33225 Results for: "Eosin+Y&pageNo=68"

Supplier: Bioss

ADAMTS (A Disintegrin And Metalloproteinase Domain with Thrombospondin type 1 Modules) is a family of zinc-dependent proteases that are implicated in a variety of normal and pathological conditions, including arthritis and cancer. ADAMTS protein family members contain an amino-terminal propeptide domain, a metalloproteinase domain, a disintegrin-like domain and a carboxy-terminus that contains a varying number of Thrombospondin type 1 (TSP-1) motifs. ADAMTS-L2 (ADAMTS-like protein 2) is a 951 amino acid secreted protein that is highly expressed in lung, kidney and liver. Mutations in the gene encoding ADAMTS are the cause of geleophysic dysplasia, an autosomal recessive disorder characterised by cardiac vavular anomalies, short stature, thick skin and brachydactyly. In individuals affected with geleophysic dysplasia, there is a significant increase in total active TGF-beta 1 and nuclear locations of p-SAMD2 in fibroblasts. Interestingly, ADAMTS-L2 interacts with LTBP-1, a glycoprotein that is part of the platelet-derived TGF-beta 1 complex.

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RAP2B belongs to a family of RAS-related GTP-binding proteins. RAP proteins share approximately 50% amino acid identity with the classical RAS proteins and have numerous structural features in common. However, at their 61st amino acid the glutamine in RAS proteins is replaced by threonine in RAP proteins. RAP2A interacts with phospholipase C, epsilon 1 (PLCE1).

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Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles (By similarity).

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May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase (By similarity). Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement.

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C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system.

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Microfibrillar-associated protein 1; MFAP1_HUMAN.

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Slc9a9 (Sodium/hydrogen exchanger 9) or NHE9 may act in electroneutral exchange of protons for Na(+) across membranes. Four isoforms of the Na+/H+ exchanger (NHE6-NHE9) are distributed to intracellular compartments in human cells. They are localised to Golgi and post-Golgi endocytic compartments as follows: mid- to trans-Golgi, NHE8; trans-Golgi network, NHE7; early recycling endosomes, NHE6; and late recycling endosomes, NHE9. The intracellular localization of the NHEs is established by the balance of transport in and out of the post-Golgi compartments as the dynamic membrane trafficking. Their in vivo function is to regulate the pH and monovalent cation concentration in these organelles.

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GDAP2.

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Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors and for proper positioning of neurons during brain development. Also implicated in the migration and selfrenewal of neural progenitors. May play a role in centriole duplication during mitosis (By similarity).

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C1orf148

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Has both beta-1,3-glucuronic acid and beta-1,4-N-acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer. Isoform 2 may facilitate PARK2 transport into the mitochondria. In collaboration with PARK2, isoform 2 may enhance cell viability and protect cells from oxidative stress.

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Detected at the highest levels in peripheral blood leukocytes and breast cancer cell lines. Found in leukocytes of the myeloid lineage, with the strongest expression observed in granulocytes and no detectable expression in lymphocytes. Expressed in thymic epithelial cells and fibroblasts. Belongs to the SECTM family.

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Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.

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Hydrolyses extracellular nucleotides into membrane permeable nucleosides. Exhibits AMP-, NAD-, and NMN-nucleosidase activities.

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C2orf69.

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Members of the protein-tyrosine phosphatase superfamilycooperate with protein kinases to regulate cell proliferation anddifferentiation. This superfamily is separated into two familiesbased on the substrate that is dephosphorylated. One family, thedual specificity phosphatases (DSPs) acts on both phosphotyrosineand phosphoserine/threonine residues. This gene encodes differentbut related DSP proteins through the use of non-overlapping openreading frames, alternate splicing, and presumed differenttranscription promoters. Expression of the distinct proteins fromthis gene has been found to be tissue specific and the proteins maybe involved in postnatal development of specific tissues. A proteinencoded by the upstream ORF was found in skeletal muscle, whereasthe encoded protein from the downstream ORF was found only intestis. In mouse, a similar pattern of expression was found.Multiple alternatively spliced transcript variants were described,but the full-length sequence of only some were determined.[provided by RefSeq, Jul 2008].

