Dropping with the temps: Cool deals on CST mAbs | Learn More >>

Product listing: Akt Isoform Antibody Sampler Kit, UniProt ID P31749 #9940 to B Cell Signaling Antibody Sampler Kit, UniProt ID P06239 #9768

Akt Isoform Specific Antibody Sampler Kit provides an economical means of distinguishing between the three Akt isoforms, Akt1, Akt2 and Akt3, as well as a pan-Akt antibody. The kit provides enough primary and secondary antibodies to perform two Western blot experiments.

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).

The ALK Activation Antibody Sampler Kit provides an economical means to evaluate the activation status of multiple members of the ALK pathway, including phosphorylated ALK, Jak2, Jak3, Stat3, Stat5, PLCγ1, Akt, Src, and p44/42 MAPK. The kit includes enough antibody to perform two western blot experiments with each primary antibody.

Background: Anaplastic lymphoma kinase (ALK) is a tyrosine kinase receptor for pleiotrophin (PTN), a growth factor involved in embryonic brain development (1-3). In ALK-expressing cells, PTN induces phosphorylation of both ALK and the downstream effectors IRS-1, Shc, PLCγ, and PI3 kinase (1). ALK was originally discovered as a nucleophosmin (NPM)-ALK fusion protein produced by a translocation (4). Investigators have found that the NPM-ALK fusion protein is a constitutively active, oncogenic tyrosine kinase associated with anaplastic lymphoma (4). Research literature suggests that activation of PLCγ by NPM-ALK may be a crucial step for its mitogenic activity and involved in the pathogenesis of anaplastic lymphomas (5).A distinct ALK oncogenic fusion protein involving ALK and echinoderm microtubule-associated protein like 4 (EML4) has been described in the research literature from a non-small cell lung cancer (NSCLC) cell line, with corresponding fusion transcripts present in some cases of lung adenocarcinoma. The short, amino-terminal region of the microtubule-associated protein EML4 is fused to the kinase domain of ALK (6-8).

The Alzheimer's Disease Antibody Sampler Kit provides an economical means of evaluating Alzheimer's Disease-related signaling. The kit contains enough primary and secondary antibodies to perform two western blot experiments per primary antibody.
The AMPA Receptor (GluA) Antibody Sampler Kit provides an economical means of evaluating the four subunits of AMPARs. The kit contains enough primary and secondary antibodies to perform two western blot experiments with each 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 comprised of four subunits (GluR 1-4), 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 GluR 2-containing AMPARs, AMPARs that lack GluR 2 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 of AMPARs. Research studies have implicated activity changes in AMPARs in a variety of diseases including Alzheimer’s, amyotrophic lateral sclerosis (ALS), stroke, and epilepsy (1).

The AMPK and ACC Antibody Sampler Kit provides an economical means to investigate energy homeostasis and fatty acid synthesis within the cell. The kit contains primary and secondary antibodies to perform two Western blots with each antibody.
The AMPK Substrate Antibody Sampler Kit provides an economical means of detecting total and phosphorylated substrates of AMPK. The kit provides enough antibody to perform two western blots with each primary antibody.

Background: AMP-activated protein kinase (AMPK) is highly conserved from yeast to plants and animals and plays a key role in the regulation of energy homeostasis (1). AMPK is a heterotrimeric complex composed of a catalytic α subunit and regulatory β and γ subunits, each of which is encoded by two or three distinct genes (α1, 2; β1, 2; γ1, 2, 3) (2). The kinase is activated by an elevated AMP/ATP ratio due to cellular and environmental stress, such as heat shock, hypoxia, and ischemia (1). The tumor suppressor LKB1, in association with accessory proteins STRAD and MO25, phosphorylates AMPKα at Thr172 in the activation loop, and this phosphorylation is required for AMPK activation (3-5).AMPK phosphorylates a number of targets controlling cellular processes such as metabolism, cell growth, and autophagy (6). It suppresses the activity of the mammalian target of rapamycin (mTOR), that plays a key role in promoting cell growth. The regulatory associated protein of mTOR (Raptor) was identified as an mTOR binding partner that mediates mTOR signaling to downstream targets (7,8). Raptor binds to mTOR substrates, including 4E-BP1 and p70 S6 kinase, through their TOR signaling (TOS) motifs and is required for mTOR-mediated phosphorylation of these substrates (9,10). AMPK directly phosphorylates Raptor at Ser722/Ser792, and this phosphorylation is essential for inhibition of the raptor-containing mTOR complex 1 (mTORC1) and induces cell cycle arrest when cells are stressed for energy (11). AMPK also promotes autophagy by directly phosphorylating ULK1 (11,12). ULK1 is a Ser/Thr kinase required for the Initiation and formation of the autophagosome. AMPK, activated during low nutrient conditions, directly phosphorylates ULK1 at multiple sites including Ser317, Ser555, and Ser777 (11,12). Conversely, mTOR, which is a regulator of cell growth and an inhibitor of autophagy, phosphorylates ULK1 at Ser757 and disrupts the interaction between ULK1 and AMPK (11). AMPK can also directly phosphorylate Beclin-1, a component of the complex downstream of ULK1 in autophagosome formation that activates the class III phosphatidylinositol 3-kinase VPS34. AMPK phosphorylates Beclin-1 at Ser93 and Ser96 residues in human, which correspond to murine Ser91 and Ser94 (14).

