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Product listing: Anti-rabbit IgG (H+L), F(ab')2 Fragment (Alexa Fluor® 647 Conjugate) #4414 to SignalSilence® Akt2 siRNA I (Mouse Specific), UniProt ID Q60823 #6407

$142
250 µl
Anti-rabbit IgG (H+L) F(ab')2 Fragment was conjugated to Alexa Fluor® 647 fluorescent dye under optimal conditions and formulated at 2 mg/ml. This F(ab')2 fragment product results in less non-specific binding, as it lacks the Fc domain that can bind to the cells with Fc receptors.
APPLICATIONS

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

$199
250 µl
Anti-rabbit IgG (H+L), F(ab')2 Fragment was conjugated to phycoerythrin (PE) under optimal conditions. This F(ab')2 fragment product results in less non-specific binding, as it lacks the Fc domain that can bind to the cells with Fc receptors.
APPLICATIONS

Application Methods: Flow Cytometry

$203
250 µl
Anti-rabbit IgG (H+L), F(ab')2 Fragment was conjugated to phycoerythrin (PE) under optimal conditions and formulated at 1 mg/ml. This F(ab')2 fragment results in less non-specific binding to cells through Fc receptors.
APPLICATIONS

Application Methods: Flow Cytometry

$131
1 ml
This Cell Signaling Technology antibody is immobilized via covalent binding of primary amino groups to N-hydroxysuccinimide (NHS)-activated Sepharose® beads. Anti-rabbit IgG F(ab') 2 Fragment (Sepharose® Bead Conjugate) is useful for the immunoprecipitation of antibodies raised in rabbit.
APPLICATIONS

Application Methods: Immunoprecipitation

$142
1 ml
Affinity purified goat anti-rabbit IgG (H&L) antibody is conjugated to calf intestinal alkaline phosphatase. This product has been optimized for use as a secondary antibody in western blotting and ELISA applications.
APPLICATIONS

Application Methods: ELISA, Western Blotting

Background: The alkaline phosphatase (AP) conjugated secondary antibodies are utilized in conjunction with specific chemiluminescent or other substrates for detection on western blots. One of the advantages of AP conjugation is that the reaction rate remains linear for a long period of time.

$76
100 µl
$142
1 ml
$452
5 ml
Designed for use with rabbit polyclonal and monoclonal antibodies, this affinity purified goat anti-rabbit IgG (heavy and light chain) antibody is conjugated to horseradish peroxidase(HRP) for chemiluminescent detection.  This product is thoroughly validated with CST primary antibodies and will work optimally with the CST western immunoblotting protocol, ensuring accurate and reproducible results.
APPLICATIONS

Application Methods: Western Blotting

Background: Chemiluminescence systems have emerged as the best all-around method for western blot detection. They eliminate the hazards associated with radioactive materials and toxic chromogenic substrates. The speed and sensitivity of these methods are unequalled by traditional alternatives, and because results are generated on film, it is possible to record and store data permanently. Blots detected with chemiluminescent methods are easily stripped for subsequent reprobing with additional antibodies. HRP-conjugated secondary antibodies are utilized in conjunction with specific chemiluminescent substrates to generate the light signal. HRP conjugates have a very high turnover rate, yielding good sensitivity with short reaction times.

$121
250 µl
Anti-rat IgG (H+L) antibody was conjugated to Alexa Fluor® 488 fluorescent dye under optimal conditions and formulated at 2 mg/ml. This product has been optimized for use as a secondary antibody in immunofluorescent applications. Cell Signaling Technology’s strict quality control procedures assure that each conjugate provides optimal specificity and fluorescence.
APPLICATIONS

Application Methods: Immunofluorescence (Immunocytochemistry)

$121
250 µl
Anti-rat IgG (H+L) antibody was conjugated to Alexa Fluor® 555 fluorescent dye under optimal conditions and formulated at 2 mg/mL.
APPLICATIONS

Application Methods: Immunofluorescence (Immunocytochemistry)

$121
250 µl
Anti-rat IgG (H+L) was conjugated to Alexa Fluor® 647 fluorescent dye under optimal conditions and formulated at 2 mg/ml.
APPLICATIONS

