"Other Essentials"

Supplier: Bioss

RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Requires for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs. Required for 5,8S rRNA 3'-end processing. Also binds to 5,8S ribosomal RNA. Binds with high affinity to the stem-loop structure of replication-dependent histone pre-mRNAs.

Supplier: Bioss

RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Requires for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs. Required for 5,8S rRNA 3'-end processing. Also binds to 5,8S ribosomal RNA. Binds with high affinity to the stem-loop structure of replication-dependent histone pre-mRNAs.

Supplier: ProSci Inc.

Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 comprise a family of nuclear proteins related by the presence in each of a methyl-CpG binding domain (MBD). Each of these proteins, with the exception of MBD3, is capable of binding specifically to methylated DNA. MECP2, MBD1 and MBD2 can also repress transcription from methylated gene promoters. In contrast to other MBD family members, MECP2 is X-linked and subject to X inactivation. MECP2 is dispensible in stem cells, but is essential for embryonic development. MECP2 gene mutations are the cause of some cases of Rett syndrome, a progressive neurologic developmental disorder and one of the most common causes of mental retardation in females.DNA methylation is the major modification of eukaryotic genomes and plays an essential role in mammalian development. Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 comprise a family of nuclear proteins related by the presence in each of a methyl-CpG binding domain (MBD). Each of these proteins, with the exception of MBD3, is capable of binding specifically to methylated DNA. MECP2, MBD1 and MBD2 can also repress transcription from methylated gene promoters. In contrast to other MBD family members, MECP2 is X-linked and subject to X inactivation. MECP2 is dispensible in stem cells, but is essential for embryonic development. MECP2 gene mutations are the cause of some cases of Rett syndrome, a progressive neurologic developmental disorder and one of the most common causes of mental retardation in females.

Supplier: ProSci Inc.

CDC23 shares strong similarity with Saccharomyces cerevisiae Cdc23, a protein essential for cell cycle progression through the G2/M transition. This protein is a component of anaphase-promoting complex (APC), which is composed of eight protein subunits and highly conserved in eukaryotic cells. APC catalyzes the formation of cyclin B-ubiquitin conjugate that is responsible for the ubiquitin-mediated proteolysis of B-type cyclins. This protein and 3 other members of the APC complex contain the TPR (tetratricopeptide repeat), a protein domain important for protein-protein interaction.The protein encoded by this gene shares strong similarity with Saccharomyces cerevisiae Cdc23, a protein essential for cell cycle progression through the G2/M transition. This protein is a component of anaphase-promoting complex (APC), which is composed of eight protein subunits and highly conserved in eucaryotic cells. APC catalyzes the formation of cyclin B-ubiquitin conjugate that is responsible for the ubiquitin-mediated proteolysis of B-type cyclins. This protein and 3 other members of the APC complex contain the TPR (tetratricopeptide repeat), a protein domain important for protein-protein interaction.

Supplier: Bioss

The protease enzyme Lethal Factor (LF) is one of the three proteins (LF, EF & PA) composing the anthrax toxin produced by Bacillus anthracis, a bacteria which can infect many mammalian species and that may be fatal. LF is not toxic by itself, but when associated with Protective Antigen (PA), can then gain entry to cells. Once inside the cell, LF then cleaves the N terminal of most dual specificity mitogen activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5). Cleavage invariably occurs within the N terminal proline rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein protein interactions necessary for the assembly of signaling complexes. There may be other cytosolic targets of LF involved in cytotoxicity. The proteasome may mediate a toxic process initiated by LF in the cell cytosol involving degradation of unidentified molecules that are essential for macrophage homeostasis. This is an early step in LF intoxication, but it is downstream of the cleavage by LF of MEK1 or other putative substrates.

Supplier: ProSci Inc.

MCM8 is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein complex formed by the MCM proteins is a key component of the pre-replication complex (pre_RC) and may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. This protein contains the central domain that is conserved among the MCM proteins. This protein has been shown to co-immunoprecipitate with MCM4, 6 and 7, which suggests that it may interact with other MCM proteins and play a role in DNA replication. Alternatively spliced transcript variants encoding distinct isoforms have been described.

Supplier: Bioss

RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Requires for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs. Required for 5,8S rRNA 3'-end processing. Also binds to 5,8S ribosomal RNA. Binds with high affinity to the stem-loop structure of replication-dependent histone pre-mRNAs.

Supplier: Bioss

Mapping to chromosome 21, the FASP1 gene (FAPP1-associated protein 1) encodes a 233 amino acid protein that is homologous to the fission yeast protein Mis18. In yeast, Mis18 is localized to the centrosome and forms a complex with Mis16 to maintain the deacetylated state of histones specifically in the central core of centromeres. FASP1, also known as Protein Mis18-alpha and C21orf45, is required for the recruitment of CENP-A to centrosomes and is thereby essential for normal chromosome segregation during mitosis. With expression in testis, FASP1 exists as a homodimer, a heterodimer with MIS18B or is present in a complex containing other Mis18 family members. FASP1 has been shown to bind to pp5644 in Hela cells, where overexpression of pp5644 leads to inhibited growth and colony formation.

