"Other Essentials"

Supplier: ProSci Inc.

PARC Antibody: The continued localization of p53 to the nucleus is essential for its function as a tumor suppressor. PARC, a large, Parkin-like ubiquitin ligase has recently been identified as a cytoplasmic anchor protein in p53-associated protein complexes. In the absence of stress, PARC inactivation results in nuclear localization of p53 and activation of p53-dependent apoptosis, while overexpression of this protein promoted cytoplasmic sequestration of p53. Surprisingly, PARC knockout mice were viable and exhibited no obvious phenotype, suggesting that other proteins, such as the highly related cullin family of E3 ubiquitin ligases, may perform similar functions in the absence of PARC. Additionally, it has been suggested that p53 binding to PARC may serve to control PARC function.

Supplier: Bioss

This gene encodes a polypeptide hormone precursor that undergoes extensive, tissue-specific, post-translational processing via cleavage by subtilisin-like enzymes known as prohormone convertases. There are eight potential cleavage sites within the polypeptide precursor and, depending on tissue type and the available convertases, processing may yield as many as ten biologically active peptides involved in diverse cellular functions. 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. [provided by RefSeq].

Supplier: Bioss

The Golgi apparatus is a highly complex organelle comprised of a stack of cisternal membranes on the secretory pathway from the ER to the cell surface. The structure is maintained by an exoskeleton or Golgi matrix constructed from a family of coiled-coil protein, the golgins and other peripheral membrane components such as GRASP55 and GRASP65 (1). GRASP55 (Golgi reassembly stacking protien or p59) is a component of the Golgi stacking machinery. GRASP55 is highly homologous to GRASP65 and contains two PDZ domains. GRASP55 is myristoylated and palmitoylated. Unlike GRASP65, GRASP55 does not have detectable binding with the vesicle docking protein GM130 and is located on the medial-Golgi rather than cis-Golgi. Both GRASP55 and GRASP65 function in the stacking of Golgi Cisternae (2,3). The novel coiled-coil protein golgin 45 interacts with GRASP55 and the GTP form of Rab 2, suggesting that GRASP55 and golgin 45 form a Rab 2 effector complex on medial-Golgi essential for normal protein transport and Golgi structure (4). ERK2 directly phosphorylates GRASP55, which is phosphorylated in mitotic cells, suggesting that mitogen-activated protein kinase kinase (MKK)/ERK pathway phosphorylates the Golgi during mitosis (5).

Supplier: ProSci Inc.

The general transcription factor TFIIE has an essential role in eukaryotic transcription initiation together with RNA polymerase II and other general factors. Human TFIIE consists of two subunits of relative molecular mass 57,000 (TFIIE-alpha) and 34,000 (TFIIE-beta) and joins the preinitiation complex after RNA polymerase II and TFIIF. TFIIE-alpha is necessary for transcription initiation together with TFIIE-beta, and recombinant TFIIE-alpha can fully replace the natural subunit in an in vitro transcription assay. Its sequence contains several interesting structural motifs (leucine repeat, zinc finger and helix-turn-helix) and sequence similarities to bacterial sigma factors that suggest direct involvement in the regulation of transcription initiation

Supplier: Bioss

The Golgi apparatus is a highly complex organelle comprised of a stack of cisternal membranes on the secretory pathway from the ER to the cell surface. The structure is maintained by an exoskeleton or Golgi matrix constructed from a family of coiled-coil protein, the golgins and other peripheral membrane components such as GRASP55 and GRASP65 (1). GRASP55 (Golgi reassembly stacking protien or p59) is a component of the Golgi stacking machinery. GRASP55 is highly homologous to GRASP65 and contains two PDZ domains. GRASP55 is myristoylated and palmitoylated. Unlike GRASP65, GRASP55 does not have detectable binding with the vesicle docking protein GM130 and is located on the medial-Golgi rather than cis-Golgi. Both GRASP55 and GRASP65 function in the stacking of Golgi Cisternae (2,3). The novel coiled-coil protein golgin 45 interacts with GRASP55 and the GTP form of Rab 2, suggesting that GRASP55 and golgin 45 form a Rab 2 effector complex on medial-Golgi essential for normal protein transport and Golgi structure (4). ERK2 directly phosphorylates GRASP55, which is phosphorylated in mitotic cells, suggesting that mitogen-activated protein kinase kinase (MKK)/ERK pathway phosphorylates the Golgi during mitosis (5).

Supplier: Bioss

The Golgi apparatus is a highly complex organelle comprised of a stack of cisternal membranes on the secretory pathway from the ER to the cell surface. The structure is maintained by an exoskeleton or Golgi matrix constructed from a family of coiled-coil protein, the golgins and other peripheral membrane components such as GRASP55 and GRASP65 (1). GRASP55 (Golgi reassembly stacking protien or p59) is a component of the Golgi stacking machinery. GRASP55 is highly homologous to GRASP65 and contains two PDZ domains. GRASP55 is myristoylated and palmitoylated. Unlike GRASP65, GRASP55 does not have detectable binding with the vesicle docking protein GM130 and is located on the medial-Golgi rather than cis-Golgi. Both GRASP55 and GRASP65 function in the stacking of Golgi Cisternae (2,3). The novel coiled-coil protein golgin 45 interacts with GRASP55 and the GTP form of Rab 2, suggesting that GRASP55 and golgin 45 form a Rab 2 effector complex on medial-Golgi essential for normal protein transport and Golgi structure (4). ERK2 directly phosphorylates GRASP55, which is phosphorylated in mitotic cells, suggesting that mitogen-activated protein kinase kinase (MKK)/ERK pathway phosphorylates the Golgi during mitosis (5).

