495862 Results for: "Total Dietary Fiber Kit Reagent Kit for 100 Determinations"

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VOL.FLASK 100ML NS12/21 A HOLLOW GLASS 1 * 2 items

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MEASURING CYLINDER 100ML HF DUR. W.CERT. 1 * 2 items

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The c-Jun proto-oncogene was first identified as the cellular homolog of the avian sarcoma virus v-Jun oncogene. The c-Jun protein, along with c-Fos, is a component of the AP-1 transcriptional complex. c-Jun can form either Jun/Jun homodimers or Jun/Fos heterodimers via the leucine repeats in both proteins. Jun B and Jun D, have been shown to be almost identical to c-Jun in their C-terminal regions, which are involved in dimerization and DNA binding, whereas their N-terminal domains, which are involved in transcriptional activation, diverge. JunB is involved in many types of human carcinoma including T-cell lymphomas, CML,primary cutaneous lymphomas. Aberrantly expressed c-Jun and JunB are a hallmark of Hodgkin lymphoma cells, stimulate proliferation and synergize with NF-kappa B. JunB potentiates function of BRCA1 activation domain 1 (AD1) through a coiled-coil-mediated interaction.JunB is an important regulator of erythroid Differentiation.

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PUF60 is a Ro RNP-binding protein. It interacts with Ro RNPs and their interaction is thought to represent a gain of function for Ro RNPs. This protein also forms a ternary complex with far upstream element (FUSE) and FUSE-binding protein. It can repress a c-myc reporter via the FUSE. It is also known to target transcription factor IIH and inhibit activated transcription.The protein encoded by this gene is a Ro RNP-binding protein. It interacts with Ro RNPs and their interaction is thought to represent a gain of function for Ro RNPs. This protein also forms a ternary complex with far upstream element (FUSE) and FUSE-binding protein. It can repress a c-myc reporter via the FUSE. It is also known to target transcription factor IIH and inhibit activated transcription. This gene is implicated in the xeroderma pigmentosum disorder. There are two alternatively spliced transcript variants of this gene encoding different isoforms. There seems to be evidence of multiple polyadenylation sites for this gene.

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Programmed cell death protein 1 (PD-1) is also known as CD279 and PDCD1, is a type I membrane protein and is a member of the extended CD28/CTLA-4 family of T cell regulators. PDCD1 is expressed on the surface of activated T cells, B cells, macrophages, myeloid cells and a subset of thymocytes. PD-1 has two ligands, PD-L1 and PD-L2, which are members of the B7 family. PD-L1 is expressed on almost all murine tumor cell lines, including PA1 myeloma, P815 mastocytoma, and B16 melanoma upon treatment with IFN-γ. PD-L2 expression is more restricted and is expressed mainly by DCs and a few tumor lines. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. In vitro, treatment of anti-CD3 stimulated T cells with PD-L1-Ig results in reduced T cell proliferation and IFN-γ secretion. Monoclonal antibodies targeting PD-1 that boost the immune system are being developed for the treatment of cancer.

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PHF1 has significant sequence similarity with Drosophila Polycomblike. It contains a zinc finger-like PHD (plant homeodomain) finger which is distinct from other classes of zinc finger motifs and which shows the typical Cys4-His-Cys3 arrangement. PHD finger genes are thought to belong to a diverse group of transcriptional regulators possibly affecting eukaryotic gene expression by influencing chromatin structure. This gene encodes a protein with significant sequence similarity to Drosophila Polycomblike. The encoded protein contains a zinc finger-like PHD (plant homeodomain) finger which is distinct from other classes of zinc finger motifs and which shows the typical Cys4-His-Cys3 arrangement. PHD finger genes are thought to belong to a diverse group of transcriptional regulators possibly affecting eukaryotic gene expression by influencing chromatin structure. Two transcript variants have been found for this gene.

