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Product listing: Phospho-eIF4G (Ser1108) Antibody, UniProt ID Q04637 #2441 to Androgen Receptor (AR-V7 Specific) (E3O8L) Rabbit mAb, UniProt ID P10275-3 #19672

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

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

Background: Eukaryotic initiation factor 4E (eIF4E) binds to the mRNA cap structure to mediate the initiation of translation (1,2). eIF4E interacts with eIF4G, a scaffold protein that promotes assembly of eIF4E and eIF4A into the eIF4F complex (2). eIF4B is thought to assist the eIF4F complex in translation initiation. Upon activation by mitogenic and/or stress stimuli mediated by Erk and p38 MAPK, Mnk1 phosphorylates eIF4E at Ser209 in vivo (3,4). Two Erk and p38 MAPK phosphorylation sites in mouse Mnk1 (Thr197 and Thr202) are essential for Mnk1 kinase activity (3). The carboxy-terminal region of eIF4G also contains serum-stimulated phosphorylation sites, including Ser1108, Ser1148, and Ser1192 (5). Phosphorylation at these sites is blocked by the PI3 kinase inhibitor LY294002 and by the FRAP/mTOR inhibitor rapamycin.

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Nonmuscle myosin is an actin-based motor protein essential to cell motility, cell division, migration, adhesion, and polarity. The holoenzyme consists of two identical heavy chains and two sets of light chains. The light chains (MLCs) regulate myosin II activity and stability. The heavy chains (NMHCs) are encoded by three genes, MYH9, MYH10, and MYH14, which generate three different nonmuscle myosin II isoforms, IIa, IIb, and IIc, respectively (reviewed in 1). While all three isoforms perform the same enzymatic tasks, binding to and contracting actin filaments coupled to ATP hydrolysis, their cellular functions do not appear to be redundant and they have different subcellular distributions (2-5). The carboxy-terminal tail domain of myosin II is important in isoform-specific subcellular localization (6). Research studies have shown that phosphorylation of myosin IIa at Ser1943 contributes to the regulation of breast cancer cell migration (7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Akt, also referred to as PKB or Rac, plays a critical role in controlling survival and apoptosis (1-3). This protein kinase is activated by insulin and various growth and survival factors to function in a wortmannin-sensitive pathway involving PI3 kinase (2,3). Akt is activated by phospholipid binding and activation loop phosphorylation at Thr308 by PDK1 (4) and by phosphorylation within the carboxy terminus at Ser473. The previously elusive PDK2 responsible for phosphorylation of Akt at Ser473 has been identified as mammalian target of rapamycin (mTOR) in a rapamycin-insensitive complex with rictor and Sin1 (5,6). Akt promotes cell survival by inhibiting apoptosis through phosphorylation and inactivation of several targets, including Bad (7), forkhead transcription factors (8), c-Raf (9), and caspase-9. PTEN phosphatase is a major negative regulator of the PI3 kinase/Akt signaling pathway (10). LY294002 is a specific PI3 kinase inhibitor (11). Another essential Akt function is the regulation of glycogen synthesis through phosphorylation and inactivation of GSK-3α and β (12,13). Akt may also play a role in insulin stimulation of glucose transport (12). In addition to its role in survival and glycogen synthesis, Akt is involved in cell cycle regulation by preventing GSK-3β-mediated phosphorylation and degradation of cyclin D1 (14) and by negatively regulating the cyclin dependent kinase inhibitors p27 Kip1 (15) and p21 Waf1/Cip1 (16). Akt also plays a critical role in cell growth by directly phosphorylating mTOR in a rapamycin-sensitive complex containing raptor (17). More importantly, Akt phosphorylates and inactivates tuberin (TSC2), an inhibitor of mTOR within the mTOR-raptor complex (18,19).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Androgen receptor (AR), a zinc finger transcription factor belonging to the nuclear receptor superfamily, is activated by phosphorylation and dimerization upon ligand binding (1). This promotes nuclear localization and binding of AR to androgen response elements in androgen target genes. Research studies have shown that AR plays a crucial role in several stages of male development and the progression of prostate cancer (2,3).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: MKK7 is a MAP kinase kinase that serves as a specific activator of the SAPK/JNK pathway (1,2). MKK7 is strongly activated by TNF-α, as well as other environmental stresses, whereas SEK1/MKK4, which activates both p38 and SAPK/JNK pathways, is not activated by TNF-α (2). Sequence alignment of the activation loop of the MAP kinase kinase family members indicates that Ser271 and Thr275 are potential phosphorylation sites that are crucial for the kinase acivity.