Supplier: G-Biosciences

The final goal in molecular biology is often the expression of a recombinant protein. The transformed plasmids can be used as templates by the bacteria to produce protein. Students learn about essential promoters and other elements necessary for successful protein expression in bacteria, including the differences between inducible and constitutive (unregulated) expression.The Expression of a Recombinant Protein kit allows students to express a protein either constitutively or under the control of an inducible promoter, which is activated with IPTG (isopropyl-beta-D-thiogalactopyranoside).

Supplier: Bioss

Mapping to chromosome 21, the FASP1 gene (FAPP1-associated protein 1) encodes a 233 amino acid protein that is homologous to the fission yeast protein Mis18. In yeast, Mis18 is localized to the centrosome and forms a complex with Mis16 to maintain the deacetylated state of histones specifically in the central core of centromeres. FASP1, also known as Protein Mis18-alpha and C21orf45, is required for the recruitment of CENP-A to centrosomes and is thereby essential for normal chromosome segregation during mitosis. With expression in testis, FASP1 exists as a homodimer, a heterodimer with MIS18B or is present in a complex containing other Mis18 family members. FASP1 has been shown to bind to pp5644 in Hela cells, where overexpression of pp5644 leads to inhibited growth and colony formation.

Supplier: Bioss

The encoded protein is synthesized mainly in corticotroph cells of the anterior pituitary where four cleavage sites are used; adrenocorticotrophin, essential for normal steroidogenesis and the maintenance of normal adrenal weight, and lipotropin beta are the major end products. In other tissues, including the hypothalamus, placenta, and epithelium, all cleavage sites may be used, giving rise to peptides with roles in pain and energy homeostasis, melanocyte stimulation, and immune modulation. These include several distinct melanotropins, lipotropins, and endorphins that are contained within the adrenocorticotrophin and beta-lipotropin peptides. Mutations in this gene have been associated with early onset obesity, adrenal insufficiency, and red hair pigmentation. Alternatively spliced transcript variants encoding the same protein have been described.

Supplier: ProSci Inc.

LHX8 is a member of the LIM homeobox family. Members of this family share common structural features. They all contain 2 tandemly repeated cysteine-rich double-zinc finger motifs, called LIM domains, in addition to a homeodomain. The homeodomain is a DNA-binding domain, and the LIM domains are essential for regulating the activity of these molecules by interacting with other proteins. Members of the family are required for the patterning or the specification and differentiation of different cell types during embryonic development.

Supplier: ProSci Inc.

CRB2 Antibody: CRB2 (Crumbs homolog 2), like its homologs CRB1 and CRB3, is similar to the Drosophila crumbs protein and is expressed in retina, brain and kidney. Along with other proteins, the Crumbs proteins form a complex that help set up cell polarity in developing neuroepithelial cells. At the onset of neural specification, embryonic stem cells (ESCs) upregulate CRB2, which then localizes apically in neural rosettes. Gain- and loss-of-function studies of CRB2 have shown that CRB2 is essential for the stabilization of other polarity proteins. Unlike CRB1, mutations in CRB2 do not appear to play a role in retinitis pigmentosa or in Leber congenital amaurosis.

Supplier: ProSci Inc.

This gene encodes a predicted transmembrane protein containing two extracellular CUB domains followed by a low-density lipoprotein class A (LDLa) domain. It also has an intracellular FXNPXY-like motif, which has been shown in other proteins to be essential for the internalization of clathrin coated pits during endocytosis. Alternatively spliced transcript variants have been observed, but they have not been fully characterized. [provided by RefSeq].

Supplier: ProSci Inc.

The protein encoded by the MCM6 gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein complex formed by the MCM proteins is a key component of the pre-replication complex (pre_RC) and may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. The MCM complex consisting of this protein and MCM2, 4 and 7 proteins possesses DNA helicase activity, and may act as a DNA unwinding enzyme. The phosphorylation of the complex by CDC2 kinase reduces the helicase activity, suggesting a role in the regulation of DNA replication.The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein complex formed by the MCM proteins is a key component of the pre-replication complex (pre_RC) and may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. The MCM complex consisting of this protein and MCM2, 4 and 7 proteins possesses DNA helicase activity, and may act as a DNA unwinding enzyme. The phosphorylation of the complex by CDC2 kinase reduces the helicase activity, suggesting a role in the regulation of DNA replication.

Supplier: Bioss

The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein complex formed by the MCM proteins is a key component of the pre-replication complex (pre_RC) and may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. The MCM complex consisting of this protein and MCM2, 4 and 6 proteins possesses DNA helicase activity, and may act as a DNA unwinding enzyme. Cyclin D1-dependent kinase, CDK4, is found to associate with this protein, and may regulate the binding of this protein with the tumorsuppressor protein RB1/RB. Alternatively spliced transcript variants encoding distinct isoforms have been reported. [provided by RefSeq, Jul 2008].