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Programmed cell death protein 1 (PD-1) is also known as CD279 and PDCD1, is a type I membrane protein and is a member of the extended CD28/CTLA-4 family of T cell regulators. PDCD1 is expressed on the surface of activated T cells, B cells, macrophages, myeloid cells and a subset of thymocytes. PD-1 has two ligands, PD-L1 and PD-L2, which are members of the B7 family. PD-L1 is expressed on almost all murine tumor cell lines, including PA1 myeloma, P815 mastocytoma, and B16 melanoma upon treatment with IFN-γ. PD-L2 expression is more restricted and is expressed mainly by DCs and a few tumor lines. PD1 inhibits the T-cell proliferation and production of related cytokines including IL-1, IL-4, IL-10 and IFN-γ by suppressing the activation and transduction of PI3K/AKT pathway. In addition, coligation of PD1 inhibits BCR-mediating signal by dephosphorylating key signal transducer. In vitro, treatment of anti-CD3 stimulated T cells with PD-L1-Ig results in reduced T cell proliferation and IFN-γ secretion. Monoclonal antibodies targeting PD-1 that boost the immune system are being developed for the treatment of cancer.

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DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this DEAD box protein family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. DDX50 is a DEAD box enzyme that may be involved in ribosomal RNA synthesis or processing. DDX50 and DDX21, also called RH-II/GuA, have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. DDX50 gene has pseudogenes on chromosomes 2, 3 and 4. Alternative splicing of this gene generates multiple transcript variants, but the full length nature of all the other variants but one has not been defined.

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HIV-1, the causative agent of acquired immunodeficiency syndrome (AIDS), contains an RNA genome that produces a chromosomally integrated DNA during the replicative cycle. Activation of HIV-1 gene expression by the transactivator Tat is dependent on an RNA regulatory element (TAR) located downstream of the transcription initiation site. TARDBP is a transcriptional repressor that binds to chromosomally integrated TAR DNA and represses HIV-1 transcription.HIV-1, the causative agent of acquired immunodeficiency syndrome (AIDS), contains an RNA genome that produces a chromosomally integrated DNA during the replicative cycle. Activation of HIV-1 gene expression by the transactivator Tat is dependent on an RNA regulatory element (TAR) located downstream of the transcription initiation site. The protein encoded by this gene is a transcriptional repressor that binds to chromosomally integrated TAR DNA and represses HIV-1 transcription. In addition, this protein regulates alternate splicing of the CFTR gene. A similar pseudogene is present on chromosome 20.

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The c-Jun proto-oncogene was first identified as the cellular homolog of the avian sarcoma virus v-Jun oncogene. The c-Jun protein, along with c-Fos, is a component of the AP-1 transcriptional complex. c-Jun can form either Jun/Jun homodimers or Jun/Fos heterodimers via the leucine repeats in both proteins. Jun B and Jun D, have been shown to be almost identical to c-Jun in their C-terminal regions, which are involved in dimerization and DNA binding, whereas their N-terminal domains, which are involved in transcriptional activation, diverge. JunB is involved in many types of human carcinoma including T-cell lymphomas, CML,primary cutaneous lymphomas. Aberrantly expressed c-Jun and JunB are a hallmark of Hodgkin lymphoma cells, stimulate proliferation and synergize with NF-kappa B. JunB potentiates function of BRCA1 activation domain 1 (AD1) through a coiled-coil-mediated interaction.JunB is an important regulator of erythroid Differentiation.

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Tyrosine-protein phosphatase non-receptor type substrate 1 (SHPS1) is also known as CD172 antigen-like family member A (CD172a), Macrophage fusion receptor, MyD-1 antigen, Signal-regulatory protein alpha (SIRPA or SIRP alpha) or p84, is a member of the SIRP family, and also belongs to the immunoglobulin superfamily. SIRP alpha is Ubiquitous and highly expressed in brain. SIRPA / CD172a is immunoglobulin-like cell surface receptor for CD47 and acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. SIRPA / SHPS-1 supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment and may play a key role in intracellular signaling during synaptogenesis and in synaptic function By similarity. SIRPA / MyD1 involved in the negative regulation of receptor tyrosine kinase-coupled cellular responses induced by cell adhesion, growth factors or insulin and mediates negative regulation of phagocytosis, mast cell activation and dendritic cell activation. CD47 binding prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells.