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

Application Methods: Immunoprecipitation, Western Blotting

Background: HGK (MAP4K4 or mitogen-activated protein kinase kinase kinase kinase 4) is a serine/threonine kinase that belongs to the mammalian STE20/MAP4K kinase family involved in response to environmental stress and cytokines such as TNF-α (1-3). HGK specifically activates the c-Jun N-terminal kinase (JNK) signaling pathway and increases AP-1-mediated transcriptional activity in vivo (1). HGK is broadly expressed in many types of human cancer and cancer cell lines and plays an important role in cell transformation, invasiveness, adhesion and migration (4,5).

$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.

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

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

Background: DDX5 (DEAD box polypeptide 5), also known as p68, was first identified as a 68 kDa nuclear protein with similarity to translation initiation factor eIF-4A (1). DDX5 is a member of the DEAD box family of putative RNA helicases, defined by the presence of a conserved DEAD (Asp-Glu-Ala-Asp) motif that appears to function primarily in the regulation of RNA secondary structure. DDX5 exhibits ATP-dependent RNA helicase activity (2) and has been identified as a critical subunit of the DROSHA complex that regulates miRNA and rRNA processing (3,4). DDX may also regulate mRNA splicing (5) and has been shown to interact with HDAC1, where it can regulate promoter-specific transcription (6). DDX5 interacts with a diverse group of proteins, including Runx2, p53, Smad3, CBP, and p300 (7-10), suggesting an important role for DDX5 in a multitude of developmental processes. Notably, DDX5 may be involved in growth factor-induced epithelial mesechymal transition (EMT). Phosphorylation of DDX5 at Tyr593 following PDGF stimulation was shown to displace Axin from β-catenin; this prevented phosphorylation of β-catenin by GSK-3β, leading to Wnt-independent nuclear translocation of β-catenin (11) and increased transcription of c-Myc, cyclin D1, and Snai1 (12,13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: AML1 (also known as Runx1, CBFA2, and PEBP2αB) is a member of the core binding factor (CBF) family of transcription factors (1,2). It is required for normal development of all hematopoietic lineages (3-5). AML1 forms a heterodimeric DNA binding complex with its partner protein CBFβ and regulates the expression of cellular genes by binding to promoter and enhancer elements. AML1 is commonly translocated in hematopoietic cancers: chromosomal translocations include t(8;21) AML1-ETO, t(12;21) TEL-AML, and t(8;21) AML-M2 (6). Phosphorylation of AML1 on several potential serine and threonine sites, including Ser249, is thought to occur in an Erk-dependent manner (7,8).

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

Application Methods: Western Blotting

Background: Rho family small GTPases, including Rho, Rac and cdc42, act as molecular switches, regulating processes such as cell migration, adhesion, proliferation and differentiation. They are activated by guanine nucleotide exchange factors (GEFs), which catalyze the exchange of bound GDP for GTP, and inhibited by GTPase activating proteins (GAPs), which catalyze the hydrolysis of GTP to GDP. A third level of regulation is provided by the stoichiometric binding of Rho GDP dissociation inhibitor (RhoGDI) (1). RhoA, RhoB and RhoC are highly homologous, but appear to have divergent biological functions. Carboxy-terminal modifications and differences in subcellular localization allow these three proteins to respond to and act on distinct signaling molecules (2,3).