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IGFBPL1 is a secreted IGF (Insulin-like growth factor) binding protein that is known to contain an Ig-like C2-type (immunoglobulin-like) domain, an IGFBP N-terminal domain and a Kasal-like domain. IGF-binding proteins characteristically act to extend the half-life of IGFs and may influence the growth promoting effects of the IGFs. The interaction of IGFBPs with IGFs can affect cell surface receptors, specifically, IGFBPs may enhance or decrease a cells insulin sensitivity. IGFBPL1 has been found to be down-regulated in multiple tumors and thus may be a likely tumor suppressor candidate. Highly expressed in both brain and testis, IGFBPL1 is found at lower levels in the prostate, bladder and lung.

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This gene encodes a protein that phosphorylates carbohydrates such as ribulose, ribitol, and L-arabinitol. Genome-wide association studies in some populations have found an association between polymorphisms in this gene and sporadic amyotrophic lateral sclerosis, but studies of other populations have not been able to replicate this association. Alternative splicing results in multiple transcript variants.

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The minichromosome maintenance protein 3 (MCM3) is one of the MCM proteins essential for the initiation of DNA replication. The protein encoded by this gene is a MCM3 binding protein. It was reported to have phosphorylation-dependent DNA-primase activity, which was up-regulated in antigen immunisation induced germinal center. This protein was demonstrated to be an acetyltransferase that acetylates MCM3 and plays a role in DNA replication. The mutagenesis of a nuclear localisation signal of MCM3 affects the binding of this protein with MCM3, suggesting that this protein may also facilitate MCM3 nuclear localisation.

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This is a receptor for the anterior pituitary hormone prolactin (PRL). Acts as a prosurvival factor for spermatozoa by inhibiting sperm capacitation through suppression of SRC kinase activation and stimulation of AKT. Isoform 4 is unable to transduce prolactin signaling. Isoform 6 is unable to transduce prolactin signaling.

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The protein encoded by this gene belongs to the NALP protein family. Members of the NALP protein family typically contain a NACHT domain, a NACHT-associated domain (NAD), a C-terminal leucine-rich repeat (LRR) region, and an N-terminal pyrin domain (PYD). This protein may play a regulatory role in the innate immune system as similar family members belong to the signal-induced multiprotein complex, the inflammasome, that activates the pro-inflammatory caspases, caspase-1 and caspase-5.

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The gene encoding the Mixed-Lineage Leukemia (MLL) proteins is located on chromosome 11q23. Chromosomal translocations involving band 11q23 result in rogue activator proteins that are associated with approximately 10% of patients with acute lymphoblastic leukemia (ALL) and 5% of patients with acute myeloid leukemia (AML). Most patients affected are less than 1 year of age. MLLT11, also known as mixed-lineage leukemia translocated to 11 or AF1q, is a 90 amino acid MLL fusion partner. Based on the expression patterns of MLLT11, it is thought that MLLT11 plays a role in leukemogenesis and, specifically, the progression of acute monocytic leukemia (AML). Also, expressed in embryonic brain cortex, MLLT11 is upregulated during neuronal differentiation and is thought to play a role in the development of the central nervous system. Finally, MLLT11 has been shown to be differentially expressed in highly metastatic cells, in comparison with non-metastatic parent cells. Such findings suggest a role of MLLT11 in tumorigenesis.

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GPR120, a member of the rhodopsin family of G protein-coupled receptors (GPCRs), is a 377 amino acid protein which is expressed in the intestine. GPR120 is a receptor for unsaturated long-chain FFAs (free fatty acids). FFAs act as signaling molecules and are an important energy source. They also employ various physiological responses through their GPCRs. One such response occurs when dietary FFAs stimulate GPR120. This stimulation promotes the secretion of glucagon-like peptide 1 (GLP-1) in vivo and in vitro. GLP-1 belongs to the class of molecules known as the incretins, which are associated with insulin secreted from the pancreas as a result of food intake. GLP-1 also inhibits glucagon and gastric acid secretion and gastric emptying. Consequently, the role of GPR120 in the secretion of GLP-1 is critical in the treatment of diabetes.

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Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins MAP1LC3, GABARAPL1, GABARAPL2 and GABARAP, to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Has also an activity of delipidating enzyme for the PE-conjugated forms.