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CYP3A7 is a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This enzyme hydroxylates testosterone and dehydroepiandrosterone 3-sulphate, which is involved in the formation of estriol during pregnancy. The enzyme also metabolizes some drugs such as aflatoxin B1.This gene, CYP3A7, encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This enzyme hydroxylates testosterone and dehydroepiandrosterone 3-sulphate, which is involved in the formation of estriol during pregnancy. The enzyme also metabolizes some drugs such as aflatoxin B1. This gene is part of a cluster of cytochrome P450 genes on chromosome 7q21.1. Transcript variants have been described, but it is not known whether these transcripts are normally produced.

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Cluster of differentiation 14 (CD14), is a cell surface glycoprotein, and is a is a component of the innate immune system. CD14 is a myelomonocytic differentiation antigen preferentially expressed on monocytes, macrophages, and activated granulocytes. CD14 exists in two forms. Either it is anchored into the membrane by a glycosylphosphatidylinositol tail (mCD14) or it appears in a soluble form (sCD14). Soluble CD14 either appears after shedding of mCD14 (48 kDa) or is directly secreted from intracellular vesicles (56 kDa). CD14 acts as a co-receptor (along with the Toll-like receptor TLR 4 and MD-2) for the detection of bacterial lipopolysaccharide (LPS). CD14 can bind LPS only in the presence of lipopolysaccharide-binding protein (LBP). CD14 has been proposed to be involved in various biological processes, including transportation of other lipids, cell-cell interaction during different immune responses, as well as recognition of apoptotic cells. Although LPS is considered its main ligand, CD14 also recognizes other pathogen-associated molecular patterns. CD14+ cells are monocytes that can differentiate into a host of different cells. CD14 has been shown to interact with Lipopolysaccharide-binding protein.

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Bacteriophage T7 RNA Polymerase is a DNA-dependent RNA polymerase with high specificity for the T7 promoter. This enzyme catalyzes t he 5Æ to 3Æ synthesis of RNA from DNA downstream from its promoter.
This product with activity data is belong to b 1 * 25.000 Unit

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CF™583 succinimidyl ester is a superior deep-red fluorescent dye with an amine-reactive group. CF™583 is spectrally identical to Cy® 3.5 but yields much brighter protein conjugates due to its high quantum yield and exceptional water solubility. 1 * 1 µmol

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The ULT25NEU is the only portable ULT freezer solution available today for bringing ULT storage to the patient. This small lightweight, and efficient portable −80 °C freezer is ideal for clinical trials and biologic drug delivery.

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Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates.

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Cell surface protein involved in cell-cell-interactions, exocytosis of secretory granules and regulation of signal transmission. Function is isoform-specific. Alpha-type isoforms have a long N-terminus with six laminin G-like domains and play an important role in synaptic signal transmission. Alpha-type isoforms play a role in the regulation of calcium channel activity and Ca(2+)-triggered neurotransmitter release at synapses and at neuromuscular junctions. They play an important role in Ca(2+)-triggered exocytosis of secretory granules in pituitary gland. They may effect their functions at synapses and in endocrine cells via their interactions with proteins from the exocytotic machinery. Likewise, alpha-type isoforms play a role in regulating the activity of postsynaptic NMDA receptors, a subtype of glutamate-gated ion channels. Both alpha-type and beta-type isoforms may play a role in the formation or maintenance of synaptic junctions via their calcium-dependent interactions (via the extracellular domains) with neuroligin family members, CBLN1 or CBLN2. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Alpha-type isoforms were first identified as receptors for alpha-latrotoxin from spider venom (By similarity).

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The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. SLITRK5 (SLIT and NTRK-like family, member 5), also known as LRRC11 (leucine-rich repeat-containing protein 11), is a 958 amino acid single-pass type I membrane protein that contains 16 LRR repeats and belongs to the SLITRK family. Expressed at high levels in the cerebral cortex, but also present in areas of the spinal cord and medulla, SLITRK5 functions to suppress neurite outgrowth, thereby playing a regulatory role in neuronal function. The gene encoding SLITRK5 maps to human chromosome 13, which houses over 400 genes, such as BRCA2 and RB1, and comprises nearly 4% of the human genome. Trisomy 13, also known as Patau syndrome, is deadly and the few who survive past one year suffer from permanent neurologic defects, difficulty eating and vulnerability to serious respiratory infections.