The AMPK Subunit Antibody Sampler Kit provides an economical means to investigate the role played by all AMPK subunits in cellular energy homeostasis. The kit contains enough primary and secondary antibodies to perform two Western blots with each antibody.

Background: AMP-activated protein kinase (AMPK) is highly conserved from yeast to plants and animals and plays a key role in the regulation of energy homeostasis (1). AMPK is a heterotrimeric complex composed of a catalytic α subunit and regulatory β and γ subunits, each of which is encoded by two or three distinct genes (α1, 2; β1, 2; γ1, 2, 3) (2). The kinase is activated by an elevated AMP/ATP ratio due to cellular and environmental stress, such as heat shock, hypoxia, and ischemia (1). The tumor suppressor LKB1, in association with accessory proteins STRAD and MO25, phosphorylates AMPKα at Thr172 in the activation loop, and this phosphorylation is required for AMPK activation (3-5). AMPKα is also phosphorylated at Thr258 and Ser485 (for α1; Ser491 for α2). The upstream kinase and the biological significance of these phosphorylation events have yet to be elucidated (6). The β1 subunit is post-translationally modified by myristoylation and multi-site phosphorylation including Ser24/25, Ser96, Ser101, Ser108, and Ser182 (6,7). Phosphorylation at Ser108 of the β1 subunit seems to be required for the activation of AMPK enzyme, while phosphorylation at Ser24/25 and Ser182 affects AMPK localization (7). Several mutations in AMPKγ subunits have been identified, most of which are located in the putative AMP/ATP binding sites (CBS or Bateman domains). Mutations at these sites lead to reduction of AMPK activity and cause glycogen accumulation in heart or skeletal muscle (1,2). Accumulating evidence indicates that AMPK not only regulates the metabolism of fatty acids and glycogen, but also modulates protein synthesis and cell growth through EF2 and TSC2/mTOR pathways, as well as blood flow via eNOS/nNOS (1).

The Angiogenesis Antibody Sampler Kit provides an economical means to investigate the angiogenic pathway downstream of VEGFR2. The kit contains enough primary antibody to perform two western blots per primary antibody.
The Jak Isoform Antibody Sampler Kit provides an economical means to examine several Jak isoforms. The kit contains enough primary and secondary antibodies to perform two Western blot experiments per primary antibody.

Background: Members of the Janus family of tyrosine kinases (Jak1, Jak2, Jak3, and Tyk2) are activated by ligands binding to a number of associated cytokine receptors (1). Upon cytokine receptor activation, Jak proteins become autophosphorylated and phosphorylate their associated receptors to provide multiple binding sites for signaling proteins. These associated signaling proteins, such as Stats (2), Shc (3), insulin receptor substrates (4), and focal adhesion kinase (FAK) (5), typically contain SH2 or other phospho-tyrosine-binding domains.

The NF-κB Pathway Sampler Kit contains reagents to examine the activation state and total protein levels of key proteins in the NF-κB pathway: IKKα, IKKβ, NF-κB p65/RelA and IκBα. The kit contains enough primary and secondary antibodies to perform two Western blot experiments per primary antibody.