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

$142
1 ml
Affinity purified goat anti-rat IgG (heavy and light chain) antibody is conjugated to horseradish peroxidase(HRP) for chemiluminescent detection.  This product is thoroughly validated with CST primary antibodies and will work optimally with the CST western immunoblotting protocol, ensuring accurate and reproducible results.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Western Blotting

Background: Chemiluminescence systems have emerged as the best all-around method for western blot detection. They eliminate the hazards associated with radioactive materials and toxic chromogenic substrates. The speed and sensitivity of these methods are unequalled by traditional alternatives, and because results are generated on film, it is possible to record and store data permanently. Blots detected with chemiluminescent methods are easily stripped for subsequent reprobing with additional antibodies. HRP-conjugated secondary antibodies are utilized in conjunction with specific chemiluminescent substrates to generate the light signal. HRP conjugates have a very high turnover rate, yielding good sensitivity with short reaction times.

$146
100 µl
Affinity purified mouse anti-rabbit IgG (Conformation Specific) antibody. This product has been optimized for use as a secondary antibody in Western blotting applications.
APPLICATIONS

Application Methods: Western Blotting

$172
100 µl
Affinity purified mouse anti-rabbit IgG (Conformation Specific) HRP Conjugate antibody.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Western Blotting

$178
100 µl
APPLICATIONS

Application Methods: Western Blotting

$142
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups.
APPLICATIONS

Application Methods: Western Blotting

$172
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups.
APPLICATIONS

Application Methods: Western Blotting

$39
1 ml
$367
15 ml
SignalStain® Boost IHC Detection Reagent (HRP, Mouse) is a ready-to-use solution intended for use in immunohistochemical assays to detect mouse primary antibodies. SignalStain® Boost IHC Detection Reagent (HRP, Mouse) is a highly sensitive, one-step, polymer-based detection reagent that is specific for mouse IgG. It can be used to visualize targets in both paraffin-embedded and frozen tissue sections and it is compatible with all peroxidase-based substrates.
APPLICATIONS

Application Methods: Immunohistochemistry (Paraffin)

$39
1 ml
$367
15 ml
SignalStain® Boost IHC Detection Reagent (HRP, Rabbit) is a ready-to-use solution intended for use in immunohistochemical assays to detect rabbit primary antibodies. SignalStain® Boost IHC Detection Reagent (HRP, Rabbit) is a highly sensitive, one-step, polymer-based detection reagent that is specific for rabbit IgG. It can be used to visualize targets in both paraffin-embedded and frozen tissue sections and it is compatible with all peroxidase-based substrates.
APPLICATIONS

Application Methods: Immunohistochemistry (Paraffin)

Senescence Associated Secretory Phenotype (SASP) Antibody Sampler Kit provides an economical means of detecting multiple components of the SASP. The kit includes enough antibody to perform two western blot experiments with each primary antibody.

Background: Senescence is characterized by stable stress-induced proliferative arrest and resistance to mitogenic stimuli, as well as the secretion of proteins such as cytokines, growth factors and proteases. These secreted proteins comprise the senescence-associated secretory phenotype (SASP). Senescent cells are thought to accumulate as an organism ages, and contribute to age-related diseases, including cancer, through promotion of inflammation and disruption of normal cellular function (1,2). The composition of the SASP varies, and SASP components can be either beneficial or deleterious in human disease, depending on the context (3).Senescence Associated Secretory Phenotype (SASP) Antibody Sampler Kit provides a collection of antibodies to various SASP components, including TNF-alpha, interleukin-6 (IL-6), the multifunctional cytokine IL-1beta, the chemokines CXCL10, RANTES/CCL5 and MCP-1, the matrix metalloprotease MMP3, and the serine-protease inhibitor PAI-1.

The Senescence Marker Antibody Sampler Kit provides an economical means of detecting multiple markers of cellular senescence. The kit includes enough antibody to perform two western blot experiments with each primary antibody.

