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Product listing: BAF Complex Antibody Sampler Kit #12854 to Double Strand Breaks (DSB) Repair Antibody Sampler Kit, UniProt ID Q13315 #9653

The BAF Complex Antibody Sampler Kit provides an economical means of detecting total protein from the SWI/SNF family members including ARID1A/BAF250A, Brg1, BRM, SMARCC1/BAF155, SMARCC2/BAF170 and SMARCB1/BAF47. The kit contains enough primary antibody to perform two western blots per primary antibody.
The BAF Complex Antibody Sampler Kit II provides an economical means of detecting levels of various BAF complex components. The kit contains enough primary antibodies to perform at least two western blot experiments.
Branched Ubiquitin Antibody Sampler Kit provides an economical means of detecting total and common branch specific forms of ubiquitin. The kit includes enough antibody to perform two western blot experiments with each primary antibody.

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).

The c-Kit Antibody Sampler Kit provides a fast and economical means of evaluating levels of c-Kit receptor protein phosphorylated at the specified sites, as well as total c-Kit receptor levels. The kit contains enough primary and secondary antibody to perform two Western blot experiments.

Background: c-Kit is a member of the subfamily of receptor tyrosine kinases that includes PDGF, CSF-1, and FLT3/flk-2 receptors (1,2). It plays a critical role in activation and growth in a number of cell types including hematopoietic stem cells, mast cells, melanocytes, and germ cells (3). Upon binding with its stem cell factor (SCF) ligand, c-Kit undergoes dimerization/oligomerization and autophosphorylation. Activation of c-Kit results in the recruitment and tyrosine phosphorylation of downstream SH2-containing signaling components including PLCγ, the p85 subunit of PI3 kinase, SHP2, and CrkL (4). Molecular lesions that impair the kinase activity of c-Kit are associated with a variety of developmental disorders (5), and mutations that constitutively activate c-Kit can lead to pathogenesis of mastocytosis and gastrointestinal stromal tumors (6). Tyr719 is located in the kinase insert region of the catalytic domain. c-Kit phosphorylated at Tyr719 binds to the p85 subunit of PI3 kinase in vitro and in vivo (7).

The c-Oncogene Antibody Sampler Kit provides an economical means of evaluating total levels of various oncogenic proteins. The kit contains enough primary and secondary antibodies to perform two Western blot experiments.
The C/EBP Antibody Sampler Kit provides an economical means of evaluating the C/EBP family of transcription factors and several phosphorylation sites that are involved in its activation. The kit includes enough antibody to perform two western blot experiments with each primary antibody.
This Cadherin-Catenin Antibody Sampler kit contains reagents to examine the total protein levels of key proteins found in cell-cell adherens junctions. The kit contains enough primary and secondary antibodies to perform two Western blot experiments.
The Calcium Ion Regulation Antibody Sampler Kit provides an economical way to investigate the regulation of calcium ions within the cell. The kit contains enough primary and secondary antibodies to perform two western blot experiments per primary antibody.
The Cardiogenesis Marker Antibody Sampler Kit provides an economical means of evaluating proteins involved in heart development. This kit contains enough antibody to perform two western blot experiments per primary antibody.
The Cas9 and Associated Proteins Antibody Sampler Kit provides an economical means of detecting Cas9 and Cas9-related family members. The kit includes enough antibody to perform two western blot experiments with each primary antibody.

Background: CRISPR-Cas (clustered regularly interspaced short palindromic repeats and CRISPR-associated proteins) are RNA-guided nuclease effectors that are utilized for precise genome editing in mammalian systems (1). Class 2 CRISPR systems rely on single-component effector proteins to mediate DNA interference (2). Several Class 2 CRISPR effector proteins, derived from specific bacterial species, are used for genome editing. Cas9 family of proteins, derived from S. pyogenes and S. aureus, are some of the most well characterized and widely used editing effector enzymes. Additional members of the Class2 CRISPR system include Cpf1 (CRISPR from Prevotella and Francisella) endonucleases (3). Cpf1 endonucleases, compared to Cas9 systems, have several unique features that increase the utility of CRISPR-based genome editing techniques: 1) Cpf1-mediated cleavage relies on a single and short CRISPR RNA (crRNA) without the requirement of a trans-activating crRNA (tracrRNA), 2) Cpf1 utilizes T-Rich protospacer adjacent motif (PAM) sequences rather than a G-Rich PAM, and 3) Cpf1 generates a staggered, rather than a blunt-ended, DNA double-stranded break (3). These features broaden the utility of using CRISPR-Cas systems for specific gene regulation and therapeutic applications. Several Cpf1 bacterial orthologs, e.g. Francisella novicida U112 and Acidaminococcus sp. BV3L6, have been characterized for CRISPR-mediated mammalian genome editing (3, 4).