Background: The transcriptional nuclear factor κB (NF-κB)/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins. Activation occurs via phosphorylation of IκBα at Ser32 and Ser36, resulting in the ubiquitin-mediated proteasome-dependent degradation of IκBα and the release and nuclear translocation of active NF-κB dimers. The regulation of IκBβ and IκBε is similar to that of IκBα, however, the phosphorylation and degradation of these proteins occurs with much slower kinetics. Phosphorylation of IκBβ occurs at Ser/Thr19 and Ser23, while IκBε can be phosphorylated at Ser18 and Ser22. The key regulatory step in this pathway involves activation of a high molecular weight IkappaB kinase (IKK) complex, consisting of three tightly associated IKK subunits. IKKα and IKKβ serve as the catalytic subunits of the kinase. Activation of IKK depends on phosphorylation at Ser177 and Ser181 in the activation loop of IKKβ (176 and 180 in IKKα). NF-κB-inducing kinase (NIK), TANK-binding kinase 1 (TBK1), and its homolog IKKε (IKKi), phosphorylate and activate IKKα and IKKβ.

The Phospho-Erk1/2 Pathway Sampler Kit provides an economical means of evaluating multiple members of the Erk pathway as well as their activation state. The kit contains enough primary and secondary antibodies to perform two Western blot experiments.

Background: Mitogen-activated protein kinases (MAPKs) are a widely conserved family of serine/threonine protein kinases involved in many cellular programs, such as cell proliferation, differentiation, motility, and death. The p44/42 MAPK (Erk1/2) signaling pathway can be activated in response to a diverse range of extracellular stimuli including mitogens, growth factors, and cytokines (1-3), and research investigators consider it an important target in the diagnosis and treatment of cancer (4). Upon stimulation, a sequential three-part protein kinase cascade is initiated, consisting of a MAP kinase kinase kinase (MAPKKK or MAP3K), a MAP kinase kinase (MAPKK or MAP2K), and a MAP kinase (MAPK). Multiple p44/42 MAP3Ks have been identified, including members of the Raf family, as well as Mos and Tpl2/COT. MEK1 and MEK2 are the primary MAPKKs in this pathway (5,6). MEK1 and MEK2 activate p44 and p42 through phosphorylation of activation loop residues Thr202/Tyr204 and Thr185/Tyr187, respectively. Several downstream targets of p44/42 have been identified, including p90RSK (7) and the transcription factor Elk-1 (8,9). p44/42 are negatively regulated by a family of dual-specificity (Thr/Tyr) MAPK phosphatases, known as DUSPs or MKPs (10), along with MEK inhibitors, such as U0126 and PD98059.

The Phospho-p38 MAPK Pathway Sampler Kit provides an economical means to evaluate the activation status of multiple members of the p38 MAPK pathway, including phosphorylated MSK1, p38 MAPK, MKK3/MKK6, ATF-2, HSP27 and MAPKAPK-2. The kit includes enough primary and secondary antibodies to perform two Western blot experiments.

Background: p38 MAP kinase (MAPK), also called RK (1) or CSBP (2), is the mammalian orthologue of the yeast HOG kinase that participates in a signaling cascade controlling cellular responses to cytokines and stress (1-4). Four isoforms of p38 MAPK, p38α, β, γ (also known as Erk6 or SAPK3), and δ (also known as SAPK4) have been identified. Similar to the SAPK/JNK pathway, p38 MAPK is activated by a variety of cellular stresses including osmotic shock, inflammatory cytokines, lipopolysaccharide (LPS), UV light, and growth factors (1-5). MKK3, MKK6, and SEK activate p38 MAPK by phosphorylation at Thr180 and Tyr182. Activated p38 MAPK has been shown to phosphorylate and activate MAPKAP kinase 2 (3) and to phosphorylate the transcription factors ATF-2 (5), Max (6), and MEF2 (5-8). SB203580 (4-(4-fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(4-pyridyl)-imidazole) is a selective inhibitor of p38 MAPK. This compound inhibits the activation of MAPKAPK-2 by p38 MAPK and subsequent phosphorylation of HSP27 (9). SB203580 inhibits p38 MAPK catalytic activity by binding to the ATP-binding pocket, but does not inhibit phosphorylation of p38 MAPK by upstream kinases (10).

