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Human Dna-Dependent Protein Kinase Activity

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: HMGA2 belongs to the family of high mobility group with AT-hook DNA binding domain. HMGA proteins are considered architectural transcription factors; they do not have direct transcriptional activation capacity, but instead regulate gene expression by changing DNA conformation through binding to AT-rich regions in the DNA and/or direct interaction with other transcription factors (1,2). HMGA2 is abundantly and ubiquitously expressed and plays a crucial role during embryonic development (3). HMGA2 promotes stem cell self-renewal and research studies have shown that decreased HMGA2 expression is associated with stem cell aging (4-7). Investigators have shown that expression levels of HMGA2 are very low in normal adult tissues, while either overexpression or rearrangement is associated with many types of cancer (8-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: HMGA2 belongs to the family of high mobility group with AT-hook DNA binding domain. HMGA proteins are considered architectural transcription factors; they do not have direct transcriptional activation capacity, but instead regulate gene expression by changing DNA conformation through binding to AT-rich regions in the DNA and/or direct interaction with other transcription factors (1,2). HMGA2 is abundantly and ubiquitously expressed and plays a crucial role during embryonic development (3). HMGA2 promotes stem cell self-renewal and research studies have shown that decreased HMGA2 expression is associated with stem cell aging (4-7). Investigators have shown that expression levels of HMGA2 are very low in normal adult tissues, while either overexpression or rearrangement is associated with many types of cancer (8-11).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: DNA-dependent protein kinase (DNA-PK) is an important factor in the repair of double-stranded breaks in DNA. Cells lacking DNA-PK or in which DNA-PK is inhibited fail to show proper nonhomologous end-joining (NHEJ) (1-7). DNA-PK is composed of two DNA-binding subunits (Ku70 and Ku86) and one 450 kDa catalytic subunit (DNA-PKcs) (8). It is thought that a heterodimer of Ku70 and Ku86 binds to double-stranded DNA broken ends before DNA-PKcs binds and is activated (1,9). Activated DNA-PKcs is a serine/threonine kinase that has been shown to phosphorylate a number of proteins in vitro, including p53, transcription factors, RNA polymerase, and Ku70/Ku86 (10,11). DNA-PKcs autophosphorylation at multiple sites, including Thr2609 and Ser2056, results in an inactivation of DNA-PK kinase activity and NHEJ ability (12,13). It has been demonstrated, however, that DNA-PK preferentially phosphorylates substrates before it autophosphorylates, suggesting that DNA-PK autophosphorylation may play a role in disassembly of the DNA repair machinery (14,15). Autophosphorylation at Thr2609 has also been shown to be required for DNA-PK-mediated double strand break repair, and phosphorylated DNA-PK co-localizes with H2A.X and 53BP1 at sites of DNA damage (16). Phosphorylation at Ser2056 occurs in response to double-stranded DNA breaks and ATM activation (17).