliferation, drug resistance, and poor tumor prognosis (2,7,10).

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

Background: Arrestin proteins function as negative regulators of G protein-coupled receptor (GPCR) signaling. Cognate ligand binding stimulates GPCR phosphorylation, which is followed by binding of arrestin to the phosphorylated GPCR and the eventual internalization of the receptor and desensitization of GPCR signaling (1). Four distinct mammalian arrestin proteins are known. Arrestin 1 (also known as S-arrestin) and arrestin 4 (X-arrestin) are localized to retinal rods and cones, respectively. Arrestin 2 (also known as β-arrestin 1) and arrestin 3 (β-arrestin 2) are ubiquitously expressed and bind to most GPCRs (2). β-arrestins function as adaptor and scaffold proteins and play important roles in other processes, such as recruiting c-Src family proteins to GPCRs in Erk activation pathways (3,4). β-arrestins are also involved in some receptor tyrosine kinase signaling pathways (5-8). Additional evidence suggests that β-arrestins translocate to the nucleus and help regulate transcription by binding transcriptional cofactors (9,10).

$262
3 nmol
300 µl
SignalSilence® β-Catenin siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit β-catenin 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: β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (8).

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

Background: β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (8).

$262
3 nmol
300 µl
SignalSilence® β-Catenin siRNA II from Cell Signaling Technology (CST) allows the researcher to specifically inhibit β-catenin 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: β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (8).

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

Background: β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (8).

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

Background: Also known as plakoglobin, γ-catenin is a member of the Armadillo family of signaling molecules, which includes β-catenin and the Drosophila protein armadillo (1). This family of proteins is involved in Wnt signaling, which is important in embryonic development and in tumorigenesis (2-3). Although the two vertebrate proteins β- and γ-catenin display sequence homology, γ-catenin likely plays a role distinct from that of β-catenin (1, 4-6). γ-catenin localizes to desmosomes and adherens junctions, both sites of intercellular adhesion, and interacts with the cytoplasmic domains of classical and desmosomal cadherins. Interaction of γ- or β-catenin with α-catenin, desmoplakin and other junction proteins provides a link between intercellular junctions and the actin and intermediate filament cytoskeleton. Maintenance and/or modification of this link is vital for control of cell adhesion and migration (1). γ-catenin is modified by phosphorylation, affecting both adhesion and β-catenin dependent transcription (7), and by and O-glycosylation, affecting adhesion (8). Recent evidence suggests that γ-catenin regulates desmosomal adhesion in response to growth factor stimulation (9).

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

Background: Also known as plakoglobin, γ-catenin is a member of the Armadillo family of signaling molecules, which includes β-catenin and the Drosophila protein armadillo (1). This family of proteins is involved in Wnt signaling, which is important in embryonic development and in tumorigenesis (2-3). Although the two vertebrate proteins β- and γ-catenin display sequence homology, γ-catenin likely plays a role distinct from that of β-catenin (1, 4-6). γ-catenin localizes to desmosomes and adherens junctions, both sites of intercellular adhesion, and interacts with the cytoplasmic domains of classical and desmosomal cadherins. Interaction of γ- or β-catenin with α-catenin, desmoplakin and other junction proteins provides a link between intercellular junctions and the actin and intermediate filament cytoskeleton. Maintenance and/or modification of this link is vital for control of cell adhesion and migration (1). γ-catenin is modified by phosphorylation, affecting both adhesion and β-catenin dependent transcription (7), and by and O-glycosylation, affecting adhesion (8). Recent evidence suggests that γ-catenin regulates desmosomal adhesion in response to growth factor stimulation (9).

The Silent Synapses Antibody Sampler Kit provides an economical means of detecting the activation of AMPA-type glutamate receptors (AMPAR) using phospho-specific and control antibodies. AMPARs expression can be compared to other synaptic components including NMDA-type glutamate receptor subunit GluN1 and the synaptic scaffolding protein PSD95. The kit includes enough antibody to perform two western blot experiments with each primary antibody.