The StemLight™ iPS cell Reprogramming Antibody Kit contains a panel of antibodies for the detection of various proteins, combinations of which have been used to reprogram somatic cells to Induced Pluripotent Stem (iPS) cells. The kit can be used to track efficiency of expression of the reprogramming factors following transfection, viral transduction and other means of protein delivery. The kit components are pre-optimized for parallel use in immunofluorescent analysis at a standard dilution, but components are also validated for use in other applications --please refer to individual data sheet information for application specific recommendations. Enough reagents are provided for 160 immunofluorescent assays based on a working volume of 100 μl.

Background: Pluripotency is the ability of a cell to differentiate into cell types of the three germ layers, the endoderm, ectoderm and mesoderm. It is a property shared by embryonic stem cells, embryonic carcinoma and induced pluripotent cells.Oct-4, Sox2 and Nanog are key transcriptional regulators that are highly expressed in pluripotent cells (1). Together they form a transcriptional network that maintains cells in a pluripotent state (2,3). Over-expression of Oct-4 and Sox2 along with Klf4 and c- Myc can induce pluripotency in both mouse and human somatic cells, highlighting their roles as key regulators of the transcrip- tional network necessary for renewal and pluripotency (4-5). It has also been demonstrated that overexpression of Oct-4, Sox2, Nanog and Lin28 can induce pluripotency in human somatic cells (6). Upon differentiation of pluripotent cultures, expression of Oct-4, Nanog and Sox2 is downregulated.SSEA4, TRA-1-81 and TRA-1-60 antibodies recognize antigens expressed on the cell surface of all pluripotent cells. SSEA4 recognizes a glycolipid carbohydrate epitope (7). TRA-1-60(S) and TRA-1-81 antibodies recognize different proteoglycan epitopes on variants of the same protein, podocalyxin (8). These epitopes are neuraminadase sensitive and resistant, respectively. Reactivity of SSEA4, TRA-1-81 and TRA-1-60 antibodies with their respective cell surface markers are lost upon differentiation of pluripotent cells, corresponding with a loss of pluripotent potential (9).

The StemLight™ Pluripotency Antibody Kit contains a panel of antibodies for the detection of proteins that are specifically expressed in human pluripotent cells. The kit can be used to track the pluripotent potential of human embryonic stem (ES) or induced pluripotent (iPS) cells. The loss of these markers indicates a loss of pluripotency or differentiation of the culture. The kit components are pre-optimized for parallel use in immunofluorescent analysis. Enough reagents are provided for 100 assays based on a working volume of 100 µl.

Background: Pluripotency is the ability of a cell to differentiate into cell types of the three germ layers, the endoderm, ectoderm and mesoderm. It is a property shared by embryonic stem cells, embryonic carcinoma and induced pluripotent cells.Oct-4, Sox2 and Nanog are key transcriptional regulators that are highly expressed in pluripotent cells (1). Together they form a transcriptional network that maintains cells in a pluripotent state (2,3). Over-expression of Oct-4 and Sox2 along with Klf4 and c- Myc can induce pluripotency in both mouse and human somatic cells, highlighting their roles as key regulators of the transcrip- tional network necessary for renewal and pluripotency (4-5). It has also been demonstrated that overexpression of Oct-4, Sox2, Nanog and Lin28 can induce pluripotency in human somatic cells (6). Upon differentiation of pluripotent cultures, expression of Oct-4, Nanog and Sox2 is downregulated.SSEA4, TRA-1-81 and TRA-1-60 antibodies recognize antigens expressed on the cell surface of all pluripotent cells. SSEA4 recognizes a glycolipid carbohydrate epitope (7). TRA-1-60(S) and TRA-1-81 antibodies recognize different proteoglycan epitopes on variants of the same protein, podocalyxin (8). These epitopes are neuraminadase sensitive and resistant, respectively. Reactivity of SSEA4, TRA-1-81 and TRA-1-60 antibodies with their respective cell surface markers are lost upon differentiation of pluripotent cells, corresponding with a loss of pluripotent potential (9).

The StemLight™ Surface Marker Kit contains a panel of antibodies for the detection of antigens that are specifically expressed on the surface of human pluripotent cells. The kit can be used to track the pluripotent potential of human embryonic stem (ES) or induced pluripotent (iPS) cells. The loss of these markers indicates a loss of pluripotency or differentiation of the culture. The kit components are pre-optimized for parallel use in immunofluorescent analysis.

