"Other Essentials"

Supplier: Genetex

SMADs are members of the MAD-related family of molecules. MAD-related proteins are a family of intracellular proteins that are essential components in the signaling pathways of the serine/threonine kinase receptors of the transforming growth factor beta superfamily. SMADs can be divided into receptor-regulated SMADs (R-SMADs: SMAD1, SMAD2, SMAD5, SMAD8 and SMAD9), common-mediator SMAD (co-SMAD: SMAD4), and inhibitory SMADs (I-SMADs: SMAD6 and SMAD7). SMAD1, SMAD5, SMAD8 and SMAD9 have high degrees of homology and antibodies are available that recognize sequences common to all of them. SMAD8 and SMAD9 are typically used as alternate names for one another in the literature.

Supplier: Genetex

The Toll-like receptor (TLR) family in mammal comprises a family of transmembrane proteins characterized by multiple copies of leucine rich repeats in the extracellular domain and IL1 receptor motif in the cytoplasmic domain. Like its counterparts in Drosophila, TLRs signal through adaptor molecules and could constitute an important and unrecognized component of innate immunity in humans. The TRL family is a phylogenetically conserved mediator of innate immunity that is essential for microbial recognition. TLRs characterized so far activate the MyD88/interleukin 1 receptor-associated kinase (IRAK) signaling pathway. Ten human homologs of TLRs (TLR1-10) have been described.

Supplier: Genetex

The protein encoded by this gene is a member of the dual specificity protein kinase family, which acts as a mitogen-activated protein (MAP) kinase kinase. MAP kinases, also known as extracellular signal-regulated kinases (ERKs), act as an integration point for multiple biochemical signals. This protein kinase lies upstream of MAP kinases and stimulates the enzymatic activity of MAP kinases upon wide variety of extra- and intracellular signals. As an essential component of MAP kinase signal transduction pathway, this kinase is involved in many cellular processes such as proliferation, differentiation, transcription regulation and development. [provided by RefSeq]

Supplier: Genetex

Rad50 is a protein involved in DNA double-strand break repair. This protein forms a complex with MRE11 and NBS1. The protein complex binds to DNA and displays numerous enzymatic activities that are required for nonhomologous joining of DNA ends. This protein, cooperating with its partners, is important for DNA double-strand break repair, cell cycle checkpoint activation, telomere maintenance, and meiotic recombination. Knockout studies of the mouse homolog suggest this gene is essential for cell growth and viability. Two alternatively spliced transcript variants of this gene, which encode distinct proteins, have been reported.

Supplier: Wards

Stainless steel spirit lamp, provides a reliable and safe heat source for various laboratory applications.

Supplier: Genetex

Meiotic recombination and chromosome segregation require the formation of double-strand breaks (DSBs) in paired chromosome homologs. During meiosis in yeast, a meiotic recombination protein is covalently-linked to the 5' end of DSBs and is essential for the formation of DSBs. The protein encoded by this gene is similar in sequence and conserved features to the yeast meiotic recombination protein. The encoded protein belongs to the TOP6A protein family. Several transcript variants encoding different isoforms have been found for this gene, but the full-length nature of only two of them have been described. [provided by RefSeq]

Supplier: Genetex

The protein encoded by this gene is a member of the family of inhibitor of apoptosis proteins (IAP) and contains a single copy of a baculovirus IAP repeat (BIR) as well as a RING-type zinc finger domain. The BIR domain is essential for inhibitory activity and interacts with caspases, while the RING finger domain sometimes enhances antiapoptotic activity but does not inhibit apoptosis alone. Two transcript variants encoding different isoforms have been found for this gene. The two isoforms have different antiapoptotic properties, with isoform alpha protecting cells from apoptosis induced by staurosporine and isoform b protecting cells from apoptosis induced by etoposide. [provided by RefSeq]

Supplier: Dickies

Dickies® style WL451.

Supplier: BD

Fluid Selenite-Cystine Broth is used as an enrichment medium for isolation of Salmonella species from foods, dairy products, materials of sanitary importance, and clinical specimens.

Supplier: Thermo Scientific

Pierce™ Recombinant Peroxidase Conjugated (HRP-Horseradish Peroxidase) Protein A can be used to probe and detect rabbit and human antibodies, especially IgG isotypes, in Western blotting, ELISA, IHC and other immunoassay protocols.

Supplier: Analytik Jena US

The EL Series UV Lamps from Analytik Jena provide models with longwave, shortwave, midrange UV and/or white light in four, six or eight watts intensities. Some models feature multiple UV wavelengths in the same lamp.

Supplier: Genetex

This gene encodes the enzyme responsible for the excision of 8-oxoguanine, a mutagenic base byproduct which occurs as a result of exposure to reactive oxygen. The action of this enzyme includes lyase activity for chain cleavage. Alternative splicing of the C-terminal region of this gene classifies splice variants into two major groups, type 1 and type 2, depending on the last exon of the sequence. Type 1 alternative splice variants end with exon 7 and type 2 end with exon 8. All variants share the N-terminal region in common. Many alternative splice variants for this gene have been described, but the full-length nature for every variant has not been determined. The N-terminus of this gene contains a mitochondrial targetting signal, essential for mitochondrial localization.

Supplier: Genetex

The Toll like receptor (TLR) family in mammal comprises a family of transmembrane proteins characterized by multiple copies of leucine rich repeats in the extracellular domain and IL 1 receptor motif in the cytoplasmic domain. Like its counterparts in Drosophila, TLRs signal through adaptor molecules and could constitute an important and unrecognized component of innate immunity in humans. The TRL family is a phylogenetically conserved mediator of innate immunity that is essential for microbial recognition. TLRs characterized so far activate the MyD88/interleukin 1 receptor-associated kinase (IRAK) signaling pathway. Ten human homologs of TLRs (TLR1 10) have been described. Stimulation of the NFkB signaling pathway by TLR7 suggests that it plays a role in immune response.

Supplier: Genetex

Eukaryotic DNA ligases are ATP-dependent enzymes that catalyse the joining of single and double-strand DNA breaks, which is an essential final step in DNA replication, recombination and repair. Four biochemically distinct DNA ligases, termed ligases I-IV, have been identified in mammalian cells. DNA ligase I is functionally homologous to the DNA ligase encoded by the Saccharomyces cerevisiae Cdc9 gene. The joining of Okazaki fragments during lagging strand DNA replication in mammalian cells is due to DNA ligase I. A combination of DNA polymerase epsilon, PCNA, replication factor C, replication protein A, and DNA ligase I is well-suited to the task of creating nucleotide excision repair patches.

Supplier: BD

McClung Toabe Agar is used for detection and isolation of Clostridium perfringens from food samples.

Supplier: Genetex

Component of the THO subcomplex of the TREX complex. The TREX complex specifically associates with spliced mRNA and not with unspliced pre-mRNA. It is recruited to spliced mRNAs by a transcription-independent mechanism. Binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export. The recruitment occurs via an interaction between THOC4 and the cap-binding protein NCBP1. UAP56 functions as a bridge between THOC4 and the THO complex. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. The recruitment of the TREX complex to the intronless viral mRNA occurs via an interaction between KSHV ORF57 protein and THOC4.