Supplier: IMMUNOLOGIC

Anti-CEA is employed essentially as a tool to assist in the distinction between adenocarcinoma and epithelioid malignant mesotheliomas,¹ along with other markers such as those against calretinin, CK 5&6, CD15, HBME-1, MOC-31, and Ber-EP4.¹ Another suggested use of anti-CEA is to immunophenotype various metastatic adenocarcinomas as a means of identifying their origin within a panel of different markers.¹ Its positivity is seen in adenocarcinomas from the lung, colon, stomach, esophagus, pancreas, gallbadder, urachus, salivary gland, ovary, and endocervix.^2,3 Polyclonal anti-CEA is useful in staining hepatocellular carcinoma in a canalicular pattern.^2,4

Supplier: ProSci Inc.

FOXA1 Antibody: FOXA1 is one of three members of the FOXA family, a subset of the forkhead family of transcription factors which play vital roles in development. It has also been implicated in the development of a number of other organs including the androgen and estrogen regulated tissues of the breast and prostate. FOXA1 modulates the transcriptional activity of nuclear hormone receptors and regulates apoptosis by inhibiting the expression of BCL-2. It is an essential protein for the transcriptional activity of both androgen receptor (AR) and estrogen receptor-beta (ER). FOXA1 plays a pivotal role from early stage cancer through to drug resistant and metastatic disease. FOXA1 is not only an attractive therapeutic target but could potentially function as a novel biomarker.

Supplier: Bioss

This gene encodes a polypeptide hormone precursor that undergoes extensive, tissue-specific, post-translational processing via cleavage by subtilisin-like enzymes known as prohormone convertases. There are eight potential cleavage sites within the polypeptide precursor and, depending on tissue type and the available convertases, processing may yield as many as ten biologically active peptides involved in diverse cellular functions. 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. [provided by RefSeq, Jul 2008].

Supplier: Bioss

The Golgi apparatus is a highly complex organelle comprised of a stack of cisternal membranes on the secretory pathway from the ER to the cell surface. The structure is maintained by an exoskeleton or Golgi matrix constructed from a family of coiled-coil protein, the golgins and other peripheral membrane components such as GRASP55 and GRASP65 (1). GRASP55 (Golgi reassembly stacking protien or p59) is a component of the Golgi stacking machinery. GRASP55 is highly homologous to GRASP65 and contains two PDZ domains. GRASP55 is myristoylated and palmitoylated. Unlike GRASP65, GRASP55 does not have detectable binding with the vesicle docking protein GM130 and is located on the medial-Golgi rather than cis-Golgi. Both GRASP55 and GRASP65 function in the stacking of Golgi Cisternae (2,3). The novel coiled-coil protein golgin 45 interacts with GRASP55 and the GTP form of Rab 2, suggesting that GRASP55 and golgin 45 form a Rab 2 effector complex on medial-Golgi essential for normal protein transport and Golgi structure (4). ERK2 directly phosphorylates GRASP55, which is phosphorylated in mitotic cells, suggesting that mitogen-activated protein kinase kinase (MKK)/ERK pathway phosphorylates the Golgi during mitosis (5).

Supplier: Bioss

The Golgi apparatus is a highly complex organelle comprised of a stack of cisternal membranes on the secretory pathway from the ER to the cell surface. The structure is maintained by an exoskeleton or Golgi matrix constructed from a family of coiled-coil protein, the golgins and other peripheral membrane components such as GRASP55 and GRASP65 (1). GRASP55 (Golgi reassembly stacking protien or p59) is a component of the Golgi stacking machinery. GRASP55 is highly homologous to GRASP65 and contains two PDZ domains. GRASP55 is myristoylated and palmitoylated. Unlike GRASP65, GRASP55 does not have detectable binding with the vesicle docking protein GM130 and is located on the medial-Golgi rather than cis-Golgi. Both GRASP55 and GRASP65 function in the stacking of Golgi Cisternae (2,3). The novel coiled-coil protein golgin 45 interacts with GRASP55 and the GTP form of Rab 2, suggesting that GRASP55 and golgin 45 form a Rab 2 effector complex on medial-Golgi essential for normal protein transport and Golgi structure (4). ERK2 directly phosphorylates GRASP55, which is phosphorylated in mitotic cells, suggesting that mitogen-activated protein kinase kinase (MKK)/ERK pathway phosphorylates the Golgi during mitosis (5).

Supplier: ProSci Inc.

