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.
Rabbit anti-SARS-CoV-2 Nucleocapsid Protein mAb (CAP) Reference: RM17574 Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. Coronavirus N protein is required for coronavirus RNA synthesis, and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is a most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
Anti-SARS-CoV-2 Spike S1 Control Antibody,Chimeric MAb Reference: RM17582 The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. The spike is essential for both host specificity and viral infectivity. The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. It''s been reported that SARS-CoV-2 (COVID-19 coronavirus, 2019-nCoV) can infect the human respiratory epithelial cells through interaction with the human ACE2 receptor. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.