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: DNA-dependent protein kinase (DNA-PK) is an important factor in the repair of double-stranded breaks in DNA. Cells lacking DNA-PK or in which DNA-PK is inhibited fail to show proper nonhomologous end-joining (NHEJ) (1-7). DNA-PK is composed of two DNA-binding subunits (Ku70 and Ku86) and one 450 kDa catalytic subunit (DNA-PKcs) (8). It is thought that a heterodimer of Ku70 and Ku86 binds to double-stranded DNA broken ends before DNA-PKcs binds and is activated (1,9). Activated DNA-PKcs is a serine/threonine kinase that has been shown to phosphorylate a number of proteins in vitro, including p53, transcription factors, RNA polymerase, and Ku70/Ku86 (10,11). DNA-PKcs autophosphorylation at multiple sites, including Thr2609 and Ser2056, results in an inactivation of DNA-PK kinase activity and NHEJ ability (12,13). It has been demonstrated, however, that DNA-PK preferentially phosphorylates substrates before it autophosphorylates, suggesting that DNA-PK autophosphorylation may play a role in disassembly of the DNA repair machinery (14,15). Autophosphorylation at Thr2609 has also been shown to be required for DNA-PK-mediated double strand break repair, and phosphorylated DNA-PK co-localizes with H2A.X and 53BP1 at sites of DNA damage (16). Phosphorylation at Ser2056 occurs in response to double-stranded DNA breaks and ATM activation (17).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: DNA-dependent protein kinase (DNA-PK) is an important factor in the repair of double-stranded breaks in DNA. Cells lacking DNA-PK or in which DNA-PK is inhibited fail to show proper nonhomologous end-joining (NHEJ) (1-7). DNA-PK is composed of two DNA-binding subunits (Ku70 and Ku86) and one 450 kDa catalytic subunit (DNA-PKcs) (8). It is thought that a heterodimer of Ku70 and Ku86 binds to double-stranded DNA broken ends before DNA-PKcs binds and is activated (1,9). Activated DNA-PKcs is a serine/threonine kinase that has been shown to phosphorylate a number of proteins in vitro, including p53, transcription factors, RNA polymerase, and Ku70/Ku86 (10,11). DNA-PKcs autophosphorylation at multiple sites, including Thr2609 and Ser2056, results in an inactivation of DNA-PK kinase activity and NHEJ ability (12,13). It has been demonstrated, however, that DNA-PK preferentially phosphorylates substrates before it autophosphorylates, suggesting that DNA-PK autophosphorylation may play a role in disassembly of the DNA repair machinery (14,15). Autophosphorylation at Thr2609 has also been shown to be required for DNA-PK-mediated double strand break repair, and phosphorylated DNA-PK co-localizes with H2A.X and 53BP1 at sites of DNA damage (16). Phosphorylation at Ser2056 occurs in response to double-stranded DNA breaks and ATM activation (17).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: DNA-dependent protein kinase (DNA-PK) is an important factor in the repair of double-stranded breaks in DNA. Cells lacking DNA-PK or in which DNA-PK is inhibited fail to show proper nonhomologous end-joining (NHEJ) (1-7). DNA-PK is composed of two DNA-binding subunits (Ku70 and Ku86) and one 450 kDa catalytic subunit (DNA-PKcs) (8). It is thought that a heterodimer of Ku70 and Ku86 binds to double-stranded DNA broken ends before DNA-PKcs binds and is activated (1,9). Activated DNA-PKcs is a serine/threonine kinase that has been shown to phosphorylate a number of proteins in vitro, including p53, transcription factors, RNA polymerase, and Ku70/Ku86 (10,11). DNA-PKcs autophosphorylation at multiple sites, including Thr2609 and Ser2056, results in an inactivation of DNA-PK kinase activity and NHEJ ability (12,13). It has been demonstrated, however, that DNA-PK preferentially phosphorylates substrates before it autophosphorylates, suggesting that DNA-PK autophosphorylation may play a role in disassembly of the DNA repair machinery (14,15). Autophosphorylation at Thr2609 has also been shown to be required for DNA-PK-mediated double strand break repair, and phosphorylated DNA-PK co-localizes with H2A.X and 53BP1 at sites of DNA damage (16). Phosphorylation at Ser2056 occurs in response to double-stranded DNA breaks and ATM activation (17).