Background: AMPA- (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid), kainate-, and NMDA- (N-methyl-D-aspartate) receptors are the three main families of ionotropic glutamate-gated ion channels. AMPA receptors (AMPARs) are composed of four subunits (GluA1-4), which assemble as homo- or hetero-tetramers to mediate the majority of fast excitatory transmissions in the central nervous system. AMPARs are implicated in synapse formation, stabilization, and plasticity (1). In contrast to GluA2-containing AMPARs, AMPARs that lack GluA2 are permeable to calcium (2). Post-transcriptional modifications (alternative splicing, nuclear RNA editing) and post-translational modifications (glycosylation, phosphorylation) result in a very large number of permutations, fine-tuning the kinetic properties and surface expression of AMPARs representing key pathways to mediate synaptic plasticity (3). During development and mature states, some synapses exhibit “silent synapses” that lack functional AMPAR-mediated transmission. Synapses become “unsilenced” by post-translational modification of GluAs, particularly GluA1, which alters its kinetic properties and/or surface expression while other synaptic components, such as other glutamate receptors like NMDARs and postsynaptic scaffolding proteins like PSD95, remain unaltered. Conversely, reducing the AMPAR kinetic properties and surface expression can silence synapses. Key post-translational modifications implicated in regulating these processes include phosphorylation of GluA1 at Ser831 and Ser845 (4). Research studies have implicated activity-dependent changes in AMPARs in a variety of diseases, including Alzheimer’s, amyotrophic lateral sclerosis (ALS), stroke, and epilepsy (1).

The Sirtuin Antibody Sampler Kit provides an economical means of evaluating total levels of sirtuin proteins. The kit includes enough antibody to perform at least two western blot experiments with each primary antibody.
The Smad1/5/9 Antibody Sampler Kit provides an economical means of detecting target proteins of the BMP signaling pathway. The kit includes enough antibody to perform two western blots with each primary antibody.
The Smad2/3 Antibody Sampler Kit provides an economical means of detecting target proteins of the TGF-β signaling pathway. The kit includes enough antibody to perform two western blots with each primary antibody.
The SQSTM1/p62-like Receptor Antibody Sampler Kit provides an economical means of detecting members of the SQSTM1/p62-like Receptor (SLR) family. The kit includes enough antibody to perform two western blot experiments with each primary antibody.

Background: Autophagy is a catabolic process for the autophagosome-lysosomal degradation of bulk cytoplasmic contents (1,2). Selective autophagy targets the degradation of distinct sets of substrates and organelles and can occur through the utilization of a number of autophagy cargo receptors (3-5). Autophagy cargo receptors contain an LC3-interacting region (LIR) required for interaction with Atg8/LC3 family members targeted to the autophagosome. SQSTM1/p62-like receptors (SLRs) are a family of autophagy cargo receptors that contain domains for binding to ubiquitin. This family includes prototypical member SQSTM1/p62, NBR1, NDP52, Optineurin, and TAX1BP1. Targets of SLRs include ubiquitylated protein aggregates (aggrephagy), organelles such as mitochondria (mitoophagy) and peroxisomes (pexophagy), and intracellular bacteria (xenophagy).Upon binding of cargo to these receptors, the complex is delivered to the autophagosome where both the cargo and receptor are degraded through the autophagic process. While some redundancy may exist among SLR family members, they can have unique activities. Many SLRs can have additional roles as scaffolding proteins for various signaling pathways. For example, SQSTM1/p62 interacts with KEAP1, a cytoplasmic inhibitor of NRF2, a key transcription factor involved in cellular responses to oxidative stress (6). Thus, accumulation of SQSTM1/p62 can lead to an increase in NRF2 activity.

The Src Antibody Sampler kit provides an economical means of evaluating total Src protein levels and its phosphorylation status. The kit contains enough primary and secondary antibodies to perform two Western blot experiments per primary antibody.