The cdc25C Antibody Sampler Kit provides an economical means to investigate the entry of eukaryotic cells into mitosis. The kit contains enough primary and secondary antibodies to perform two Western blots with each antibody.

Background: Cdc25 is a protein phosphatase responsible for dephosphorylating and activating cdc2, a crucial step in regulating the entry of all eukaryotic cells into mitosis (1). cdc25C is constitutively phosphorylated at Ser216 throughout interphase by c-TAK1, while phosphorylation at this site is DNA damage-dependent at the G2/M checkpoint (2). When phosphorylated at Ser216, cdc25C binds to members of the 14-3-3 family of proteins, sequestering cdc25C in the cytoplasm and thereby preventing premature mitosis (3). The checkpoint kinases Chk1 and Chk2 phosphorylate cdc25C at Ser216 in response to DNA damage (4,5).

The CDK Antbody Sampler Kit provides and economical means of evaluating Cdk proteins. The kit contains enough primary and secondary antibodies to perform two western blot experiments.
The Cell Cycle Regulation Sampler Kit II provides an economical means of evaluating cell cycle proteins. The kit contains enough primary and secondary antibodies to perform two western blot experiments.
Cell Cycle Regulation Antibody Sampler kit offers an economical way of detecting eight integral cell cycle regulation proteins. The kit contains enough primary and secondary antibodies to perform two western blot experiments with each primary antibody.

Background: Eukaryotic cell cycle progression is dependent, in part, on the tightly regulated activity of cyclin dependent kinases (CDKs). Cyclin D/CDK4/6 activity occurs in mid-late G1 phase, upstream of CDK2/cyclin E activity. Both of these activities are required for hyperphosphorylation of the retinoblastoma gene product (pRb). pRb phosphorylation allows the release of S phase-promoting transcription factors and is indicative of the cell's commitment to proliferate. This point in the cell cycle is known as the restriction point. Cyclin protein levels oscillate throughout the cell cycle, and their availability is a means of controlling CDK activity and cell proliferation. Cyclin D is degraded through the ubiquitin proteasome pathway in the absence of mitogenic signaling. Ubiquitination of cyclin D1 is enhanced by phosphorylation at Thr286 by glycogen synthase kinase 3b (GSK-3b) (1). p27/Kip1, p57 Kip2 and p21 Waf1/Cip1 are members of the Cip/Kip family of cyclin-dependent kinase inhibitors. They form heterotrimeric complexes with cyclins and CDKs, inhibiting kinase activity and blocking progression through G1/S phase (2). However, p21 may enhance assembly and activity of cyclin D/CDK4/6 complexes (3). Levels of p21 and p27 protein are controlled through ubiquitination and proteasomal degradation (4). Levels of p27 are upregulated in quiescent cells and in cells treated with negative cell cycle regulators. p27 nuclear localization is controlled by Akt-dependent phosphorylation at Thr157 (5). The inhibitors of CDK4 (INK4) family include p15 INK4B, p16 INK4A, p18 INK4C, and p19 INK4D. All INK4 proteins selectively inhibit CDK4/6 activity, either in a binary complex, or in a ternary complex including cyclin D, resulting in inhibition of cell division (6,7).

The Cell Cycle/Checkpoint Antibody Sampler Kit provides a fast and economical means of evaluating multiple proteins involved in the cell cyle and checkpoint control. The kit contains enough primary and secondary antibody to perform four Western blot experiments.

Background: The cell division cycle demands accuracy to avoid the accumulation of genetic damage. This process is controlled by molecular circuits called "checkpoints" that are common to all eukaryotic cells (1). Checkpoints monitor DNA integrity and cell growth prior to replication and division at the G1/S and G2/M transitions, respectively. The cdc2-cyclin B kinase is pivotal in regulating the G2/M transition (2,3). Cdc2 is phosphorylated at Thr14 and Tyr15 during G2-phase by the kinases Wee1 and Myt1, rendering it inactive. The tumor suppressor protein retinoblastoma (Rb) controls progression through the late G1 restriction point (R) and is a major regulator of the G1/S transition (4). During early and mid G1-phase, Rb binds to and represses the transcription factor E2F (5). The phosphorylation of Rb late in G1-phase by CDKs induces Rb to dissociate from E2F, permitting the transcription of S-phase-promoting genes. In vitro, Rb can be phosphorylated at multiple sites by cdc2, cdk2, and cdk4/6 (6-8). DNA damage triggers both the G2/M and the G1/S checkpoints. DNA damage activates the DNA-PK/ATM/ATR kinases, which phosphorylate Chk at Ser345 (9), Chk2 at Thr68 (10) and p53 (11). The Chk kinases inactivate cdc25 via phosphorylation at Ser216, blocking the activation of cdc2.