Background: Senescence is characterized by stable stress-induced proliferative arrest and resistance to mitogenic stimuli, as well as the secretion of proteins such as cytokines, growth factors and proteases. These secreted proteins comprise the senescence-associated secretory phenotype (SASP). Senescent cells are thought to accumulate as an organism ages, and contribute to age-related diseases, including cancer, through promotion of inflammation and disruption of normal cellular function (1,2).Because there is no single biomarker that can be used to definitively identify senescent cells, researchers must rely on a collection of biomarkers commonly associated with senescence. The Senescence Marker Antibody Sampler Kit provides a collection of antibodies to commonly used biomarkers of senescence-associated cell cycle arrest (p16 INK4A, p21 Waf1/Cip1), senescence-associated DNA damage (gamma-Histone H2A.X), and the SASP (HMGB1, IL-6, TNF-alpha, MMP3). The kit also includes an antibody to Lamin B1, which is frequently reduced in senescent cells.

The Sequestosome Signaling Antibody Sampler Kit contains reagents to investigate sequestosome signaling within the cell. The kit contains enough antibodies to perform two western blot experiments per primary antibody.
The SET1/COMPASS Antibody Sampler Kit provides an economical means of detecting SET1/COMPASS proteins using control antibodies against SET1A, SET1B, MLL1, MLL2, WDR5, WDR82, and Menin. This kit contains enough primary antibodies to perform at least two western blot experiments.

Background: The Set1 histone methyltransferase protein was first identified in yeast as part of the Set1/COMPASS histone methyltransferase complex, which methylates histone H3 on lysine 4 and functions as a transcriptional co-activator (1). While yeast contain only one known Set1 protein, mammals contain six Set1-related proteins: SET1A, SET1B, MLL1, MLL2, MLL3 and MLL4, all of which methylate histone H3 on lysine 4 (2,3). These Set1-related proteins are each found in distinct protein complexes, all of which share the common core structural subunits WDR5, RBBP5 and ASH2L (2-6). WDR82 is a core subunit specific to SET1A and SET1B complexes, while Menin is a core subunit specific to the MLL complexes (4,5,7).Like yeast Set1, all six Set1-related mammalian proteins methylate histone H3 on lysine 4 (2-6). SET1A, SET1B, MLL1 and MLL2 mediate di- and tri-methylation of histone H3 Lys4 at gene promoters to facilitate transcription activation. MLL3 and MLL4 function primarily to mono-methylate histone H3 Lys4 at gene enhancers. MLL1 and MLL2 function as master regulators of both embryogenesis and hematopoiesis, and are required for proper expression of Hox genes (8-10). MLL1 is a large approximately 4000 amino acid protein that is cleaved by the Taspase 1 threonine endopeptidase to form N-terminal (MLL1-N) and C-terminal MLL1 (MLL1-C) fragments, both of which are subunits of the functional MLL1/COMPASS complex (11,12). MLL1 translocations are found in a large number of hematological malignancies, suggesting that Set1 histone methyltransferase complexes play a critical role in leukemogenesis (6). Like MLL1, MLL2 is also a large, approximately 2700 amino acid protein that is cleaved by the Taspase 1 threonine endopeptidase to form N-terminal (MLL2-N) and C-terminal (MLL2-C) fragments, both of which are subunits of the functional MLL2/COMPASS complex. MLL2 has also been implicated as a modulator of hematological malignancies (13). MLL3 and MLL4 proteins are not cleaved by Taspase 1.

The SHP-2 Antibody Sampler Kit provides an economical means to evaluate levels of SHP-2 protein phosphorylated at the specified sites, as well as total SHP-2 levels. The kit contains enough primary and secondary antibody to perform two western blot experiments per antibody.

Background: SHP-2 (PTPN11) is a ubiquitously expressed, nonreceptor protein tyrosine phosphatase (PTP). It participates in signaling events downstream of receptors for growth factors, cytokines, hormones, antigens, and extracellular matrices in the control of cell growth, differentiation, migration, and death (1). Activation of SHP-2 and its association with Gab1 is critical for sustained Erk activation downstream of several growth factor receptors and cytokines (2). In addition to its role in Gab1-mediated Erk activation, SHP-2 attenuates EGF-dependent PI3 kinase activation by dephosphorylating Gab1 at p85 binding sites (3). SHP-2 becomes phosphorylated at Tyr542 and Tyr580 in its carboxy-terminus in response to growth factor receptor activation (4). These phosphorylation events are thought to relieve basal inhibition and stimulate SHP-2 tyrosine phosphatase activity (5). Mutations in the corresponding gene result in a pair of clinically similar disorders (Noonan syndrome and LEOPARD syndrome) that may result from abnormal MAPK regulation (6).