Grik3 Antibody: Glutamate receptors are the predominant excitatory neurotransmitter receptors in the mammalian brain and are activated in a variety of normal neurophysiologic processes. Grik3, also known as glutamate receptor 7, belongs to the kainate family of glutamate receptors, which are composed of four subunits and function as ligand-activated ion channels. Grik3 is highly homologous to the related ionotrophic glutamate receptors Grik2 and Grik1. Grik3 has recently been shown to be an essential subunit of presynaptic kainate autoreceptors at hippocampal mossy fiber synapses as grik3-null mice show significantly reduced short- and long-term synaptic potentiation. Other reports have suggested that different polymorphisms in the Grik3 protein may be associated with neurological defects such as recurrent major depressive disorder and schizophrenia. This Grik3 antibody does not cross-react with Grik2.

Supplier: Bioss

Melamine is combined with formaldehyde to produce melamine resin, a very durable thermosetting plastic used in Formica, and melamine foam, a polymeric cleaning product. The end products include countertops, dry erase boards, fabrics, glues, housewares and flame retardants. Melamine is one of the major components in Pigment Yellow 150, a colorant in inks and plastics.Melamine also enters the fabrication of melamine poly-sulfonate used as superplasticiser for making high-resistance concrete. Sulfonated melamine formaldehyde (SMF) is a polymer used as cement admixture to reduce the water content in concrete while increasing the fluidity and the workability of the mix during its handling and pouring. It results in concrete with a lower porosity and a higher mechanical strength exhibiting an improved resistance to aggressive environments and a longer life-time. The use of melamine as fertiliser for crops had been envisaged during the '50s and '60s because of its high nitrogen content (2/3).[7] However melamine is much more expensive to produce than other common nitrogen fertilisers, such as urea. To be effective as a fertiliser, it is essential that the plant nutrients are released or made available in a manner that matches the needs of the growing crop. The nitrogen mineralisation process for melamine is extremely slow, making this product both economically and scientifically impractical for use as a fertiliser.

Supplier: ProSci Inc.

ZIP12 Antibody: The zinc transporter ZIP12, also known as SLC39A12, is a member of a family of divalent ion transporters. Zinc is an essential ion for cells and plays significant roles in the growth, development, and differentiation. The zinc transporter family is divided into four subfamilies (I, II, LIV-1 and gufA). ZIP12 is a multipass membrane protein that belongs to the ZIP transporter subfamily LIV-1. Increased levels of ZIP12 have been observed during acute inflammation in the airway and asthma, suggesting that it may be promote increased zinc uptake, as this can reduce inflammation. The zinc content in brains in individuals with schizophrenia is lower than in individuals with other cerebral diseases, and mutations in ZIP12 have been observed in a small group of schizophrenic patients, suggesting that ZIP12 may play a role in this disease.

Supplier: ProSci Inc.

POLR2H is one of the essential subunits of RNA polymerase II that is shared by the other two eukaryotic DNA-directed RNA polymerases, I and III.This gene encodes one of the essential subunits of RNA polymerase II that is shared by the other two eukaryotic DNA-directed RNA polymerases, I and III. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications. This gene encodes a member of the E2F transcription factor protein family. E2F family members play a crucial role in control of the cell cycle and of the action of tumor suppressor proteins. They are also a target of the transforming proteins of small DNA tumor viruses. Many E2F proteins contain several evolutionarily conserved domains: a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. The encoded protein of this gene is atypical because it lacks the transactivation and tumor suppressor protein association domains. It contains a modular suppression domain and is an inhibitor of E2F-dependent transcription. The protein is part of a multimeric protein complex that contains a histone methyltransferase and the transcription factors Mga and Max. Multiple transcript variants have been reported for this gene, but it has not been clearly demonstrated that they encode valid isoforms. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications. PRIMARYREFSEQ_SPAN PRIMARY_IDENTIFIER PRIMARY_SPAN COMP 1-400 AU142999.1 1-400 401-907 BI772069.1 287-793 908-1792 BC008348.1 928-1812 1793-3185 AC099344.4 111461-112853 c

Supplier: Bioss

Ran (ras-related nuclear protein) is a small GTP binding protein belonging to the RAS superfamily that is essential for the translocation of RNA and proteins through the nuclear pore complex. The Ran protein is also involved in control of DNA synthesis and cell cycle progression. Nuclear localization of Ran requires the presence of regulator of chromosome condensation 1 (RCC1). Mutations in Ran disrupt DNA synthesis. Because of its many functions, it is likely that Ran interacts with several other proteins. Ran regulates formation and organization of the microtubule network independently of its role in the nucleus-cytosol exchange of macromolecules. Ran could be a key signaling molecule regulating microtubule polymerization during mitosis. RCC1 generates a high local concentration of Ran-GTP around chromatin which, in turn, induces the local nucleation of microtubules. Ran is an androgen receptor (AR) coactivator that binds differentially with different lengths of polyglutamine within the androgen receptor. Polyglutamine repeat expansion in the AR is linked to Kennedy's disease (X-linked spinal and bulbar muscular atrophy). Ran coactivation of the AR diminishes with polyglutamine expansion within the AR, and this weak coactivation may lead to partial androgen insensitivity during the development of Kennedy's disease.