Asc (AL177) Antibody + Blocking Peptide Set Reference: AG-44B-2000 The Asc (AL177) Antibody + Blocking Peptide Set contains one vial each of the anti-Asc, pAb (AL177) (Prod. No. AG-25B-0006) and the Asc Antibody (AL177) Blocking Peptide (Prod. No. AG-37B-0001). Both compounds are provided with the appropriate product datasheet including additional product information.
NLRP3 Inflammasome Human Antibodies Starter Set Reference: AG-44B-0008 The NLRP3 Inflammasome Human Antibodies Starter Set is an all-in-one solution to study the NLRP3 inflammasome using Western blotting application. This antibody starter set comprises our KO extract validated STANDARD antibodies against the key components of the NLRP3 inflammasome including NLRP3, Asc and Caspase-1, used and published by the experts in inflammasome research. This economic starter set contains enough primary antibodies to perform at least 3 western blot experiments. Each antibody is available in 100µg catalog sizes for further experiments.
NLRP3 Inflammasome Mouse Antibodies Starter Set Reference: AG-44B-0009 The NLRP3 Inflammasome Mouse Antibodies Starter Set is an all-in-one solution to study the NLRP3 inflammasome using Western blotting application. This antibody starter set comprises our KO extract validated STANDARD antibodies against the key components of the NLRP3 inflammasome including NLRP3, Asc and Caspase-1, used and published by the experts in inflammasome research. This economic starter set contains enough primary antibodies to perform at least 3 western blot experiments. Each antibody is available in 100µg catalog sizes for further experiments.
PANoptosome Human Antibodies Starter Set Reference: AG-44B-0012 The PANoptosome Human Antibodies Starter Set is an all-in-one solution to study the three key modes of programmed cell death, including pyroptosis, apoptosis and necroptosis using Western blotting application. This antibody starter set comprises our KO extract validated STANDARD antibodies against the key components of the NLRP3 inflammasome including NLRP3, Asc and Caspase-1, the cytosolic RNA/DNA sensor ZBP1 and the apoptosis target caspase-8. These antibodies are used and published by the experts in inflammasome and cell death research. This economic starter set contains enough primary antibodies to perform at least 3 western blot experiments. Each antibody is available in 100µg catalog sizes for further experiments.
PANoptosome Mouse Antibodies Starter Set Reference: AG-44B-0013 The PANoptosome Mouse Antibodies Starter Set is an all-in-one solution to study the three key modes of programmed cell death, including pyroptosis, apoptosis and necroptosis using Western blotting application. This antibody starter set comprises our KO extract validated STANDARD antibodies against the key components of the NLRP3 inflammasome including NLRP3, Asc and Caspase-1, the cytosolic RNA/DNA sensor ZBP1 and the apoptosis target caspase-8. These antibodies are used and published by the experts in inflammasome and cell death research. This economic starter set contains enough primary antibodies to perform at least 3 western blot experiments. Each antibody is available in 100µg catalog sizes for further experiments.
Histone H3.3 Mutation Antibody Panel (G34W, G34R, G34V) Reference: REV-31-1325-MP Histone H3 is one of the DNA-binding proteins found in the chromatin of all eukaryotic cells. H3 along with four core histone proteins binds to DNA forming the structure of the nucleosome. Histones play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. Histone H3 has three main variants, H3.1 and H3.2, which are deposited in chromatin only during DNA replication and H3.3, which is replication independent and is found primarily in the regions of active transcription and heterochromatin. Post translationally, histones are modified in a variety of ways to either directly change the chromatin structure or allow for the binding of specific transcription factors. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of post-translational modification that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine. Histone modifications are one form of epigenetic information that relate closely to gene regulation. Aberrant histone methylation caused by alteration in chromatin-modifying enzymes has long been implicated in cancers. Recently, recurrent histone mutations have been identified in multiple cancers and have been shown to impede histone methylation. All identified histone mutations (including H3K4M, H3K9M, H3K27M, H3K36M, and H3G34V/R/W) result in amino acid substitution at/near a lysine residue that is a target of methylation.
Histone H3 Mutation Antibody Panel (K4M, K9M, K27M, K36M) Reference: REV-31-1326-MP Histone H3 is one of the DNA-binding proteins found in the chromatin of all eukaryotic cells. H3 along with four core histone proteins binds to DNA forming the structure of the nucleosome. Histones play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. Histone H3 has three main variants, H3.1 and H3.2, which are deposited in chromatin only during DNA replication and H3.3, which is replication independent and is found primarily in the regions of active transcription and heterochromatin. Post translationally, histones are modified in a variety of ways to either directly change the chromatin structure or allow for the binding of specific transcription factors. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of post-translational modification that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine. Histone modifications are one form of epigenetic information that relate closely to gene regulation. Aberrant histone methylation caused by alteration in chromatin-modifying enzymes has long been implicated in cancers. Recently, recurrent histone mutations have been identified in multiple cancers and have been shown to impede histone methylation. All identified histone mutations (including H3K4M, H3K9M, H3K27M, H3K36M, and H3G34V/R/W) result in amino acid substitution at/near a lysine residue that is a target of methylation.
Histone H3 Mutation Antibody Panel (K4M, K9M, K27M, K36M) + H3.3 Mutation... Reference: REV-31-1327-MP Histone H3 is one of the DNA-binding proteins found in the chromatin of all eukaryotic cells. H3 along with four core histone proteins binds to DNA forming the structure of the nucleosome. Histones play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. Histone H3 has three main variants, H3.1 and H3.2, which are deposited in chromatin only during DNA replication and H3.3, which is replication independent and is found primarily in the regions of active transcription and heterochromatin. Post translationally, histones are modified in a variety of ways to either directly change the chromatin structure or allow for the binding of specific transcription factors. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of post-translational modification that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine. Histone modifications are one form of epigenetic information that relate closely to gene regulation. Aberrant histone methylation caused by alteration in chromatin-modifying enzymes has long been implicated in cancers. Recently, recurrent histone mutations have been identified in multiple cancers and have been shown to impede histone methylation. All identified histone mutations (including H3K4M, H3K9M, H3K27M, H3K36M, and H3G34V/R/W) result in amino acid substitution at/near a lysine residue that is a target of methylation.