966 Results for: "Other Essentials"

Supplier: Bioss

Non-receptor tyrosine-protein kinase that plays an essential role in the selection and maturation of developing T-cells in the thymus and in the function of mature T-cells. Plays a key role in T-cell antigen receptor (TCR)-linked signal transduction pathways. Constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, thereby recruiting the associated LCK protein to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosines residues within the immunoreceptor tyrosine-based activation motifs (ITAM) of the cytoplasmic tails of the TCR-gamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. Once stimulated, the TCR recruits the tyrosine kinase ZAP7, that becomes phosphorylated and activated by LCK. Following this, a large number of signaling molecules are recruited, ultimately leading to lymphokine production. LCK also contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, which leads to hyperphosphorylation and activation of LCK. Also plays a role in the IL2 receptor-linked signaling pathway that controls the T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR. Phosphorylates other substrates including RUNX3, PTK2B/PYK2, the microtubule-associated protein MAPT, RHOH or TYROBP.

Supplier: ProSci Inc.

Prosapip2 Antibody: Prosapip2 (TBKBP1) is essential for signal transduction during viral infection thus plays a major role in the TNF/NF-kappa B pathway. It is an adaptor protein that constitutively binds TBK1 (TANK-binding kinase) and IKBKE and may play a role in antiviral innate immunity. Prosapip2 is a 615 amino acid adaptor protein belonging to the fibrillar collagen family, consisting of trimers of identical alpha 1 chains which are linked to each other by interchain disulfide bonds. It has a ubiquitous expression with highest levels in ovary, followed by the neuronal system. Prosapip2 binds to TBK1 and helps in the activation of IRF3 which controls the expression of antiviral genes during infection. Recent studies show that Prosapip2 is an interaction partner of ProSAP2/Shank3 and actin, suggesting a role as a linker molecule between postsynaptic density and the cytoskeleton.

Supplier: ProSci Inc.

Ligand for the receptor-type protein-tyrosine kinase KIT. Plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. KITLG/SCF binding can activate several signaling pathways. Promotes phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and subsequent activation of the kinase AKT1. KITLG/SCF and KIT also transmit signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. KITLG/SCF and KIT promote activation of STAT family members STAT1, STAT3 and STAT5. KITLG/SCF and KIT promote activation of PLCG1, leading to the production of the cellular signaling molecules diacylglycerol and inositol-1, 4, 5-trisphosphate. KITLG/SCF acts synergistically with other cytokines, probably interleukins.

Supplier: MP Biomedicals

This product is the lyophilized powder of horseradish peroxidase (HRP)-conjugated goat IgG fraction to rabbit IgG (whole molecule) and buffer salts. Anti-Human IgG is developed in goat using IgG from pooled normal human serum as the immunogen. Whole antiserum is fractionated and then further purified by ion exchange chromatography to provide the IgG fraction of antiserum. This fraction is essentially free of other goat serum proteins. Specificity for human IgG is determined by immunoelectrophoresis (IEP) versus purified human IgA, IgG, IgM, Bence Jones kappa, and Bence Jones lambda myeloma proteins.Identity and purity of the antibody is established by immunoelectrophoresis (IEP), prior to conjugation. Electrophoresis of the antibody preparation followed by diffusion versus anti-goat IgG and anti-goat whole serum result in single arcs of precipitation in the gamma region.

Supplier: MP Biomedicals

Coenzyme A is an essential cofactor in enzymatic acetyl transfer reactions. The principal biologically active forms of pantothenic acid are coenzyme A (CoA) and acyl carrier protein (ACP). In CoA, the business center of the molecule is the pantothenic acid metabolite 4'-phosphopantetheine. Coenzyme A is comprised of 4'-phosphopantetheine linked by an anhydride bond to the nucloetide adenosine 5'-monophosphate. 4'-Phosphopantetheine itself is comprised of pantothenic acid linked at one end, via an amide bond, to beta-mercaptoethylamine, derived from L-cysteine, and at the other end to a phosphate group. The sulfhydryl group of 4'-phosphopantetheine, which is the business end of the coenzyme, forms thioesters with acyl groups producing acyl-CoA derivatives, including acetyl-CoA.
Coenzyme A facilitates removal of lipid peroxides by increasing mobilization of fatty acids, and promote repair of plasma membranes by activating phospholipid synthesis.

Supplier: ProSci Inc.