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Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Binding of extracellular ligands such as growth factors, cytokines and hormones to their cell-surface receptors activates RAS and this initiates RAF1 activation. RAF1 then further activates the dual-specificity protein kinases MAP2K1/MEK1 and MAP2K2/MEK2. Both MAP2K1/MEK1 and MAP2K2/MEK2 function specifically in the MAPK/ERK cascade, and catalyse the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2, leading to their activation and further transduction of the signal within the MAPK/ERK cascade. Depending on the cellular context, this pathway mediates diverse biological functions such as cell growth, adhesion, survival and differentiation, predominantly through the regulation of transcription, metabolism and cytoskeletal rearrangements. One target of the MAPK/ERK cascade is peroxisome proliferator-activated receptor gamma (PPARG), a nuclear receptor that promotes differentiation and apoptosis. MAP2K1/MEK1 has been shown to export PPARG from the nucleus. The MAPK/ERK cascade is also involved in the regulation of endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC), as well as in the fragmentation of the Golgi apparatus during mitosis.

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The Hox proteins play a role in patterns of embryonic development and cellular differentiation by regulating downstream target genes. in vivo, the HoxD9 protein interacts with the autoregulatory and cross-regulatory enhancers of the murine HoxB1 and human HoxD9 genes. Specifically, the HoxD9 protein interacts with the human control region (HCR) of the HoxD9 gene, thus inducing transcription of the HoxD9 promoter. HoxD9 may be a multifunctional transcriptional regulator, as it contains different activation domains. Activation of HoxD9 depends on the structure of the target regulatory element, and results in differential cofactor interaction. The HoxD9 protein is expressed in the early stages of mouse joint development, primarily in the articular cartilage. HoxD9 transcripts are also detected in the synovial tissue of arthritic mice, but not in that of normal mice, suggesting that HoxD9 may have a role in the pathology of arthritis. Furthermore, the HoxD9 protein is highly expressed in the synoviocytes of patients with rheumatoid arthritis (RA), but not in osteoarthritis patients. The human HoxD9 protein is also differentially expressed in the human cervical cancer cell line HeLa, but is not expressed in the normal cervix and may thus play a role in tumorigenesis.

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The amphoterin-induced gene and ORF (AMIGO) family of proteins consists of AMIGO-1, AMIGO-2 and AMIGO-3. All three members are single pass type I membrane proteins that contain several leucine-rich repeats, one IgG domain, and a transmembrane domain. The AMIGO proteins are specifically expressed on fiber tracts of neuronal tissues and participate in their formation. The AMIGO proteins can form complexes with each other, but can also bind itself. AMIGO-1, also designated Alivin-2, promotes growth and fasciculation of neurites and plays a role in myelination and fasciculation of developing neural axons. In cerebellar neurons, AMIGO-2 (Alivin-1) is crucial for depolarisation-dependent survival. Similar to AMIGO-1 and AMIGO-2, AMIGO-3 (Alivin-3) plays a role in homophilic and/or heterophilic cell-cell interaction and signal transduction.

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F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.

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The A Kinase Anchor proteins (AKAPs) are a group of structurally diverse proteins, which have the common function of binding to the regulatory subunit of protein kinase A (PKA) and confining the holoenzyme to discrete locations within the cell. AKAP6 is a member of the AKAP family. It is highly expressed in various brain regions and cardiac and skeletal muscle. It is specifically localised to the sarcoplasmic reticulum and nuclear membrane, and is involved in anchoring PKA to the nuclear membrane or sarcoplasmic reticulum.

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Poly (ADP-ribosylation) is a method of DNA damage-dependent posttranslational modification that helps to rescue injured proliferating cells from cell death. The PARP (poly (ADP-ribose) polymerase) proteins comprise a superfamily of enzymes that functionally modify histones and other nuclear proteins, thereby preventing cell death. PARPs use NAD+ as a substrate to catalytically transfer ADP-ribose residues onto protein acceptors; a process that, when repeated multiple times, leads to the formation of poly (ADPribose) chains on the protein. The presence of these chains alters the function of the target protein and promotes cell survival. PARP proteins are implicated in a variety of diseases, including cancer, neurodegenerative and inflammatory disorders. PARP-16 is a 322 amino acid poly (ADP-ribose) polymerase protein localised to the membrane. Expressed as three isoforms produced by alternative splicing, PARP-16 contains one PARP catalytic domain.