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

Application Methods: Western Blotting

Background: Ataxia telangiectasia mutated kinase (ATM) is a serine/threonine kinase that regulates cell cycle checkpoints and DNA repair (1). Activation of ATM by autophosphorylation on Ser1981 occurs in response to exposed DNA double stranded breaks. ATM kinase regulates a number of proteins involved in cell cycle checkpoint control, apoptosis, and DNA repair. Known substrates include p53, Chk2, Chk1, CtIP, 4E-BP1, BRCA1, RPA3, H2A.X, SMC1, FANCD2, Rad17, Artemis, Nbs1, and the I-2 regulatory subunit of PP1 (1,2). Mutations in the corresponding ATM gene result in ataxia telangiectasia (AT), an autosomal recessive disease characterized by uncoordinated muscle movement and neurodegeneration. Cells from AT patients display defective DNA damage-induced checkpoint activation, sensitivity to radiation, and a higher frequency of chromosome breakage (3,4).

$122
20 µl
$303
100 µl
$717
300 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Ataxia telangiectasia mutated kinase (ATM) is a serine/threonine kinase that regulates cell cycle checkpoints and DNA repair (1). Activation of ATM by autophosphorylation on Ser1981 occurs in response to exposed DNA double stranded breaks. ATM kinase regulates a number of proteins involved in cell cycle checkpoint control, apoptosis, and DNA repair. Known substrates include p53, Chk2, Chk1, CtIP, 4E-BP1, BRCA1, RPA3, H2A.X, SMC1, FANCD2, Rad17, Artemis, Nbs1, and the I-2 regulatory subunit of PP1 (1,2). Mutations in the corresponding ATM gene result in ataxia telangiectasia (AT), an autosomal recessive disease characterized by uncoordinated muscle movement and neurodegeneration. Cells from AT patients display defective DNA damage-induced checkpoint activation, sensitivity to radiation, and a higher frequency of chromosome breakage (3,4).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Ataxia telangiectasia mutated kinase (ATM) is a serine/threonine kinase that regulates cell cycle checkpoints and DNA repair (1). Activation of ATM by autophosphorylation on Ser1981 occurs in response to exposed DNA double stranded breaks. ATM kinase regulates a number of proteins involved in cell cycle checkpoint control, apoptosis, and DNA repair. Known substrates include p53, Chk2, Chk1, CtIP, 4E-BP1, BRCA1, RPA3, H2A.X, SMC1, FANCD2, Rad17, Artemis, Nbs1, and the I-2 regulatory subunit of PP1 (1,2). Mutations in the corresponding ATM gene result in ataxia telangiectasia (AT), an autosomal recessive disease characterized by uncoordinated muscle movement and neurodegeneration. Cells from AT patients display defective DNA damage-induced checkpoint activation, sensitivity to radiation, and a higher frequency of chromosome breakage (3,4).

$262
3 nmol
300 µl
SignalSilence® ATM siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit ATM 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: Ataxia telangiectasia mutated kinase (ATM) is a serine/threonine kinase that regulates cell cycle checkpoints and DNA repair (1). Activation of ATM by autophosphorylation on Ser1981 occurs in response to exposed DNA double stranded breaks. ATM kinase regulates a number of proteins involved in cell cycle checkpoint control, apoptosis, and DNA repair. Known substrates include p53, Chk2, Chk1, CtIP, 4E-BP1, BRCA1, RPA3, H2A.X, SMC1, FANCD2, Rad17, Artemis, Nbs1, and the I-2 regulatory subunit of PP1 (1,2). Mutations in the corresponding ATM gene result in ataxia telangiectasia (AT), an autosomal recessive disease characterized by uncoordinated muscle movement and neurodegeneration. Cells from AT patients display defective DNA damage-induced checkpoint activation, sensitivity to radiation, and a higher frequency of chromosome breakage (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Ataxia telangiectasia mutated kinase (ATM) is a serine/threonine kinase that regulates cell cycle checkpoints and DNA repair (1). Activation of ATM by autophosphorylation on Ser1981 occurs in response to exposed DNA double stranded breaks. ATM kinase regulates a number of proteins involved in cell cycle checkpoint control, apoptosis, and DNA repair. Known substrates include p53, Chk2, Chk1, CtIP, 4E-BP1, BRCA1, RPA3, H2A.X, SMC1, FANCD2, Rad17, Artemis, Nbs1, and the I-2 regulatory subunit of PP1 (1,2). Mutations in the corresponding ATM gene result in ataxia telangiectasia (AT), an autosomal recessive disease characterized by uncoordinated muscle movement and neurodegeneration. Cells from AT patients display defective DNA damage-induced checkpoint activation, sensitivity to radiation, and a higher frequency of chromosome breakage (3,4).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Western Blotting

Background: Ataxia telangiectasia mutated kinase (ATM) is a serine/threonine kinase that regulates cell cycle checkpoints and DNA repair (1). Activation of ATM by autophosphorylation on Ser1981 occurs in response to exposed DNA double stranded breaks. ATM kinase regulates a number of proteins involved in cell cycle checkpoint control, apoptosis, and DNA repair. Known substrates include p53, Chk2, Chk1, CtIP, 4E-BP1, BRCA1, RPA3, H2A.X, SMC1, FANCD2, Rad17, Artemis, Nbs1, and the I-2 regulatory subunit of PP1 (1,2). Mutations in the corresponding ATM gene result in ataxia telangiectasia (AT), an autosomal recessive disease characterized by uncoordinated muscle movement and neurodegeneration. Cells from AT patients display defective DNA damage-induced checkpoint activation, sensitivity to radiation, and a higher frequency of chromosome breakage (3,4).