Hairy/enhancer of split-related proteins, such as HEY1, are basic helix-loop-helix (bHLH) transcription factors implicated in cell fate decision and boundary formation. HEY genes are direct transcriptional targets of the Notch signaling pathways in Drosophila and vertebrates. This gene encodes an estrogen receptor, a ligand-activated transcription factor composed of several domains important for hormone binding, DNA binding, and activation of transcription. The protein localizes to the nucleus where it may form a homodimer or a heterodimer with estrogen receptor 2. Estrogen and its receptors are essential for sexual development and reproductive function, but also play a role in other tissues such as bone. Estrogen receptors are also involved in pathological processes including breast cancer, endometrial cancer, and osteoporosis. Alternative splicing results in several transcript variants, which differ in their 5' UTRs and use different promoters.

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

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: 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.

Recognises a protein of 165 kDa, identified as Desmoglein-2 (DSG2). This monoclonal antibody Recognises the extracellular domain of human desmoglein-2. Desmoglein-2 is a member of the desmosomal cadherin family. Desmosomes are intercellular adhering junctions that represent cell surface attachment sites for intermediate filament. Desmocollins and desmogleins are the main desmosomal transmembrane proteins. Desmogleins consist of Dsg1, Dsg2, Dsg3, and Dsg4 isoforms. Within the desmosome, the extracellular domain of desmoglein is essential for calcium dependent heterophilic binding to the desmocollins, whereas the intracellular domain is essential for binding to the desmosomal plaque protein, plakoglobin. Human Desmoglein-2 is a type I transmembrane glycoprotein of 1117 amino acid (aa) residues with a 23 aa signal peptide and a 25 aa propeptide. It differs from other classic cadherins by having four instead of five cadherin repeat domains in its extracellular region, and a much larger cytoplasmic region containing five desmoglein repeat domains which share homology with the cadherin repeats. Instead of having the HAV adhesion motif found in type I cadherins, desmogleins have R/YAL as the adhesion motif on its amino-terminal cadherin repeat. The cytoplasmic tails of desmogleins interact with desmoplakins, plakoglobin and plakophilins. In turn, these proteins link the desmogleins with the intermediate filaments. Desmoglein-2 has been shown to be important in establishing cell-cell adhesion and function in epithelial cells. Desmoglein2 was originally identified in colon carcinoma and colon, and was named HDGC (human desmoglein colon).

Supplier: ProSci Inc.

APC4 Antibody: Cell cycle regulated protein ubiquitination and degradation within subcellular domains is thought to be essential for the normal progression of mitosis. APC4 is a highly conserved component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. APC/C is responsible for degrading anaphase inhibitors, mitotic cyclins, and spindle-associated proteins ensuring that events of mitosis take place in proper sequence. The individual APC/C components mRNA and protein levels are expressed at approximately the same levels in most tissues and cell lines, suggesting that they perform their functions as part of a complex. While little is known of APC4, it is thought that APC4 associates with other APC/C components APC1, APC5, and CDC23 interdependently, such that loss of any one subunit reduces binding between the remaining three.

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

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: 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: 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.

ARL15 Antibody: ADP-ribosylation factors (ARFs) are highly conserved guanine nucleotide binding proteins that enhance the ADP-ribosyltransferase activity of cholera toxin. ARFs are important in eukaryotic vesicular trafficking pathways and they play an essential role in the activation of phospholipase D (PC-PLD). ARL15 (ADP-ribosylation factor-like 15), is a member of the ARF family of the Ras superfamily of small GTPases that are known to be involved in multiple regulatory pathways altered in human carcinogenesis. Other members of this protein family include ARL11, thought to be a tumor suppressor and may play a role in the regulation of apoptosis, ARL2 which plays an important role in microtubule dynamics and cell cycle progression, and ARL4, which may play a role in neurogenesis during embryonic development. The gene encoding ARL15 maps to chromosome 5p15 in humans. At least three isoforms of ARL15 are known to exist.

Supplier: ProSci Inc.

The protein encoded by MCM4 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 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, 6 and 7 proteins possesses DNA helicase activity, and may act as a DNA unwinding enzyme. The phosphorylation of this protein by CDC2 kinase reduces the DNA helicase activity and chromatin binding of the MCM complex. This gene is mapped to a region on the chromosome 8 head-to-head next to the PRKDC/DNA-PK, a DNA-activated protein kinase involved in the repair of DNA double-strand breaks. Alternatively spliced transcript variants encoding the same protein have been reported.

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: ProSci Inc.