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Induces susceptibility to atherosclerosis (By similarity). Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-69 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes. Prevents phagocyte ingestion of closely apposed viable cells by transmitting 'detachment' signals, and changes function on apoptosis, promoting tethering of dying cells to phagocytes (the encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces leads to the viable cell's active repulsion from the phagocyte. During apoptosis, the inside-out signaling of PECAM1 is somehow disabled so that the apoptotic cell does not actively reject the phagocyte anymore. The lack of this repulsion signal together with the interaction of the eat-me signals and their respective receptors causes the attachment of the apoptotic cell to the phagocyte, thus triggering the process of engulfment). Isoform Delta15 is unable to protect against apoptosis. Modulates BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in human umbilical cord vein cells (HUVEC).

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Structural Maintenance of Chromosomes (SMC) family proteins play critical roles in various nuclear events that require structural changes of chromosomes, including mitotic chromosome organization, DNA recombination and repair and global transcriptional repression. The chromosome proteins are conserved in eukaryotes and can lead to mitotic chromosome segregation defects, suggesting a critical function of SMC family proteins in mitotic chromosome dynamics. SMC1 and SMC3 form a heterodimeric complex required for metaphase progression in mitotic cells. Specifically this SMC1/SMC3 complex is responsible for sister chromatid cohesion during metaphase. A number of cellular factors interact with hSMC1/hSMC3 during cell cycle. The major population of hSMC1/hSMC3 is in a compex with hRAD21 forming the human cohesion complex. Human cohesion complex associates with chromosomes which peaks at S phase and dissociates from chromosomes during G2/M transition. In addition, a subpopulation of hSMC1/hSMC3 associates tightly with nuclear matrix and centrosomes during interphase. A subset of hSMC1/hSMC3 is localized to spindle poles, spindles and kinetochores during mitosis when cohesin is in the cytoplasm. hSMC1/hSMC3 is required for spindle aster formation in vitro and reacts with nuclear mitotic apparatus protein in vivo.

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Self-contained ductless enclosures allow safe handling of organic, formaldehyde, acid gas, sulphur compounds, or ammonia chemical fumes and vapours, as well as particulates. Air inside the enclosures passes through carbon filters, and in some cases additional HEPA particulate filters, before being safely exhausted back into the laboratory. No outside ducting is required.

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Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFC and VEGFD, and plays an essential role in adult lymphangiogenesis and in the development of the vascular network and the cardiovascular system during embryonic development. Promotes proliferation, survival and migration of endothelial cells, and regulates angiogenic sprouting. Signaling by activated FLT4 leads to enhanced production of VEGFC, and to a lesser degree VEGFA, thereby creating a positive feedback loop that enhances FLT4 signaling. Modulates KDR signaling by forming heterodimers. The secreted isoform 3 may function as a decoy receptor for VEGFC and/or VEGFD and play an important role as a negative regulator of VEGFC-mediated lymphangiogenesis and angiogenesis. Binding of vascular growth factors to isoform 1 or isoform 2 leads to the activation of several signaling cascades; isoform 2 seems to be less efficient in signal transduction, because it has a truncated C-terminus and therefore lacks several phosphorylation sites. Mediates activation of the MAPK1/ERK2, MAPK3/ERK1 signaling pathway, of MAPK8 and the JUN signaling pathway, and of the AKT1 signaling pathway. Phosphorylates SHC1. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Promotes phosphorylation of MAPK8 at 'Thr-183' and 'Tyr-185', and of AKT1 at 'Ser-473'.

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Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4-phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Participates in cellular signaling in response to various growth factors. Involved in the activation of AKT1 upon stimulation by receptor tyrosine kinases ligands such as EGF, insulin, IGF1, VEGFA and PDGF. Involved in signaling via insulin-receptor substrate (IRS) proteins. Essential in endothelial cell migration during vascular development through VEGFA signaling, possibly by regulating RhoA activity. Required for lymphatic vasculature development, possibly by binding to RAS and by activation by EGF and FGF2, but not by PDGF. Regulates invadopodia formation in breast cancer cells through the PDPK1-AKT1 pathway. Participates in cardiomyogenesis in embryonic stem cells through a AKT1 pathway. Participates in vasculogenesis in embryonic stem cells through PDK1 and protein kinase C pathway. Has also serine-protein kinase activity: phosphorylates PIK3R1 (p85alpha regulatory subunit), EIF4EBP1 and HRAS.