$305
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. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated CDK9 (C12F7) Rabbit mAb #2316.
APPLICATIONS
REACTIVITY
Bovine, Dog, Hamster, Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: P-TEFb is a general transcription factor that regulates transcription elongation through phosphorylation of the C-terminal tail domain (CTD) of RNA polymerase II (RNAP II). The P-TEFb complex is composed of a catalytic subunit, CDK9, and its regulatory cyclin partner, which can be cyclin T1, T2a, T2b or K (reviewed in 1,2). P-TEFb is recruited by the HIV Tat protein to allow transcriptional elongation, and subsequent replication of the viral genome. Inhibition of P-TEFb function therefore has potential for HIV therapy. CDK9 exists as two isoforms, an abundant 42 kDa isoform, and a less abundant 55 kDa isoform, which contains an amino-terminal extension (3). The two forms likely have distinct purposes based on differential expression during lymphocyte activation (4,5) and on their localization within the nucleus (5).Cyclin dependent kinases (CDKs) are activated in part by cyclin binding and by phosphorylation of a conserved threonine in the T-loop domain. Phosphorylation of CDK9 at the T-loop Thr186 by an unidentified nuclear kinase may be important in P-TEFb activation (6) and regulation of HIV transcription (7). Acetylation of CDK9 at Lys44 affects its ability to phosphorylate the RNAPII CTD (8).

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

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

Background: P-TEFb is a general transcription factor that regulates transcription elongation through phosphorylation of the C-terminal tail domain (CTD) of RNA polymerase II (RNAP II). The P-TEFb complex is composed of a catalytic subunit, CDK9, and its regulatory cyclin partner, which can be cyclin T1, T2a, T2b or K (reviewed in 1,2). P-TEFb is recruited by the HIV Tat protein to allow transcriptional elongation, and subsequent replication of the viral genome. Inhibition of P-TEFb function therefore has potential for HIV therapy. CDK9 exists as two isoforms, an abundant 42 kDa isoform, and a less abundant 55 kDa isoform, which contains an amino-terminal extension (3). The two forms likely have distinct purposes based on differential expression during lymphocyte activation (4,5) and on their localization within the nucleus (5).Cyclin dependent kinases (CDKs) are activated in part by cyclin binding and by phosphorylation of a conserved threonine in the T-loop domain. Phosphorylation of CDK9 at the T-loop Thr186 by an unidentified nuclear kinase may be important in P-TEFb activation (6) and regulation of HIV transcription (7). Acetylation of CDK9 at Lys44 affects its ability to phosphorylate the RNAPII CTD (8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: P-TEFb is a general transcription factor that regulates transcription elongation through phosphorylation of the C-terminal tail domain (CTD) of RNA polymerase II (RNAP II). The P-TEFb complex is composed of a catalytic subunit, CDK9, and its regulatory cyclin partner, which can be cyclin T1, T2a, T2b or K (reviewed in 1,2). P-TEFb is recruited by the HIV Tat protein to allow transcriptional elongation, and subsequent replication of the viral genome. Inhibition of P-TEFb function therefore has potential for HIV therapy. CDK9 exists as two isoforms, an abundant 42 kDa isoform, and a less abundant 55 kDa isoform, which contains an amino-terminal extension (3). The two forms likely have distinct purposes based on differential expression during lymphocyte activation (4,5) and on their localization within the nucleus (5).Cyclin dependent kinases (CDKs) are activated in part by cyclin binding and by phosphorylation of a conserved threonine in the T-loop domain. Phosphorylation of CDK9 at the T-loop Thr186 by an unidentified nuclear kinase may be important in P-TEFb activation (6) and regulation of HIV transcription (7). Acetylation of CDK9 at Lys44 affects its ability to phosphorylate the RNAPII CTD (8).