Background: Pluripotency is the ability of a cell to differentiate into cell types of the three germ layers, the endoderm, ectoderm, and mesoderm. It is a property shared by embryonic stem cells, embryonic carcinoma, and induced pluripotent cells.SSEA4, TRA-1-81, and TRA-1-60 antibodies recognize antigens expressed on the cell surface of all pluripotent cells. SSEA4 recognizes a glycolipid carbohydrate epitope (1). TRA-1-60(S) and TRA-1-81 antibodies recognize different proteoglycan epitopes on variants of the same protein, podocalyxin (2). These epitopes are neuraminidase sensitive and resistant, respectively. Reactivity of SSEA4, TRA-1-81 and TRA-1-60 antibodies with their respective cell surface markers are lost upon differentiation of pluripotent cells, corresponding with a loss of pluripotent potential (3).

StemLight™ Pluripotency Transcription Factor Antibody Kit contains a panel of antibodies for the detection of Oct-4, Nanog, and Sox2, key components of the core pluripotency transcription network in embryonic stem (ES) and induced pluripotent stem (iPS) cells. The kit can be used to track the pluripotent potential of human ES or iPS cells. The loss of these markers indicates a loss of pluripotency or differentiation of the culture. The kit components are pre-optimized for parallel use in immunofluorescent analysis at a standard dilution, but components are also validated for use in other applications - please refer to individual datasheet information for application specific recommendations. Enough reagents are provided for 160 immunofluorescent assays based on a working volume of 100 μl.

Background: Pluripotency is the ability of a cell to differentiate into cell types of the three germ layers, the endoderm, ectoderm and mesoderm. It is a property shared by embryonic stem cells, embryonic carcinoma, and induced pluripotent cells.Oct-4, Sox2, and Nanog are key transcriptional regulators that are highly expressed in pluripotent cells (1). Together they form a transcriptional network that maintains cells in a pluripotent state (2,3). Over-expression of Oct-4 and Sox2, along with KLF4 and c-Myc can induce pluripotency in both mouse and human somatic cells, highlighting their roles as key regulators of the transcriptional network necessary for renewal and pluripotency (4-5). It has also been demonstrated that overexpression of Oct-4, Sox2, Nanog, and Lin28 can induce pluripotency in human somatic cells (6). Upon differentiation of pluripotent cultures, expression of Oct-4, Nanog, and Sox2 is downregulated.

The Apoptosis Antibody Sampler Kit provides an economical means to evaluate the levels of inactive and active caspases. The kit contains enough primary and secondary antibodies to perform two Western blot experiments with each 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 Apoptosis Antibody Sampler Kit (Mouse Specific) is designed for use with mouse samples and offers an economical means to evaluate the levels of active and inactive caspases. The kit contains enough primary and secondary antibodies to perform two Western blot experiments with each 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 Apoptosis/Necroptosis Antibody Sampler Kit provides an economical means of detecting markers for apoptosis and necroptosis. The kit contains enough primary antibody to perform at least two western blot experiments.

Background: Apoptosis is a regulated physiological process leading to cell death (1,2). Caspases, a family of cysteine acid proteases, are central regulators of apoptosis. Caspases are synthesized as inactive zymogens containing a pro-domain followed by large (p20) and small subunits (p10) that are proteolytically processed in a cascade of caspase activity. 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. Apoptosis induced through the extrinsic mechanisms involving death receptors in the tumor necrosis factor receptor superfamily activates caspase-8. Activated caspase-8 cleaves and activates downstream effector caspases, such as caspase-1, -3, -6, and -7. Caspase-3 is a critical executioner of apoptosis, as it is either partially or totally responsible for the proteolytic cleavage of many key proteins, such as the nuclear enzyme poly (ADP-ribose) polymerase (PARP).Necroptosis, a regulated pathway for necrotic cell death, is triggered by a number of inflammatory signals, including cytokines in the tumor necrosis factor (TNF) family, pathogen sensors such as toll-like receptors (TLRs), and ischemic injury (3,4). Necroptosis is negatively regulated by caspase-8 mediated apoptosis in which the kinase RIP/RIPK1 is cleaved (5). Furthermore, necroptosis is inhibited by a small molecule inhibitor of RIP, necrostatin-1 (Nec-1) (6). Research studies show that necroptosis contributes to a number of pathological conditions, and Nec-1 has been shown to provide neuroprotection in models such as ischemic brain injury (7). RIP is phosphorylated at several sites within the kinase domain that are sensitive to Nec-1, including Ser14, Ser15, Ser161, and Ser166 (8). Phosphorylation drives association with RIP3, which is required for necroptosis (9-11). Mixed lineage kinase domain-like protein (MLKL) is a pseudokinase that was identified as downstream target of RIP3 in the necroptosis pathway (12). During necroptosis RIP3 is phosphorylated at Ser227, which recruits MLKL and leads to its phosphorylation at Thr357 and Ser358 (12). Knockdown of MLKL through multiple mechanisms results in inhibition of necroptosis (13). While the precise mechanism for MLKL-induced necroptosis is unclear, some studies have shown that necroptosis leads to oligomerization of MLKL and translocation to the plasma membrane, where it effects membrane integrity (14-17).