The Cell Fractionation Antibody Sampler Kit provides an economical means for determining the purity of each distinctly separated subcellular fraction by western blot using Cell Signaling Technology's Cell Fractionation Kit #9038. This antibody sampler kit includes enough primary antibody to perform at least two western blots per primary antibody.
The Cellular Localization IF Antibody Sampler Kit provides an economical means for identification of cellular organelles by fluorescence immnuocytochemistry (IF-IC). This kit includes enough primary antibody to perform at least twenty IF-IC tests or two Western blots with each antibody.
The Class I HDAC Antibody Sampler Kit provides an economical means of detecting Class I HDAC proteins using control antibodies against HDAC1, HDAC2 and HDAC3. The kit contains enough primary antibodies to perform at least two western blot experiments.

Background: Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

The Class II HDAC Antibody Sampler Kit provides an economical means of detecting Class II HDAC proteins using control antibodies against HDAC4, HDAC5, HDAC6, and HDAC7. The kit contains enough primary antibodies to perform at least two western blot experiments.

Background: Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

The Cleaved Caspase Antibody Sampler Kit provides an economical means to evaluate the activation status of caspases by detecting their cleaved forms. The kit contains enough primary and secondary antibodies to perform two western blot experiments with each primary antibody.

Background: Apoptosis is a regulated physiological process leading to cell death. Caspases, a family of cysteine acid proteases, are central regulators of apoptosis. Initiator caspases (including 8, 9, 10 and 12) are closely coupled to proapoptotic signals. Once activated, these caspases cleave and activate downstream effector caspases (including 3, 6 and 7), which in turn cleave cytoskeletal and nuclear proteins like PARP, α-fodrin, DFF and lamin A, and induce apoptosis. Cytochrome c released from mitochondria is coupled to the activation of caspase-9, a key initiator caspase (1). Proapoptotic stimuli include the FasL, TNF-α, DNA damage and ER stress. Fas and TNFR activate caspases 8 and 10 (2), DNA damage leads to the activation of caspase-9 and ER stress leads to the calcium-mediated activation of caspase-12 (3). The inhibitor of apoptosis protein (IAP) family includes XIAP and survivin and functions by binding and inhibiting several caspases (4,5). Smac/Diablo, a mitochondrial protein, is released into the cytosol upon mitochondrial stress and competes with caspases for binding of IAPs. The interaction of Smac/Diablo with IAPs relieves the inhibitory effects of the IAPs on caspases (6).

The Cofilin Activation Antibody Sampler Kit provides an economical means to evaluate the presence and status of cofilin activation. The kit contains enough primary antibody to perform two western blot experiments per antibody.

Background: Cofilin and actin-depolymerization factor (ADF) are members of a family of essential conserved small actin-binding proteins that play pivotal roles in cytokinesis, endocytosis, embryonic development, stress response, and tissue regeneration (1). In response to stimuli, cofilin promotes the regeneration of actin filaments by severing preexisting filaments (2). The severing activity of cofilin is inhibited by LIMK or TESK phosphorylation at Ser3 of cofilin (3-5). Phosphorylation at Ser3 also regulates cofilin translocation from the nucleus to the cytoplasm (6).

The Cyclin Antibody Sampler Kit provides an economical means of evaluating the presence of cyclin proteins in cells. The kit contains enough primary and secondary antibodies to perform two western blot experiments with each antibody.
The Cytokeratin Antibody Sampler Kit provides an economical means to evaluate the presence and status of selected keratin proteins. The kit provides enough primary and secondary antibodies to perform two Western blot experiments per primary antibody.

Background: Keratins (cytokeratins) are intermediate filament proteins that are mainly expressed in epithelial cells. Keratin heterodimers composed of an acidic keratin (or type I keratin, keratins 9 to 23) and a basic keratin (or type II keratin, keratins 1 to 8) assemble to form filaments (1,2). Keratin isoforms demonstrate tissue- and differentiation-specific profiles that make them useful as research biomarkers (1). Research studies have shown that mutations in keratin genes are associated with skin disorders, liver and pancreatic diseases, and inflammatory intestinal diseases (3-6).

The Cytoskeletal Marker Antibody Sampler Kit provides an economical means to evaluate the presence and status of select cytoskeleton associated proteins. The kit provides enough primary antibodies to perform two western blots per primary antibody.
The Death Receptor Antibody Sampler Kit II provides an economical means to investigate members of the death receptor family. The kit includes enough antibody to perform two western blot experiments with each primary antibody.