Background: The Src family of protein tyrosine kinases, which includes Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, are important in the regulation of growth and differentiation of eukaryotic cells (1). Src activity is regulated by tyrosine phosphorylation at two sites, but with opposing effects. While phosphorylation at Tyr416 in the activation loop of the kinase domain upregulates enzyme activity, phosphorylation at Tyr527 in the carboxy-terminal tail by Csk renders the enzyme less active (2).

This peptide is used to specifically block Src Antibody #2108 and Src (36D10) Rabbit mAb #2109 reactivity.

Background: The Src family of protein tyrosine kinases, which includes Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, are important in the regulation of growth and differentiation of eukaryotic cells (1). Src activity is regulated by tyrosine phosphorylation at two sites, but with opposing effects. While phosphorylation at Tyr416 in the activation loop of the kinase domain upregulates enzyme activity, phosphorylation at Tyr527 in the carboxy-terminal tail by Csk renders the enzyme less active (2).

The Src Family Antibody Sampler Kit provides an economical means of evaluating total levels of Src family member proteins. The kit contains enough primary and secondary antibody to perform two western blots with each antibody.

Background: The Src family of protein tyrosine kinases, which includes Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, are important in the regulation of growth and differentiation of eukaryotic cells (1). Src activity is regulated by tyrosine phosphorylation at two sites, but with opposing effects. While phosphorylation at Tyr416 in the activation loop of the kinase domain upregulates enzyme activity, phosphorylation at Tyr527 in the carboxy-terminal tail by Csk renders the enzyme less active (2).

This peptide is used to block SRC-1 (128E7) Rabbit mAb #2191 reactivity in dot blot protocols.

Background: There are three members of the steroid receptor co-activator (SRC) family of proteins: SRC-1 (NCoA-1), SRC-2 (TIF2/GRIP1/NCoA-2), and SRC-3 (ACTR/pCIP/RAC3/TRAM-1/AIB1). All SRC family members share significant structural homology and function to stimulate transcription mediated by nuclear hormone receptors and other transcriptional activators such as Stat3, NF-κB, E2F1, and p53 (1-4). Two SRC proteins, SRC-1 and SRC-3, function as histone acetyltransferases (5,6). In addition, all three family members can recruit other histone acetyltransferases (CBP/p300, PCAF) and histone methyltransferases (PRMT1, CARM1) to target promoters and cooperate to enhance expression of many genes (5-8). The SRC proteins play important roles in multiple physiological processes including cell proliferation, cell survival, somatic cell growth, mammary gland development, female reproductive function, and vasoprotection (9). SRC-1 and SRC-3 are conduits for kinase-mediated growth factor signaling to the estrogen receptor and other transcriptional activators. Seven SRC-1 phosphorylation sites and six SRC-3 phosphorylation sites have been identified, which are induced by steroids, cytokines, and growth factors and involve multiple kinase signaling pathways (9-11). Research has shown that all three SRC family members are associated with increased activity of nuclear receptors in breast, prostate, and ovarian carcinomas. According to the literature, SRC-3 is frequently amplified or overexpressed in a number of cancers (12), and SRC-1/PAX3 and SRC-2/MYST3 translocations are found associated with rhabdomyosarcoma and acute myeloid leukemia, respectively (13,14).

The Stat Antibody Sampler Kit provides an economical means to examine multiple Stat proteins: Stat1, Stat3, Stat5 and Stat6. The kit contains enough primary and secondary antibodies to perform two Western blot experiments.

