"Bioss"

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Endoplasmic reticulum proteins (ERps) are widely expressed proteins and localize to the ER. ERp19, ERp29, ERp46, ERp57 and ERp72 may act as proteases, protein disulfide isomerases, thiol-disulfide oxidases, phospholipases or a combination of these. ERp19, also designated thioredoxin domain-containing protein 12 (TXNDC12), and ERp46, also designated thioredoxin domain containing 5 (TXNDC5), belong to the thioredoxin superfamily and contain a thioredoxin fold with a consensus active-site sequence (CxxC). Both ERp19 and ERp46 are widely expressed ER luminal proteins that are most abundant in the liver and are enriched in purified liver ER vesicles. ERp19 shows significant protein thiol-disulfide oxidase activity in vitro, which is dependent on the presence of both active-site cysteines.

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Apolipoprotein E, a main apoprotein of the chylomicron, binds to a specific receptor on liver cells and peripheral cells and is essential for the normal catabolism of triglyceride-rich lipoprotein constituents.ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. Compared with E3 and E4, E2 exhibits the lowest receptor binding affinity. Defects in ApoE are a cause of hyperlipoproteinemia type III due to increased plasma cholesterol and triglycerides levels which are the consequence of impaired clearance of chylomicron and VLDL remnants.Summary: Chylomicron remnants and very low density lipoprotein (VLDL) remnants are rapidly removed from the circulation by receptor-mediated endocytosis in the liver. Apolipoprotein E, a main apoprotein of the chylomicron, binds to a specific receptor on liver cells and peripheral cells. ApoE is essential for the normal catabolism of triglyceride-rich lipoprotein constituents. The APOE gene is mapped to chromosome 19 in a cluster with APOC1 and APOC2. Defects in apolipoprotein E result in familial dysbetalipoproteinemia, or type III hyperlipoproteinemia (HLP III), in which increased plasma cholesterol and triglycerides are the consequence of impaired clearance of chylomicron and VLDL remnants. [provided by RefSeq, Jul 2008].

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SR-A1 (serine arginine-rich pre-mRNA splicing factor) is a member of the SR protein family, which interacts with the C-terminal domain of the large subunit of RNA polymerase II and involved in pre-mRNA splicing. The SR-A1 gene is located on chromosome 19q13.3-q13.4. Overexpression of SR-A1 is found in aggressive ovarian cancers.

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Human papilloma viruses (HPVs) can be classified as either high risk or low risk according to their association with cancer. HPV16 and HPV18 are the most common of the high risk group while HPV6 and HPV11 are among the low risk types. Approximately 90% of cervical cancers contain HPV DNA of the high risk types. Mutational analysis have shown that the E6 and E7 genes of the high risk HPVs are necessary and sufficient for HPV transforming function. The specific interactions of the E6 and E7 proteins with p53 and pRB, respectively, correlate with HPV high and low risk classifications. The high risk HPV E7 proteins bind to pRB with a higher affinity than do the low risk HPV proteins, and only the high risk HPV E6 proteins form detectable complexes with p53 in vitro. Human papillomaviruses (HPV) are small DNA viruses which infect epithelia of the skin and mucosa. Over 90 types have been identified and they mostly cause a variety of benign lesions such as warts and verrucae. However, some subtypes, notably types 16 and 18, 31 and 33, have been confirmed as agents which cause cervical cancer. The E6 protein is a transcriptional transactivator. Binds double-stranded DNA. This protein may be involved in the oncogenic potential of this virus (cervical neoplasia-associated virus).

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The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterized by a canonical death domain fold, which consists of a bundle of five or six antiparallel α-helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localized to the cytoplasm, ASC2 interacts with ASC to modulate NF-κB and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.

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MARCKS, (Myristoylated Alanine-Rich C Kinase Substrate), is a member of a family of calmodulin binding proteins and is a major substrate for phosphorylation by protein kinase C (PKC). The phosphorylation of Ser152/156 can be used as a measure of PKC activation. Phosphorylation of Ser152/156 modulates the binding of MARCKS to calmodulin.

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MARCH5 is a member of the E3 ubiquitin-protein ligase family. This mitochonrial E3 ubiquitin-protein ligase plays an importnat role in controlling the morphology of the mitochondria. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. MARCH5 has been shown to interact with MTFN2 and ubiquitinated forms of DRP1.

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Anti-GRP Rabbit Polyclonal Antibody

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Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle. When phosphorylated, highly effective in activating G2 cells into prophase. Directly dephosphorylates CDK1 and activates its kinase activity.

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In eukaryotes, it is essential to have the ability to detect and degrade transcripts that lack full coding potential. Nonsense-mediated RNA decay (NMD) protects the organism by avoiding the translation of truncated peptides with dominant negative or deleterious gain-of-function potential. Rent1, a mammalian ortholog of Upflp, is essential for embryonic viability (1–3). Rent1 (also designated regulator of nonsense transcripts and HUpf1) contains an N-terminal zinc finger-like domain, NTPase domains and a region comprised of domains that define Rent1 as a superfamily group I helicase.

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Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2.

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This gene encodes a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This gene is located on chromosome 13 within the minimal deletion region for B-cell chronic lymphocytic leukemia. Multiple alternatively spliced transcript variants have been found for this gene.

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Inhibits the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF produced by activated macrophages and by helper T-cells.

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MLF1 Interacting protein (also known as PBIP1, MLF1IP1, KLIP1 or KSHV latent nuclear antigen interacting protein 1) is a component of the CENPA nucleosome-associated complex (CENPA NAC), which plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. This protein is involved in transcriptional repression and interacts with the N-terminal domain of Kaposi Sarcoma Herpesvirus latent nuclear antigen (KSHV LNA).

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Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.

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Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. M-cadherin is part of the myogenic program and may provide a trigger for terminal muscle differentiation.