The protein encoded by MCM4 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 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, 6 and 7 proteins possesses DNA helicase activity, and may act as a DNA unwinding enzyme. The phosphorylation of this protein by CDC2 kinase reduces the DNA helicase activity and chromatin binding of the MCM complex. This gene is mapped to a region on the chromosome 8 head-to-head next to the PRKDC/DNA-PK, a DNA-activated protein kinase involved in the repair of DNA double-strand breaks. Alternatively spliced transcript variants encoding the same protein have been reported.

Supplier: ProSci Inc.

APC5 Antibody: Cell cycle regulated protein ubiquitination and degradation within subcellular domains is thought to be essential for the normal progression of mitosis. APC5 is a highly conserved component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. APC/C is responsible for degrading anaphase inhibitors, mitotic cyclins, and spindle-associated proteins ensuring that events of mitosis take place in proper sequence. The individual APC/C components mRNA and protein levels are expressed at approximately the same levels in most tissues and cell lines, suggesting that they perform their functions as part of a complex. While little is known of APC5, it is thought that APC5 associates with other APC/C components APC1, APC4, and CDC23 interdependently, such that loss of any one subunit reduces binding between the remaining three.

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.

IRF6 is a member of the interferon regulatory transcription factor (IRF) family. Family members share a highly-conserved N-terminal helix-turn-helix DNA-binding domain and a less conserved C-terminal protein-binding domain. Mutations in its gene can cause van der Woude syndrome and popliteal pterygium syndrome. This protein is involved in palate formation.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: ProSci Inc.

CD63 functions as cell surface receptor for TIMP1 and plays a role in the activation of cellular signaling cascades. Plays a role in the activation of ITGB1 and integrin signaling, leading to the activation of AKT, FAK/PTK2 and MAP kinases. Promotes cell survival, reorganization of the actin cytoskeleton, cell adhesion, spreading and migration, via its role in the activation of AKT and FAK/PTK2. Plays a role in VEGFA signaling via its role in regulating the internalization of KDR/VEGFR2. Plays a role in intracellular vesicular transport processes, and is required for normal trafficking of the PMEL luminal domain that is essential for the development and maturation of melanocytes. Plays a role in the adhesion of leukocytes onto endothelial cells via its role in the regulation of SELP trafficking. May play a role in mast cell degranulation in response to Ms4a2/FceRI stimulation, but not in mast cell degranulation in response to other stimuli. [UniProt].

Supplier: ProSci Inc.

FABP7 Antibody: FABP7 was initially isolated from a human fetal brain cDNA library and whose mRNA was expressed in adult brain and muscle tissues at low levels. The protein encoded by this gene is a member of the fatty acid binding protein (FABPs) family, a group of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABPs are thought to play roles in fatty acid uptake, transport, and metabolism. FABP7 is a downstream gene of the Pax6 transcription factor and has been suggested to be essential for the maintenance of neuroepithelial cells during early cortical development. More recently, FABP7 was found to be frequently expressed in melanomas. Down-regulation of FABP7 through RNAi expression could reduce in vitro cell proliferation and Matrigel invasion, suggesting that FABP7 may be a potential target for the development of diagnostic and therapeutic tools.

Supplier: ProSci Inc.

Recognises a protein of 165 kDa, identified as Desmoglein-2 (DSG2). This monoclonal antibody Recognises the extracellular domain of human desmoglein-2. Desmoglein-2 is a member of the desmosomal cadherin family. Desmosomes are intercellular adhering junctions that represent cell surface attachment sites for intermediate filament. Desmocollins and desmogleins are the main desmosomal transmembrane proteins. Desmogleins consist of Dsg1, Dsg2, Dsg3, and Dsg4 isoforms. Within the desmosome, the extracellular domain of desmoglein is essential for calcium dependent heterophilic binding to the desmocollins, whereas the intracellular domain is essential for binding to the desmosomal plaque protein, plakoglobin. Human Desmoglein-2 is a type I transmembrane glycoprotein of 1117 amino acid (aa) residues with a 23 aa signal peptide and a 25 aa propeptide. It differs from other classic cadherins by having four instead of five cadherin repeat domains in its extracellular region, and a much larger cytoplasmic region containing five desmoglein repeat domains which share homology with the cadherin repeats. Instead of having the HAV adhesion motif found in type I cadherins, desmogleins have R/YAL as the adhesion motif on its amino-terminal cadherin repeat. The cytoplasmic tails of desmogleins interact with desmoplakins, plakoglobin and plakophilins. In turn, these proteins link the desmogleins with the intermediate filaments. Desmoglein-2 has been shown to be important in establishing cell-cell adhesion and function in epithelial cells. Desmoglein2 was originally identified in colon carcinoma and colon, and was named HDGC (human desmoglein colon).