Background: Jaks (Janus Kinases) and Stats (Signal Transducers and Activators of Transcription) are utilized by receptors for a wide variety of ligands including cytokines, hormones, growth factors and neurotransmitters. Jaks, activated via autophosphorylation following ligand-induced receptor aggregation, phosphorylate tyrosine residues on associated receptors, Stat molecules and other downstream signaling proteins (1,2). The phosphorylation of Stat proteins at conserved tyrosine residues activates SH2-mediated dimerization followed rapidly by nuclear translocation. Stat dimers bind to IRE (interferon response element) and GAS (gamma interferon-activated sequence) DNA elements, resulting in the transcriptional regulation of downstream genes (1,2). The remarkable range and specificity of responses regulated by the Stats is determined in part by the tissue-specific expression of different cytokine receptors, Jaks and Stats (2,3), and by the combinatorial coupling of various Stat members to different receptors. Serine phosphorylation in the carboxy-terminal transcriptional activation domain has been shown to regulate the function of Stat1, -2, -3, -4 and -5 (1). Phosphorylation of Stat3 at Ser727 via MAPK or mTOR pathways is required for optimal transcriptional activation in response to growth factors and cytokines including IFN-gamma and CNTF (4,5). Jak/Stat pathways also play important roles in oncogenesis, tumor progression, angiogenesis, cell motility, immune responses and stem cell differentiation (6-11).

Stat Antibody Sampler Kit II provides an economical means to examine the complete Stat family: Stat1-6. The kit contains enough a primary antibody to perform two western blot experiments with each primary antibody.

Background: Jaks (Janus Kinases) and Stats (Signal Transducers and Activators of Transcription) are utilized by receptors for a wide variety of ligands including cytokines, hormones, growth factors and neurotransmitters. Jaks, activated via autophosphorylation following ligand-induced receptor aggregation, phosphorylate tyrosine residues on associated receptors, Stat molecules and other downstream signaling proteins (1,2). The phosphorylation of Stat proteins at conserved tyrosine residues activates SH2-mediated dimerization followed rapidly by nuclear translocation. Stat dimers bind to IRE (interferon response element) and GAS (gamma interferon-activated sequence) DNA elements, resulting in the transcriptional regulation of downstream genes (1,2). The remarkable range and specificity of responses regulated by the Stats is determined in part by the tissue-specific expression of different cytokine receptors, Jaks and Stats (2,3), and by the combinatorial coupling of various Stat members to different receptors. Serine phosphorylation in the carboxy-terminal transcriptional activation domain has been shown to regulate the function of Stat1, -2, -3, -4 and -5 (1). Phosphorylation of Stat3 at Ser727 via MAPK or mTOR pathways is required for optimal transcriptional activation in response to growth factors and cytokines including IFN-gamma and CNTF (4,5). Jak/Stat pathways also play important roles in oncogenesis, tumor progression, angiogenesis, cell motility, immune responses and stem cell differentiation (6-11).

This peptide is used to block Stat1 (42H3) Rabbit mAb #9175 reactivity.

Background: The Stat1 transcription factor is activated in response to a large number of ligands (1) and is essential for responsiveness to IFN-α and IFN-γ (2,3). Phosphorylation of Stat1 at Tyr701 induces Stat1 dimerization, nuclear translocation, and DNA binding (4). Stat1 protein exists as a pair of isoforms, Stat1α (91 kDa) and the splice variant Stat1β (84 kDa). In most cells, both isoforms are activated by IFN-α, but only Stat1α is activated by IFN-γ. The inappropriate activation of Stat1 occurs in many tumors (5). In addition to tyrosine phosphorylation, Stat1 is also phosphorylated at Ser727 through a p38 mitogen-activated protein kinase (MAPK)-dependent pathway in response to IFN-α and other cellular stresses (6). Serine phosphorylation may be required for the maximal induction of Stat1-mediated gene activation.

The Stress and Apoptosis Antibody Sampler Kit provides an economical means of evaluating stress and apoptotic responses of each protein. The kit contains enough primary and secondary antibody to perform two western blot experiments per primary antibody.
$320
100 µg
This peptide is used to specifically block Survivin (71G4) Rabbit mAb #2808 reactivity.
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin)

Background: Survivin is a 16 kDa anti-apoptotic protein highly expressed during fetal development and cancer cell malignancy (1). Survivin binds and inhibits caspase-3, controlling the checkpoint in the G2/M-phase of the cell cycle by inhibiting apoptosis and promoting cell division (2,3). This regulatory process requires the phosphorylation of survivin at Thr34 by p34 cdc2 kinase (4). Gene targeting using a Thr34 phosphorylation-defective survivin mutant, as well as antisense survivin, have been shown to inhibit tumor growth (5,6).