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

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

Background: Mismatch repair (MMR), a conserved process that involves correcting errors made during DNA synthesis, is crucial to the maintenance of genomic integrity. MLH1 is the human homologue of the E. coli MMR gene mutL. MMR requires recognition of a base mismatch or insertion/deletion loop by a MutS homolog followed by recruitment of a MutL heterodimeric complex consisting of MLH1 and PMS1 (MutL-γ), PMS2 (MutL-α) or MLH3 (MutL-γ). Other factors required for MMR in eukaryotes are EXO1, PCNA, RFC, RPA, DNA polymerases and DNA ligase (reviewed in 1). Inactivation of the MLH1 gene causes genome instability and predisposition to cancer (2-5). The MLH1 gene is frequently mutated in hereditary nonpolyposis colon cancer (HNPCC) (6). MLH1 also plays a role in meiotic recombination (7).

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

Application Methods: Western Blotting

Background: Carboxy-terminal Src kinase (Csk) is a ubiquitously expressed nonreceptor tyrosine kinase that negatively regulates the Src family kinases (SFKs) by phosphorylation of the SFK carboxy-terminal tyrosine (1,2). Phosphorylated carboxy-terminal tyrosine binds to the SH2 domain of SFK intramolecularly and leads to folding and inactivation of the SFK (3). This Csk-catalyzed SFK tyrosine phosphorylation is highly specific and exclusive. The SFK carboxy-terminal tyrosine is the only known physiological substrate of Csk (4).Csk consists of an SH2, an SH3, and a kinase domain. There is evidence that the SH2 and SH3 domains are essential for the regulation of SFK, and Csk can be recruited to the membrane where SFKs are in an active state. This process is mediated by a Csk-binding protein (Cbp, also called PAG), which binds tightly to the SH2 domain of Csk (5). Activation of SFK by extracellular stimuli leads to the tyrosine phosphorylation of Cbp, generating docking sites for Csk. The recruitment of Csk forms a feedback mechanism for termination of SFK function (6).

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

Application Methods: Western Blotting

Background: The Grb-associated binder (Gab) family is a family of adaptor proteins recruited by a wide variety of receptor tyrosine kinases (RTKs) such as EGFR, HGFR, insulin receptor, cytokine receptor and B cell antigen receptors. Upon stimulation of RTKs by their cognate ligand, Gab is recruited to the plasma membrane where it is phosphorylated and functions as a scaffold (1-4). Multiple tyrosine phosphorylation sites of Gab1 protein have been identified (5). Phosphorylation of Tyr472 regulates its binding to p85 PI3 kinase (6,7). Phosphorylation of Gab1 at Tyr307, Tyr373 and Tyr407 modulates its association to PLCγ (8). Phosphorylation of Tyr627 and Tyr659 is required for Gab1 binding to and activation of the protein tyrosine phosphatase SHP2 (6,9).

$489
96 assays
1 Kit
CST's PathScan® Phospho-NF-KappaB p65 (Ser536) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Phospho-NF-KappaB p65 protein. A Phospho-NF-KappaB p65 (Ser 536) Mouse mAb has been coated onto the microwells. After incubation with cell lysates, phospho-NF-KappaB p65 protein is captured by the coated antibody. Following extensive washing, NF-KappaB p65 Rabbit mAb is added to detect the captured phospho-NF-KappaB p65 protein. Anti-rabbit IgG, HRP-linked Antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of phospho-NF-KappaB p65 (Ser536).Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse

Background: Transcription factors of the nuclear factor κB (NF-κB)/Rel family play a pivotal role in inflammatory and immune responses (1,2). There are five family members in mammals: RelA, c-Rel, RelB, NF-κB1 (p105/p50), and NF-κB2 (p100/p52). Both p105 and p100 are proteolytically processed by the proteasome to produce p50 and p52, respectively. Rel proteins bind p50 and p52 to form dimeric complexes that bind DNA and regulate transcription. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins (3-5). NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKKα (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which translocates to the nucleus (9-11).

