118494 Results for: "Szufelki+do+pr\u00F3bek&pageNo=30"

Supplier: Bioss

C1orf220

Supplier: Bioss

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.

Supplier: Bioss

vars2

Supplier: Bioss

The protein encoded by this gene can polymerize and depolymerize F-actin and G-actin in a pH-dependent manner. Increased phosphorylation of this protein by LIM kinase aids in Rho-induced reorganization of the actin cytoskeleton. Cofilin is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. It is involved in the translocation of actin-cofilin complex from cytoplasm to nucleus.

Supplier: Bioss

Transcriptional regulator. Recognizes and binds to the DNA sequence 5'-CGCCCCCGC-3'(EGR-site). Activates the transcription of target genes whose products are required for mitogenesis and differentiation.

Supplier: Bioss

SRRM3

Supplier: Bioss

UQCRC2 is a component of the ubiquinol cytochrome c reductase complex (complex III), which is part of the mitochondrial respiratory chain. The core protein 2 is required for the assembly of the complex.

Supplier: Bioss

Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis.

Supplier: Bioss

G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling inhibits adenylate cyclase activity and activates a phosphatidylinositol-calcium second messenger system that regulates the release of Ca(2+) ions from intracellular stores. Plays a role in the regulation of 5-hydroxytryptamine release and in the regulation of dopamine and 5-hydroxytryptamine metabolism. Plays a role in the regulation of dopamine and 5-hydroxytryptamine levels in the brain, and thereby affects neural activity, mood and behavior. Plays a role in the response to anxiogenic stimuli.

Supplier: Bioss

AML1/Runx1 binds DNA as a monomer and through the Runt domain. DNA binding is increased by heterodimerization with CBFB. Isoform AML1L can neither bind DNA nor heterodimerize and interferes with the transactivation activity of AML1/Runx1. CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T cell receptor enhancers, LCK, IL3 and GMCSF promoters. The alpha subunit binds DNA and appears to have a role in the development of normal hematopoiesis. AML1/Runx1 is expressed in a wide variety of tissues and is expressed at the highest levels in thymus, bone marrow and peripheral blood. Defects in AML1/Runx1 are the cause of familial platelet disorder with associated myeloid malignancy, an autosomal dominant disease characterized by qualitative and quantitative platelet defects, and propensity to develop acute myelogenous leukemia.

Supplier: Bioss

Headpin is a skin-specific, UV-repressible serine proteinase inhibitor (serpin) belonging to the ovalbumin serpin family. Headpin is abundant in the human keratinocyte cell line HaCaT, and in lesional keratinocytes from psoriatic skin. Headpin downregulation occurs in squamous cell carcinoma of the oral cavity and in squamous cell carcinoma cell lines of the head and neck.

Supplier: Bioss

Band 3, also designated AE1, is an erythrocyte membrane glycoprotein that contributes to cell stuctural integrity and mediates exchange of chloride and bicarbonate across the phospholipid bilayer. The diverse functions of the approximately 900 amino acid protein are mediated by two distinct domains. The amino terminal domain, also known as cdb3 for cytoplasmic domain of erthrocyte membrane band 3, acts as an attachment site for the erythrocyte skeleton by binding ankyrin. The carboxy-terminal, membrane-associated domain carries out exchange transport of anions. Degradation of band 3 can generate an aging antigen known as senescent cell antigen, or SCA, which is expressed on old cells and marks them for removal by the immune system. An isoform of band 3, which lacks the first 65 amino acids and does not bind ankryin, is expressed in kidney.

Supplier: Bioss

This gene is an ortholog of the Drosophila fat gene, which encodes a tumor suppressor essential for controlling cell proliferation during Drosophila development. The gene product is a member of the cadherin superfamily, a group of integral membrane proteins characterized by the presence of cadherin-type repeats. In addition to containing 34 tandem cadherin-type repeats, the gene product has five epidermal growth factor (EGF)-like repeats and one laminin A-G domain. This gene is expressed at high levels in a number of fetal epithelia. Its product probably functions as an adhesion molecule and/or signaling receptor, and is likely to be important in developmental processes and cell communication. Transcript variants derived from alternative splicing and/or alternative promoter usage exist, but they have not been fully described. [provided by RefSeq].

Supplier: Bioss

Myotubularin and the myotubularin-related proteins (MTMR1-9) belong to a highly conserved family of eukaryotic phosphatases. They are protein tyrosine phosphatases that utilize inositol phospholipids, rather than phosphoproteins, as substrates. MTMR family members hydrolyze both Phosphatidylinositol 3-phosphate (PtdIns3P) and PtdIns(3,5)P2. MTMR2 interacts with MTMR5, an inactive family member that increases the enzymatic activity of MTMR2 and dictates its subcellular localization. Mutations in MTMR2 cause autosomal recessive Charcot-Marie-Tooth type 4B1 (CMT4B1), which is characterized by reduced nerve conduction velocities, focally folded myelin sheaths and demyelination. MTMR3 and MTMR4 can either interact with each other or self associate. MTMR6 regulates the activity of the calcium-activated potassium channel 3.1. MTMR9 regulates the activity of MTMR7 and MTMR8.

Supplier: Bioss

Involved in intracellular protein transport probably out of a prevacuolar endosomal compartment. May be involved in the release of components of the bilayered coat from the endosomal membrane. The association with ESCRT-III complex mediates the ATP-dependent disassembly of the ESCRT-III complex. In case of infection, the HIV-1 virus takes advantage of it for budding and exocytic cargos of viral proteins.

Supplier: Bioss

SHROOM1 is an 852 amino acid protein that contains one ASD1 domain and one ASD2 domain. Localized to both the cytoplasm and the cytoskeleton, SHROOM1 interacts with Actin and is thought to be involved in microtubule assembly during cell elongation, possibly playing a role in the development of the nervous system. Multiple isoforms of SHROOM1 exist due to alternative splicing events. The gene encoding SHROOM1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.