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

Application Methods: Western Blotting

Background: CDK-activating kinase (CAK) is a complex of CDK7 and cyclin H. The complex is involved in cell cycle regulation by phosphorylating an activating residue in the T-loop domain of cdks (1). Regulation of CAK activity is mediated by T-loop phosphorylation and by association with MAT1, both of which enhance its kinase activity toward the CTD of RNA polymerase II (2,3) and other substrates such as p53 (4). CAK is an essential component of the transcription complex TFIIH and may interact directly with TFIIH helicases (5).

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

Application Methods: Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: CDK-activating kinase (CAK) is a complex of CDK7 and cyclin H. The complex is involved in cell cycle regulation by phosphorylating an activating residue in the T-loop domain of cdks (1). Regulation of CAK activity is mediated by T-loop phosphorylation and by association with MAT1, both of which enhance its kinase activity toward the CTD of RNA polymerase II (2,3) and other substrates such as p53 (4). CAK is an essential component of the transcription complex TFIIH and may interact directly with TFIIH helicases (5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Cyclin H belongs to a conserved cyclin family that plays a critical role in the regulation of cell cycle dependent kinases (CDKs) necessary for cell cycle progression (1,2). In general, the activity of CDKs requires the binding of appropriate cyclins as well as phosphorylation driven by Cdk-activating kinase (CAK). Cyclin H is part of the CAK complex that includes the kinase CDK7, and an assembly factor p36/Mat1, which enhances binding between cyclin H and CDK7 and increases activity (3,4). CAK regulates progression through the cell cycle by activating cdc2, CDK2, and CDK4 kinases through phosphorylation of a critical threonine residue in the T-loop of the CDK-cyclin complexes (5,6). The CAK complex can exist either in its free form or in association with transcription factor IIH (TFIIH) which can affect its substrate specificity (7,8,9). When bound to TFIIH, CAK preferentially phosphorylates the carboxy-terminal domain of RNA polymerase II (9), providing a link between cell cycle control, transcriptional regulation, and DNA repair.

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

Application Methods: Immunoprecipitation, Western Blotting

Background: XPB and XPD are ATPase/helicase subunits of the TFIIH complex that are involved in nucleotide excision repair (NER) to remove lesions and photoproducts generated by UV light (1). XPB and XPD are 3’-5’ and 5’-3’ DNA helicases, respectively, that play a role in opening of the DNA damage site to facilitate repair (2,3). XPB and XPD both play an important role in maintaining genomic stability, and researchers have linked mutations of these proteins to Xeroderma Pigmentosum (XP) and Trichothiodystrophy (TTD). XP patients have abnormalities in skin pigmentation and are highly susceptible to skin cancers, while TTD patients exhibit symptoms such as brittle hair, neurological abnormalities, and mild photosensitivity (4). In addition to their role in NER, XPB and XPD are involved in transcription initiation as part of the TFIIH core complex (5). The helicase activity of XPB unwinds DNA around the transcription start site to facilitate RNA polymerase II promoter clearance and initiation of transcription (6). XPD plays a structural role linking core TFIIH components with the cdk-activating kinase (CAK) complex that phosphorylates the C-terminus of the largest subunit of RNA polymerase II, leading to transcription initiation (7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: XPB and XPD are ATPase/helicase subunits of the TFIIH complex that are involved in nucleotide excision repair (NER) to remove lesions and photoproducts generated by UV light (1). XPB and XPD are 3’-5’ and 5’-3’ DNA helicases, respectively, that play a role in opening of the DNA damage site to facilitate repair (2,3). XPB and XPD both play an important role in maintaining genomic stability, and researchers have linked mutations of these proteins to Xeroderma Pigmentosum (XP) and Trichothiodystrophy (TTD). XP patients have abnormalities in skin pigmentation and are highly susceptible to skin cancers, while TTD patients exhibit symptoms such as brittle hair, neurological abnormalities, and mild photosensitivity (4). In addition to their role in NER, XPB and XPD are involved in transcription initiation as part of the TFIIH core complex (5). The helicase activity of XPB unwinds DNA around the transcription start site to facilitate RNA polymerase II promoter clearance and initiation of transcription (6). XPD plays a structural role linking core TFIIH components with the cdk-activating kinase (CAK) complex that phosphorylates the C-terminus of the largest subunit of RNA polymerase II, leading to transcription initiation (7).