$398
120 slides
1 Kit
The Immunohistochemistry Application Solutions Kit (IHC-P) is designed to conveniently provide supporting reagents needed for immunohistochemistry staining in paraffin-embedded tissue samples or cell pellets (IHC-P). The reagents in this kit are thoroughly validated using our IHC-recommended rabbit polyclonal and monoclonal antibodies and will perform optimally with the CST immunohistochemistry staining protocol, ensuring accurate and reproducible results. This kit includes sufficient reagents for 120 slides based on a 100 µl assay volume. All reagents in this kit are available individually.IMPORTANT: Please refer to the primary antibody data sheet to determine if the antibody is approved for use on paraffin-embedded samples (IHC-P) and for information regarding the appropriate antibody dilution, diluent, and antigen unmasking procedure.
APPLICATIONS

Application Methods: Immunohistochemistry (Paraffin)

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated His-Tag (D3I1O) XP® Rabbit mAb #12698.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Flow Cytometry

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

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct flow cytometric and immunofluorescence analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Cas9 (7A9-3A3) Mouse mAb #14697.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: The CRISPR associated protein 9 (Cas9) is an RNA-guided DNA nuclease and part of the Streptococcus pyogenes CRISPR antiviral immunity system that provides adaptive immunity against extra chromosomal genetic material (1). The CRISPR antiviral mechanism of action involves three steps: (i), acquisition of foreign DNA by host bacterium; (ii), synthesis and maturation of CRISPR RNA (crRNA) followed by the formation of RNA-Cas nuclease protein complexes; and (iii), target interference through recognition of foreign DNA by the complex and its cleavage by Cas nuclease activity (2). The type II CRISPR/Cas antiviral immunity system provides a powerful tool for precise genome editing and has potential for specific gene regulation and therapeutic applications (3). The Cas9 protein and a guide RNA consisting of a fusion between a crRNA and a trans-activating crRNA (tracrRNA) must be introduced or expressed in a cell. A 20-nucleotide sequence at the 5' end of the guide RNA directs Cas9 to a specific DNA target site. As a result, Cas9 can be "programmed" to cut various DNA sites both in vitro and in cells and organisms. CRISPR/Cas9 genome editing tools have been used in many organisms, including mouse and human cells (4,5). Research studies demonstrate that CRISPR can be used to generate mutant alleles or reporter genes in rodents and primate embryonic stem cells (6-8).

The Notch Isoform Antibody Sampler Kit provides an economical means to investigate Notch Signaling. The kit contains primary and secondary antibodies to perform two western mini-blots with each antibody.

Background: Notch proteins (Notch1-4) are a family of transmembrane receptors that play important roles in development and the determination of cell fate (1). Mature Notch receptors are processed and assembled as heterodimeric proteins, with each dimer comprised of a large extracellular ligand-binding domain, a single-pass transmembrane domain, and a smaller cytoplasmic subunit (Notch intracellular domain, NICD) (2). Binding of Notch receptors to ligands of the Delta-Serrate-Lag2 (DSL) family triggers heterodimer dissociation, exposing the receptors to proteolytic cleavages; these result in release of the NICD, which translocates to the nucleus and activates transcription of downstream target genes (3,4).

$303
100 µl
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Immunoprecipitation, Peptide ELISA (DELFIA), Western Blotting

Background: Although protein kinase C (PKC) family members are involved in a number of signal transduction processes including secretion, gene expression, proliferation, and muscle contraction, many PKC substrates continue to be unidentified (1,2). Isozymes of PKC are subdivided into conventional PKCs (cPKC), novel PKCs (nPKC), and atypical PKCs (aPKC). PKCα, βI, βII, and γ isoforms belong to the cPKC group (1). When activated, cPKC isozymes phosphorylate substrates containing Ser or Thr, with Arg or Lys at the -3, -2, and +2 positions, and a hydrophobic amino acid at position +1 (1-3).

$303
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated K48-linkage Specific Polyubiquitin (D9D5) Rabbit mAb #8081.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Western Blotting