Supplier: Bioss

CIB1(Calcium and integrin binding 1) may convert the inactive conformation of integrin alpha-IIb/beta3 to an active form through the binding to the integrin cytoplasmic domain.

Supplier: Bioss

The PHEX a 749 amino acid protein that putatively consists of an intracellular, transmembrane and extracellular domain. PHEX mutations have been observed in 60-80% of hypophosphatemic rickets patients. The PHEX protein, which is a single-pass membrane protein, is also designated HYP, X-linked hypophosphatemia protein or metalloendopeptidase homolog PEX. PHEX plays an active role in bone and dentin mineralization and renal phosphate re-absorption. X-linked hypophosphatemic rickets, also designated HYP, is an X-linked dominant disorder characterized by impaired phosphate uptake in the kidney, which is likely to be caused by abnormal regulation of sodium phosphate cotransport in the proximal tubules. Clinical manifestations include skeletal deformities, growth failure, craniosynostosis, paravertebral calcifications, pseudofractures in lower extremities, and muscular hypotonia with onset in early childhood.

Supplier: Bioss

LPP (LIM containing lipoma preferred partner), is a scaffolding protein which contains three LIM domains at its carboxy terminus, preceded by a proline rich pre LIM region containing a number of protein interaction domains. LPP localizes to sites of cell adhesion, such as focal adhesions and cell-cell contacts and may be involved in cell-cell adhesion and cell motility. LPP also shuttles through the nucleus and may function as a transcriptional co-activator. The human LPP gene maps to chromosomal location 3q28, and preferentially translocates to the HMGIC gene in a subclass of human benign mesenchymal tumors known as lipomas. Alternate splicing results in multiple transcript variants.

Supplier: Bioss

Receptor for the cytotoxic ligand TRAIL. Contains a truncated death domain and hence is not capable of inducing apoptosis but protects against TRAIL-mediated apoptosis. Reports are contradictory with regards to its ability to induce the NF-kappa-B pathway. According to PubMed:9382840, it cannot but according to PubMed:9430226, it can induce the NF-kappa-B pathway.

Supplier: Bioss

Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS beta which binds to DNA mismatches thereby initiating DNA repair. When bound, the MutS beta heterodimer bends the DNA helix and shields approximately 20 base pairs. MutS beta recognizes large insertion-deletion loops (IDL) up to 13 nucleotides long. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis.

Supplier: Bioss

The protein encoded by this gene is the predominant constituent of the crystalline core of the eosinophil granule. High levels of the proform of this protein are also present in placenta and pregnancy serum, where it exists as a complex with several other proteins including pregnancy-associated plasma protein A (PAPPA), angiotensinogen (AGT), and C3dg. This protein may be involved in antiparasitic defense mechanisms as a cytotoxin and helminthotoxin, and in immune hypersensitivity reactions. It is directly implicated in epithelial cell damage, exfoliation, and bronchospasm in allergic diseases. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2011].

Supplier: Bioss

CAB39L

Supplier: Bioss

Hox, Pbx and Meis families of transcription factors form heteromeric complexes and bind DNA through specific homeobox domains. Hox proteins are involved in regulating tissue patterning during development, and are also expressed in lineage- and stage-specific patterns during adult hematopoietic differentiation and in leukemias. The Hox proteins, which include paralog groups 1-10, have a low intrinsic binding affinity for DNA and are instead associated into cooperative DNA binding complexes with Pbx or the Pbx- related Meis proteins, which result in an enhanced Hox-DNA binding affinity and an increased selectivity for the binding site. Both Meis1 and Meis2 (also known as Meis-related gene 1 or Mrg1) are members of the TALE (“three amino acid loop extension”) family of homeodomain-containing proteins. In addition to binding with Hox proteins, Meis1 also forms heterodimers with the ubiquitously expressed Pbx proteins, including Pbx1, Pbx2 and Pbx3, and these complexes contain distinct DNA-binding specificities. Like Hox and Pbx proteins, Meis1 is implicated in oncogenesis, as it is overexpressed as a result of adjacent retroviral insertion in BHX-2 myeloid leukemias. Two Meis-related proteins, Meis2 and Meis3 (also designated Mrg1 and Mrg2, respectively), possess largely similar sequence identity with Meis1 and are expressed in normal tissues and myeloid leukemias. In the pancreas, Meis2 preferentially associates with Pbx1, and together they associate with the pancreas-specific homeodomain factor, Pdx1, to repress Pdx1-induced transcriptional activation.

Supplier: Bioss

p53 binding protein 1 (53BP1) plays a critical role in tumor suppression and is a putative substrate of ATM kinase. Upon DNA damage, it is phosphorylated and relocalizes to the presumptive sites of damage, p53 binding protein 1 (53BP1) plays a critical role in tumor suppression and is a putative substrate of ATM kinase. Upon DNA damage, it is phosphorylated and relocalizes to the presumptive sites of damage, specifically, double strand breaks. This also suggests a role in DNA repair, maintaining genomic stability.

Supplier: Thermo Fisher Scientific

Iridium ≥99.8% (metals basis), wire, Ø 1.0 mm (0.04 in)

Supplier: Abcam

Mouse monoclonal [LH2] to Cytokeratin 10.

Supplier: Abcam

Rat monoclonal [M4I-10] to MRP4.

Supplier: Biotium

5-Aminoallyl-UTP can be enzymatically incorporated into RNA for subsequent labeling with an amine-reactive fluorescent dye, biotin, or other hapten.

Supplier: Thermo Fisher Scientific

Niobium ≥99.8% (metals basis), wire, Ø 1.0 mm (0.04 in)