$262
3 nmol
300 µl
SignalSilence® 4E-BP1 siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit 4E-BP1 expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Human

Background: Translation repressor protein 4E-BP1 (also known as PHAS-1) inhibits cap-dependent translation by binding to the translation initiation factor eIF4E. Hyperphosphorylation of 4E-BP1 disrupts this interaction and results in activation of cap-dependent translation (1). Both the PI3 kinase/Akt pathway and FRAP/mTOR kinase regulate 4E-BP1 activity (2,3). Multiple 4E-BP1 residues are phosphorylated in vivo (4). While phosphorylation by FRAP/mTOR at Thr37 and Thr46 does not prevent the binding of 4E-BP1 to eIF4E, it is thought to prime 4E-BP1 for subsequent phosphorylation at Ser65 and Thr70 (5).

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

Background: Acetyl-CoA carboxylase (ACC) catalyzes the carboxylation of acetyl-CoA to malonyl-CoA (1). It is the key enzyme in the biosynthesis and oxidation of fatty acids (1). In rodents, the 265 kDa ACC1 (ACCα) form is primarily expressed in lipogenic tissues, while 280 kDa ACC2 (ACCβ) is the main isoform in oxidative tissues (1,2). However, in humans, ACC2 is the predominant isoform in both lipogenic and oxidative tissues (1,2). Phosphorylation by AMPK at Ser79 or by PKA at Ser1200 inhibits the enzymatic activity of ACC (3). ACC is a potential target of anti-obesity drugs (4,5).

$262
3 nmol
300 µl
SignalSilence® ADAM9 siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit ADAM9 expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Human

Background: The ADAM (A Disintegrin and A Metalloprotease) family of multidomain membrane proteins influences cell signaling and adhesion by shedding cell surface proteins such as cytokines and growth factors, by influencing cell adhesion to the extracellular matrix (ECM), and by directly remodeling the ECM. Conserved domains in ADAM family members include a prodomain, a zinc-dependent metalloprotease domain, a disintegrin domain, a cysteine-rich domain, an EGF-like sequence, and a short cytoplasmic tail (1,2).The prodomain is thought to aid in protein folding. Disintegrin and cysteine-rich domains mediate adhesion, at least in part, through binding to integrins. Phosphorylation of the cytoplasmic tail as well as its interaction with other signaling proteins may influence intra- and extracellular signaling (1). ADAM9 is widely distributed and has been shown to affect migration in skin keratinocytes (3,4). Research studies have shown that ADAM9 is overexpressed in prostate cancer (5), pancreatic cancer (6), gastric cancer (7), and has been linked to invasion and metastasis in small cell lung cancer (8). Research has also shown that an alternatively spliced short (50 kDa) form of ADAM9 containing protease activity is involved in tumor cell invasion (9).

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

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).

SignalSilence® Akt siRNA II from Cell Signaling Technology allows the researcher to specifically inhibit Akt expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products are rigorously tested in-house and have been shown to reduce protein expression by western analysis.

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).

$262
3 nmol
300 µl
SignalSilence® Akt1 siRNA I (Mouse Specific) from Cell Signaling Technology (CST) allows the researcher to specifically inhibit Akt1 expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Mouse

Background: 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).

$262
50-100 transfections
300 µl
SignalSilence® Akt2 siRNA from Cell Signaling Technology allows the researcher to specifically inhibit Akt2 expression using RNA interference, a method in which gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products are rigorously tested in-house and have been shown to reduce protein expression in specified cell lines.
REACTIVITY
Human

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).

$262
3 nmol
300 µl
SignalSilence® Akt2 siRNA I (Mouse Specific) from Cell Signaling Technology (CST) allows the researcher to specifically inhibit Akt2 expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Mouse

Background: 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).