Background: Ubiquitin is a conserved polypeptide unit that plays an important role in the ubiquitin-proteasome pathway. Ubiquitin can be covalently linked to many cellular proteins by the ubiquitination process, which targets proteins for degradation by the 26S proteasome. Three components are involved in the target protein-ubiquitin conjugation process. Ubiquitin is first activated by forming a thiolester complex with the activation component E1; the activated ubiquitin is subsequently transferred to the ubiquitin-carrier protein E2, then from E2 to ubiquitin ligase E3 for final delivery to the epsilon-NH2 of the target protein lysine residue (1-3). The ubiquitin-proteasome pathway has been implicated in a wide range of normal biological processes and in disease-related abnormalities. Several proteins such as IκB, p53, cdc25A, and Bcl-2 have been shown to be targets for the ubiquitin-proteasome process as part of regulation of cell cycle progression, differentiation, cell stress response, and apoptosis (4-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: TIMPs are members of the family of tissue inhibitor of matrix metalloproteinases (MMPs) that includes TIMP1, TIMP2, TIMP3, and TIMP4. The main function of TIMPs is their inhibitory effect on MMPs. TIMPs irreversibly inactivate MMPs by direct binding to their catalytic zinc cofactor and resultant inhibition of proteinase function (1,2). In addition to MMP inhibition, TIMPs have also been shown to interact with various membrane receptors on the cell surface. Some of these interactions include: TIMP1 with CD63, TIMP2 with α3β1 integrin, and TIMP3 with VEGFR2, all of which result in distinct cellular effects (3). TIMPs are involved in a wide variety of biological functions, such as tumor angiogenesis and progression (4,5), wound healing, and vascular remodeling (6,7). Mutations in TIMP3 are associated with Sorsby's fundus dystrophy (8,9).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). It 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 (4).Atg9, one of the Atg proteins identified in yeast, is essential for autophagosome formation (5). There are two human functional orthologues based on the yeast homolog Atg9p: Atg9A, which has also been identified as Atg9L1 and mAtg9, and Atg9L2, which was first reported as nitric-oxide synthase 3 antisense (NOS3AS) (6,7). Atg9A is an integral membrane protein that is required for both the initiation and the expansion of the autophagosome (6,7). Recruitment of Atg9A to the autophagosomal membrane is dynamic and transient as Atg9A also cycles between autophagy-related structures known as omegasomes, the trans-Golgi network (TGN), and endosomes, and at no point becomes a stable component of the autophagosomal membrane (6,8). The precise regulation of Atg9A trafficking is not fully clarified, yet it is suggested to involve p38 mitogen-activated protein kinase (MAPK)-binding protein p38IP and the Beclin-1-binding protein Bif-1 (9,10).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: AML1 (also known as Runx1, CBFA2, and PEBP2αB) is a member of the core binding factor (CBF) family of transcription factors (1,2). It is required for normal development of all hematopoietic lineages (3-5). AML1 forms a heterodimeric DNA binding complex with its partner protein CBFβ and regulates the expression of cellular genes by binding to promoter and enhancer elements. AML1 is commonly translocated in hematopoietic cancers: chromosomal translocations include t(8;21) AML1-ETO, t(12;21) TEL-AML, and t(8;21) AML-M2 (6). Phosphorylation of AML1 on several potential serine and threonine sites, including Ser249, is thought to occur in an Erk-dependent manner (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: The Silent Information Regulator (SIR2) family of genes is a highly conserved group of genes that encode nicotinamide adenine dinucleotide (NAD)-dependent protein deacetylases, also known as class III histone deacetylases. The first discovered and best characterized of these genes is Saccharomyces cerevisiae SIR2, which is involved in silencing of mating type loci, telomere maintenance, DNA damage response, and cell aging (1). SirT1, the mammalian ortholog of Sir2, is a nuclear protein implicated in the regulation of many cellular processes, including apoptosis, cellular senescence, endocrine signaling, glucose homeostasis, aging, and longevity. Targets of SirT1 include acetylated p53 (2,3), p300 (4), Ku70 (5), forkhead (FoxO) transcription factors (5,6), PPARγ (7), and the PPARγ coactivator-1α (PGC-1α) protein (8). Deacetylation of p53 and FoxO transcription factors represses apoptosis and increases cell survival (2,3,5,6). Deacetylation of PPARγ and PGC-1α regulates the gluconeogenic/glycolytic pathways in the liver and fat mobilization in white adipocytes in response to fasting (7,8). SirT1 deacetylase activity is inhibited by nicotinamide and activated by resveratrol. In addition, SirT1 activity may be regulated by phosphorylation, as it is phosphorylated at Ser27 and Ser47 in vivo; however, the function of these phosphorylation sites has not yet been determined (9).