The Aurora A/B Substrate Antibody Sampler Kit provides an economical means to investigate the G2/M phase of the cell cycle. The kit contains enough primary antibody to perform two western blots per primary antibody.

Background: Aurora kinases belong to a highly conserved family of mitotic serine/threonine kinases with three members identified among mammals: Aurora A, B, and C (1,2). Studies on the temporal expression pattern and subcellular localization of Aurora kinases in mitotic cells suggest an association with mitotic structure. Aurora kinase functional influences span from G2 phase to cytokinesis and may be involved in key cell cycle events such as centrosome duplication, chromosome bi-orientation and segregation, cleavage furrow positioning, and ingression (3). Aurora A is detected at the centrosomes, along mitotic spindle microtubules, and in the cytoplasm of mitotically proliferating cells. Aurora A protein levels are low during G1 and S phases and peak during the G2/M phase of the cell cycle. Phosphorylation of Aurora A at Thr288 in its catalytic domain increases kinase activity. Aurora A is involved in centrosome separation, maturation, and spindle assembly and stability. Expression of Aurora B protein also peaks during the G2/M phase of the cell cycle; Aurora B kinase activity peaks at the transition from metaphase to the end of mitosis. Aurora B associates with chromosomes during prophase prior to relocalizing to the spindle at anaphase. Aurora B regulates chromosome segregation through the control of microtubule-kinetochore attachment and cytokinesis. Expression of both Aurora A and Aurora B during the G2/M phase transition is tightly coordinated with histone H3 phosphorylation (4,5); research investigators have observed overexpression of these kinases in a variety of human cancers (2,4). Aurora C localizes to the centrosome from anaphase to cytokinesis and both mRNA and protein levels peak during G2/M phase. Although typical Aurora C expression is limited to the testis, research studies report overexpression of Aurora C is detected in various cancer cell lines (6).

The Aurora Antibody Sampler Kit provides an economical means to investigate the G2/M phase of the cell cycle. The kit contains enough primary and secondary antibodies to perform two western blots with each antibody.

Background: Aurora kinases belong to a highly conserved family of mitotic serine/threonine kinases with three members identified among mammals: Aurora A, B, and C (1,2). Studies on the temporal expression pattern and subcellular localization of Aurora kinases in mitotic cells suggest an association with mitotic structure. Aurora kinase functional influences span from G2 phase to cytokinesis and may be involved in key cell cycle events such as centrosome duplication, chromosome bi-orientation and segregation, cleavage furrow positioning, and ingression (3). Aurora A is detected at the centrosomes, along mitotic spindle microtubules, and in the cytoplasm of mitotically proliferating cells. Aurora A protein levels are low during G1 and S phases and peak during the G2/M phase of the cell cycle. Phosphorylation of Aurora A at Thr288 in its catalytic domain increases kinase activity. Aurora A is involved in centrosome separation, maturation, and spindle assembly and stability. Expression of Aurora B protein also peaks during the G2/M phase of the cell cycle; Aurora B kinase activity peaks at the transition from metaphase to the end of mitosis. Aurora B associates with chromosomes during prophase prior to relocalizing to the spindle at anaphase. Aurora B regulates chromosome segregation through the control of microtubule-kinetochore attachment and cytokinesis. Expression of both Aurora A and Aurora B during the G2/M phase transition is tightly coordinated with histone H3 phosphorylation (4,5); research investigators have observed overexpression of these kinases in a variety of human cancers (2,4). Aurora C localizes to the centrosome from anaphase to cytokinesis and both mRNA and protein levels peak during G2/M phase. Although typical Aurora C expression is limited to the testis, research studies report overexpression of Aurora C is detected in various cancer cell lines (6).