Background: The tumor necrosis factor receptor family, which includes TNF-RI, TNF-R2, Fas, DR3, DR4, DR5, and DR6, plays an important role in the regulation of apoptosis in various physiological systems (1,2). The receptors are activated by a family of cytokines that include TNF, FasL, TWEAK, and TRAIL. They are characterized by a highly conserved extracellular region containing cysteine-rich repeats and a conserved intracellular region of about 80 amino acids termed the death domain (DD). The DD is important for transducing the death signal by recruiting other DD containing adaptor proteins (FADD, TRADD, RIP) to the death-inducing signaling complex (DISC) resulting in activation of caspases. The two receptors for TNF-α, TNF-R1 (55 kDa) and TNF-R2 (75 kDa) can mediate distinct cellular responses (3,4). In most cases cytotoxicity elicited by TNF has been reported to act through TNF-R1 (5,6). DR3/WSL-1/Apo-3/TRAMP/LARD is a TNFR family member containing the characteristic extracellular cysteine-repeats, transmembrane region, and an intracellular DD (7-11). DR3 is activated by its ligand Apo-3L/TWEAK to induce apoptosis and activation of NF-κB (12,13). Like TNF-R1, DR3 binds to the DD adaptor protein TRADD, which can then associate with other DD proteins like FADD and RIP as well as members of the TRAF family (7,8). Tissue expression of DR3 is very restricted, primarily seen on the surface of activated thymocytes and lymphocytes and plays an important role in thymocyte negative selection (7,8,14). Studies have also indicated an association with DR3 and rheumatoid arthritis (15,16). DR4 (TRAIL-RI, TNFRSF10A) and DR5 (TRAIL-R2, TNFRSF10B) are receptors for the cytokine TRAIL. Both receptors contain death domains that recruit DISC complexes triggering caspase activation and apoptosis (17-20). DR6, also known as TNFRSF21, is a TNFR family member able to induce apoptosis as well as activation of NF-κB and JNK (21). DR6 appears to play a critical role in the activation and differentiation of T and B lymphocytes (22,23). In the nervous system, β-amyloid precursor protein (APP) activates DR6 to trigger neuronal degeneration (24).

The Death Receptor Antibody Sampler Kit provides an economical means to investigate the machinery of death receptor-mediated apoptosis. The kit includes enough of each primary antibody to perform two western mini-blot experiments per primary.
The Di-Methyl-Histone H3 Antibody Sampler Kit provides a fast and economical means of evaluating methylation sites on histone H3. The kit contains enough primary and secondary antibodies to perform two western blots.

Background: The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. Originally thought to function as a static scaffold for DNA packaging, histones have now been shown to be dynamic proteins, undergoing multiple types of post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (1). Histone methylation is a major determinant for the formation of active and inactive regions of the genome and is crucial for the proper programming of the genome during development (2,3). Arginine methylation of histones H3 (Arg2, 17, 26) and H4 (Arg3) promotes transcriptional activation and is mediated by a family of protein arginine methyltransferases (PRMTs), including the co-activators PRMT1 and CARM1 (PRMT4) (4). In contrast, a more diverse set of histone lysine methyltransferases has been identified, all but one of which contain a conserved catalytic SET domain originally identified in the Drosophila Su(var)3-9, Enhancer of zeste, and Trithorax proteins. Lysine methylation occurs primarily on histones H3 (Lys4, 9, 27, 36, 79) and H4 (Lys20) and has been implicated in both transcriptional activation and silencing (4). Methylation of these lysine residues coordinates the recruitment of chromatin modifying enzymes containing methyl-lysine binding modules such as chromodomains (HP1, PRC1), PHD fingers (BPTF, ING2), tudor domains (53BP1), and WD-40 domains (WDR5) (5-8). The discovery of histone demethylases such as PADI4, LSD1, JMJD1, JMJD2, and JHDM1 has shown that methylation is a reversible epigenetic marker (9).

The DNA Cytosine Modification Antibody Sampler Kit provides an economical means of detecting the levels of cytosine modifications in DNA by dot blot using antibodies against 5-methylcytosine, 5-hydroxymethylcytosine, 5-formylcytosine, and 5-carboxylcytosine.

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).

This kit provides an economical means to analyze major signaling checkpoints in response to DNA damage. The kit contains primary and secondary antibodies to perform two Western blots with each antibody.
The Double Strand Breaks (DSB) Repair Antibody Sampler Kit provides an economical means to investigate repair of double-strand DNA breaks within the cell. The kit contains primary and secondary antibodies to perform two western blots with each antibody.