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

Application Methods: Western Blotting

Background: Caspase-6 (Mch2) is one of the major executioner caspases functioning in cellular apoptotic processes (1,2). Upon apoptotic stimulation, initiator caspases such as caspase-9 are cleaved and activated (3). The activated upstream caspases further process downstream executioner caspases, such as caspase-3 and caspase-6, by cleaving them into large and small subunits, thereby initiating a caspase cascade leading to apoptosis (4,5). One of the major targets for caspase-6 is the membrane associated protein lamin A (6). The cleavage of this protein causes cell membrane malfunction, membrane blebbing and eventual cell death.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Bromodomain-containing protein 7 (BRD7, BP75, CELTIX-1) is a conserved bromodomain-containing protein that was first identified in a screen for proteins that interact with the PDZ domain of PSD95 (1). Subsequent studies identified BRD7 as a major component of SWI/SNF chromatin remodeling complexes, where it was shown to interact directly with acetylated histones to regulate gene transcription (2,3). BRD7 also interacts with p53, and was shown to participate directly in p53-dependent transcriptional regulation (4). Loss-of-function BRD7 mutations were identified in a subset of wild-type p53 breast cancer tumor samples, implicating BRD7 as a putative tumor-suppressor of potential clinical significance (5). BRD7 also associates with the BRCA1 protein, an interaction that facilitates recruitment of BRCA1 to the ERα gene promoter (6).

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

Application Methods: Western Blotting

Background: Manganese superoxide dismutase (MnSOD or SOD2) is a mitochondrial detoxification enzyme that catalyzes the conversion of superoxide to hydrogen peroxide (1,2). Hydrogen peroxide is then decomposed to water by catalase, glutathione peroxidase, or peroxiredoxins (2). MnSOD/SOD2 and other enzymes involved in antioxidant defense protect cells from reactive oxygen species (ROS) (2). Calorie restriction leads to SIRT3-mediated deacetylation of MnSOD/SOD2 and the subsequent increase of its antioxidant activity (3). MnSOD/SOD2 also plays an essential role in mediating the protective effect of mTOR inhibition to reduce epithelial stem cell senescence (4).

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

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

Background: JunD, along with closely related family members c-Jun and JunB, is a transcription factor that can activate or repress a wide array of target genes (1,2). JunD transcriptional activity is modulated by phosphorylation in response to cellular stress via the c-Jun N-terminal Kinase (JNK)/Stress-Activated Protein Kinase (SAPK) family of protein kinases (3,4). JunD activity can also be modulated by the MAPK pathway in response to growth factors. Its transcriptional capacity is further regulated by other binding partners that affect JunD expression levels and DNA binding capacity (reviewed in 5). All Jun proteins are capable of forming dimers with Fos-, ATF- and CREB-family transcription factors to form the AP-1 complex that differentially regulates a variety of target genes involved in cellular growth, proliferation, differentiation, and apoptosis (reviewed in 5 and 6). Unlike JunB and c-Jun, which share a high degree of homology (>95%), JunD is less conserved (~75%) at the amino acid level (1). Growing evidence suggests that JunD protein expression is regulated independently of other family members (reviewed in 5). It is thought that JunD may have functional significance beyond the typical Jun-family milieu. This is exemplified by the fact that JunD knockout mice are viable, bearing specific defects in cardiomyocyte function and bone growth, whereas their c-Jun counterparts develop significant, multi-organ defects during embryogenesis and die at E12.5 (7-10). JunD appears to specifically regulate genes involved in antioxidant response and hydrogen peroxide production and plays an important role in angiogenesis via its ability to exert transcriptional control over the VEGF gene (11). Furthermore, JunD appears to play an important roll in metabolism via modulation of IGF-I signaling pathways (12). Recent studies have shown that JunD regulates GADD45 α and γ expression in prostate cancer cells and that inhibition of JunD promotes apoptosis. Thus, JunD may be a viable therapeutic target for the treatment of prostate cancer (13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Androgen receptor (AR), a zinc finger transcription factor belonging to the nuclear receptor superfamily, is activated by phosphorylation and dimerization upon ligand binding (1). This promotes nuclear localization and binding of AR to androgen response elements in androgen target genes. Research studies have shown that AR plays a crucial role in several stages of male development and the progression of prostate cancer (2,3).