The Autophagosome Marker Antibody Sampler Kit provides an economical means to investigate the accumulation of autophagosomes within the cell. The kit contains enough primary and secondary antibodies to perform two western blots per primary antibody.
The Autophagy Antibody Sampler Kit provides an economical means to investigate the molecular machinery of autophagy within the cell. The kit contains enough primary and secondary antibodies to perform two Western blot experiments.

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). Autophagy is generally activated by conditions of nutrient deprivation but has also been 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 referred to as autophagy-related (Atg) genes. Formation of the autophagosome involves a ubiquitin-like conjugation system in which Atg12 is covalently bound to Atg5 and targeted to autophagosome vesicles (4-6). This conjugation reaction is mediated by the ubiquitin E1-like enzyme Atg7 and the E2-like enzyme Atg10 (7,8).

The Autophagy Atg8 Family Antibody Sampler Kit provides an economical means of detecting each of the Atg8 family members. The kit contains enough primary antibody to perform at least two western blot experiments.

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). Autophagy is generally activated by conditions of nutrient deprivation, but it has also been associated with a number of physiological processes, including development, differentiation, neurodegenerative diseases, infection, and cancer (3).Atg8 is a ubiquitin-like protein that is critical for autophagosome formation. Atg8 is synthesized as a precursor protein that is processed by the cysteine protease Atg4, followed by lipidation with phosphatidylethanolamine (PE) in a ubiqutin-like conjugation pathway involving Atg7 and Atg3 (4). This processing of Atg8, which is described as a conversion from type-I to type-II forms, is frequently described as a marker for autophagy. The type-II form of Atg8 is incorporated into maturing autophagosomes and leads to the recruitment of additional autophagy components, including cargo receptors like SQSTM1/p62. While yeast has a single Atg8 gene, many eukaryotes have at least six orthologs, including three microtubule-associated protein 1 light chain 3 (MAP1LC3/LC3) family members (LC3A, LC3B, and LC3C) and three GABAA receptor associated protein (GABARAP) family members (GABARAP, GABARAPL1/GEC1, and GABARAPL2/GATE-16). While highly conserved, these various family members can have important differences in their post-translational processing, expression profile, and protein interactions including distinct cargo receptor. This complexity within the Atg8 family is critical for selective mechanisms of autophagy that have been reported (5, 6).

The Autophagy Induction (ULK1 Complex) Antibody Sampler Kit provides an economical means of detecting target proteins in the ULK1 complex. The kit contains enough antibody to perform at least two western blot experiments per primary antibody.
The Autophagy Vesicle Elongation (Atg12 Conjugation) Antibody Sampler Kit provides an economical means of detecting proteins related to autophagy vesicle elongation pathway. The kit contains enough antibody to perform two western blot experiments per primary antibody.
The Autophagy Vesicle Elongation (LC3 Conjugation) Antibody Sampler Kit provides an economical means of detecting target proteins related to autophagy vesicle elongation pathway. The kit contains enough antibody to perform two western blots per primary.
The Autophagy Vesicle Nucleation Antibody Sampler Kit provides an economical means of detecting target proteins involved in autophagosome formation and maturation. The kit contains enough antibody to perform two western blot experiments per primary antibody.
The B Cell Signaling Antibody Sampler Kit II provides an economical means to examine key signaling proteins commonly associated with B cell activation. The provided antibodies allow monitoring of both total protein levels and the phosphorylation state. The kit includes enough antibody to perform two western blot experiments with each primary antibody.
The B Cell Signaling Antibody Sampler Kit provides an economical means to examine key signaling proteins commonly associated with B cell activation. The provided antibodies allow monitoring of both total protein levels and the phosphorylation state. The kit includes enough primary and secondary antibody to perform two western mini-blot experiments.