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Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding growth factor GAS6 and which is thus regulating many physiological processes including cell survival, cell proliferation, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of AXL. Following activation by ligand, ALX binds and induces tyrosine phosphorylation of PI3-kinase subunits PIK3R1, PIK3R2 and PIK3R3; but also GRB2, PLCG1, LCK and PTPN11. Other downstream substrate candidates for AXL are CBL, NCK2, SOCS1 and TENC1. Recruitment of GRB2 and phosphatidylinositol 3 kinase regulatory subunits by AXL leads to the downstream activation of the AKT kinase. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response. In case of filovirus infection, seems to function as a cell entry factor.

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ADH4, class II alcohol dehydrogenase 4 pi subunit, which is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. Class II alcohol dehydrogenase is a homodimer composed of 2 pi subunits. It exhibits a high activity for oxidation of long-chain aliphatic alcohols and aromatic alcohols and is less sensitive to pyrazole.This gene encodes class II alcohol dehydrogenase 4 pi subunit, which is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. Class II alcohol dehydrogenase is a homodimer composed of 2 pi subunits. It exhibits a high activity for oxidation of long-chain aliphatic alcohols and aromatic alcohols and is less sensitive to pyrazole. This gene is localized to chromosome 4 in the cluster of alcohol dehydrogenase genes.

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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.

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EDG8 is a receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. It Is coupled to both the G (i/0)alpha and G (12) subclass of heteromeric G-proteins (By similarity). It may play a regulatory role in the transformation of radial glial cells into astrocytes and may affect proliferative activity of these cells.The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme functions in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase. Two alternatively spliced transcript variants have been found for this gene and they encode distinct isoforms.

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The very-low-density-lipoprotein receptor (VLDL-R) is a lipoprotein receptor that shows considerable similarity to the lowdensity-lipoprotein receptor. VLDL R is a 130 kDa type I transmembrane protein in the LDL receptor family that plays a significant role in lipid metabolism and in nervous system development and function .This receptor has been suggested to be important for the metabolism of apoprotein-E-containing triacylglycerol-rich lipoproteins, such as very-low-densitylipoprotein (VLDL), beta-migrating VLDL and intermediate-density lipoprotein. It is also one of the receptors of reelin, an extracellular matrix protein which regulates the processes of neuronal migration and synaptic plasticity. In humans, the VLDL-R is encoded by the VLDLR gene.
A rare neurological disorder first described in the 1970s under the name "disequilibrium syndrome" is now considered to be caused by the disruption of VLDLR gene. The disorder was renamed VLDLR-associated cerebellar hypoplasia (VLDLRCH) after a 2005 study. It is associated with parental consanguinity and found in secluded communities such as the Hutterites. VLDLRCH is one of the two known genetic disorders caused by a disruption of reelin signaling pathway, along with Norman-Roberts syndrome.

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UPB1 is a protein that belongs to the CN hydrolase family. Beta-ureidopropionase catalyzes the last step in the pyrimidine degradation pathway. The pyrimidine bases uracil and thymine are degraded via the consecutive action of dihydropyrimidine dehydrogenase (DHPDH), dihydropyrimidinase (DHP) and beta-ureidopropionase (UP) to beta-alanine and beta-aminoisobutyric acid, respectively. UP deficiencies are associated with N-carbamyl-beta-amino aciduria and may lead to abnormalities in neurological activityThis gene encodes a protein that belongs to the CN hydrolase family. Beta-ureidopropionase catalyzes the last step in the pyrimidine degradation pathway. The pyrimidine bases uracil and thymine are degraded via the consecutive action of dihydropyrimidine dehydrogenase (DHPDH), dihydropyrimidinase (DHP) and beta-ureidopropionase (UP) to beta-alanine and beta-aminoisobutyric acid, respectively. UP deficiencies are associated with N-carbamyl-beta-amino aciduria and may lead to abnormalities in neurological activity.