The T Cell Signaling Antibody Sampler Kit provides an economical means to investigate T cell receptor signaling. The kit contains primary and secondary antibodies to perform two western blot experiments per primary antibody.

Background: When T cells encounter antigens via the T cell receptor (TCR), information about the quantity and quality of antigens is relayed to the intracellular signal transduction machinery (1). This activation process depends mainly on CD3 (Cluster of Differentiation 3), a multiunit protein complex that directly associates with the TCR α and ß chains. CD3 is composed of four polypeptides: ζ, γ, ε and δ. Each of these polypeptides contains at least one immunoreceptor tyrosine-based activation motif (ITAM) (2). The Src family kinases Lck and Fyn are recruited to the TCR complex upon stimulation and activate the downstream tyrosine kinases to initiate signaling. Phosphorylation of Lck at Tyr394 leads to an increase in Lck activity while phosphorylation of Tyr505 in the Lck carboxy-terminal tail down-regulates Lck catalytic activity (3). Zap-70 and Syk are rapidly phosphorylated on several tyrosine residues through autophosphorylation and transphosphorylation by Src family tyrosine kinases.  Activation loop phosphorylation of Zap-70 at Tyr493 and Syk at Tyr526 leads to complete activation of both kinases (4).  Subsequent phosphorylation of other tyrosine residues within the kinase interdomain B region, including Zap-70 at Tyr315 and Zap-70 at Tyr 319, create docking sites for downstream signaling molecules.  Zap-70 and Syk phosphorylate the transmembrane adaptor protein LAT at multiple, conserved tyrosine residues within SH2 binding motifs, exposing these motifs as docking sites for downstream signaling targets (5,6). The phosphorylation of LAT at Tyr171 and Tyr191 enables the binding of Grb2, Gads/SLP-76, PLCγ1, and PI3 kinase. The adapter protein SLP-76 is phosphorylated at Tyr113 and Tyr128, allowing for binding of the Grb2-like adapter Gads.  Phosphorylation of SLP-76 at Ser376 by hematopoietic progenitor kinase 1 (HPK1) induces interaction with 14-3-3ε and down-regulates TCR signaling (7,8).  Phosphoinositide-specific phospholipase PLCγ1 enzyme activity is also stimulated by Zap-70 and Syk phosphorylation on Tyr783, Tyr711, and Tyr1253, resulting in robust PI-4,5-P2 hydrolysis (9).

The TCF/LEF Family Antibody Sampler Kit provides an economical means of detecting total protein from the TCF/LEF1 family members. The kit contains enough primary and secondary antibodies to perform two Western blots with each antibody.
This peptide is used to block TCF1/TCF7 (C63D9) Rabbit mAb #2203 reactivity in dot blot protocols.

Background: LEF1 and TCF are members of the high mobility group (HMG) DNA binding protein family of transcription factors that consists of the following: Lymphoid Enhancer Factor 1 (LEF1), T Cell Factor 1 (TCF1/TCF7), TCF3/TCF7L1, and TCF4/TCF7L2 (1). LEF1 and TCF1/TCF7 were originally identified as important factors regulating early lymphoid development (2) and act downstream in Wnt signaling. LEF1 and TCF bind to Wnt response elements to provide docking sites for β-catenin, which translocates to the nucleus to promote the transcription of target genes upon activation of Wnt signaling (3). LEF1 and TCF are dynamically expressed during development and aberrant activation of the Wnt signaling pathway is involved in many types of cancers including colon cancer (4,5).