54822 Results for: "Markery,+d\u0142ugopisy+i+grawery&pageNo=48"

Supplier: Abcam

Rabbit monoclonal [EPR23946-46] to NFAT2 - BSA and Azide free (Capture).

Supplier: Abcam

Rabbit monoclonal [EPR22651-46] to EEF1A2 - BSA and azide free.

Supplier: Abcam

Rabbit monoclonal [EPR23981-46] to Egr1 - BSA and Azide free.

Supplier: Abcam

Rabbit monoclonal [EPR24415-47] to TMEM175 - BSA and Azide free.

Supplier: Beckman Coulter

Optima™, SW 40 Ti swinging bucket rotor package, For: Ultracentrifugation

Supplier: Apollo Scientific

Dimethyl-1-(2-oxo-2-phenylethyl)-1H-1,2,3-triazole-4,5-dicarboxylate

Supplier: Apollo Scientific

tert-Butyl-4,4-dimethyl-2,2-dioxooxathiazolidine-3-carboxylate 95%

Supplier: Abcam

Rabbit monoclonal [EPR26025-45] to SNX17 - BSA and Azide free.

Supplier: Abcam

Rabbit monoclonal [EPR24487-40] to RAB35 - BSA and Azide free (Capture).

Supplier: Abcam

Rabbit monoclonal [EPR27470-43] to Angiogenin - BSA and Azide free.

Supplier: Bioss

This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-2 subunit is not known. Mediates cell adhesion of neurons and astrocytes, and promotes neurite outgrowth.

Supplier: Bioss

Receptor for interleukin-7. Also acts as a receptor for thymic stromal lymphopoietin (TSLP).

Supplier: Bioss

The peroxisomal membrane contains several ATP-binding cassette (ABC) transporters, ABCD1–4 that are known to be present in the human peroxisome membrane (1). All four proteins are ABC half-transporters, which dimerize to form an active transporter (1). A mutation in the ABCD1 causes X-linked adrenoleukodystrophy (X-ALD), a peroxisomal disorder which affects lipid storage (2,3). ABCD2 in mouse, is expressed at high levels in the brain and adrenal organs, which are adversely affected in X-ALD (4). The peroxisomal membrane comprises 2 quantitatively major proteins, PMP22 and ABCD3 (5). ABCD3 is associated with irregularly shaped vesicles which may be defective peroxisomes or peroxisome precursors (5). ABCD4 localizes to peroxisomes (1). The genes which encode ABCD1–4 map to human chromosome Xq28, 12q11-q12, 1p22-p21 and 14q24.3, respectively (3,6–8). ABCB7 is a half-transporter involved in the transport of heme from the mitochondria to the cytosol and maps to human chromosome Xq13.1-q13.3 (9).

Supplier: Bioss

A reciprocal translocation between chromosomes 22 and 9 produces the Philadelphia chromosome, which is often found in patients with chronic myelogenous leukemia. The chromosome 22 breakpoint for this translocation is located within the BCR gene. The translocation produces a fusion protein which is encoded by sequence from both BCR and ABL, the gene at the chromosome 9 breakpoint. Although the BCR-ABL fusion protein has been extensively studied, the function of the normal BCR gene product is not clear. The protein has serine/threonine kinase activity and is a GTPase-activating protein for p21rac. Two transcript variants encoding different isoforms have been found for this gene.

Supplier: Bioss

C9orf114 is a 376 amino acid protein encoded by a gene that maps to human chromosome 9q34.11. Chromosome 9 consists of about 145 million bases, represents 4% of the human genome and encodes nearly 900 genes. Thought to play a role in gender determination, deletion of the distal portion of 9p can lead to development of male to female sex reversal, the phenotype of a female with a male X,Y genotype. Hereditary hemorrhagic telangiectasia, which is characterized by harmful vascular defects, is associated with the chromosome 9 gene encoding endoglin protein, ENG. Familial dysautonomia is also associated with chromosome 9 though through the gene IKBKAP. Notably, chromosome 9 encompasses the largest interferon family gene cluster. Chromosome 9 is partnered with chromosome 22 in the translocation leading to the aberrant production of BCR-ABL fusion protein often found in leukemias.

Supplier: Bioss

Immunoglobulins belong to a group of related glyco proteins which make up 20% of serum proteins. Antigens and immunoglobulins react to confer immunity to individuals. Immunoglobulins have similar structures of two identical heavy chains and two identical light chains. Both the heavy chains and the light chains are divided into constant and variable regions. The constant regions have the same amino acid sequences between all the immunoglobulin classes. The variable regions have approximately 110 amino acids with high sequence variability. The amino acid sequence of the heavy chain determines the class of an immunoglobulin. The five types of immunoglobulin heavy chains are known as: IgG, IgA, IgM, IgD, and IgE. IgG is divided into four subclasses, and IgA is divided into two subclasses. In serum IgA and IgG are monomers with a single 4 polypeptide unit; while, IgM is a pen tamer. IgA may also form polymers. Kappa light chain antibody can be used for the identification of leukemias, plasmacytomas and certain non Hodgkin's lymphomas. Kappa light chain contains one immunoglobulin like domain. The EU sequence has the INV allotypic marker, Ala 45 and Val 83. The ROY sequence has the INV allotypic marker, Ala 45 and Leu 83.

Supplier: Bioss

Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA.

Supplier: Bioss

The protein encoded by this gene is 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. The protein localizes to cytoplasmic bodies. Its function has not been identified. Alternative splicing of this gene generates three transcript variants, named alpha, beta and gamma.

Supplier: Bioss

May activate transcription by interacting directly with the X-box.

Supplier: Bioss

The HUNK (hormonally upregulated Neu-associated kinase) protein, also designated MAK-V in mouse, has been identified as a novel SNF1-related serine/threonine kinase. The human HUNK gene localizes to chromosome 21q22 and encodes a protein with nucleocytoplasmic distribution and localizes to the centrosome. Overexpression of the HUNK protein associates with approximately 50% of breast carcinomas, and may provide diagnostic-prognostic value as a molecular marker. Serine/threonine-protein kinase SNF1-like kinase 2 (SIK) phosphorylates Ser-794 of IRS1 in insulin-stimulated adipocytes, which may modulate the efficiency of insulin signal transduction. SIK is activated by phosphorylation on Thr-175 by STK11 in complex with STE20-related adapter-α and CAB39.

Supplier: Bioss

This gene 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 protein localizes to the endoplasmic reticulum and hydroxylates medium-chain fatty acids such as laurate and myristate. [provided by RefSeq, Jul 2008].

Supplier: Bioss

Gamma-glutamyltranspeptidase (GGT) acts as a glutathionase and catalyzes the transfer of the glutamyl moiety of glutathione to a variety of amino acids and dipeptide acceptors. This enzyme is located on the outer surface of the cell membrane and is widely distributed in mammalian tissues involved in absorption and secretion. In humans, hepatic GGT activity is elevated in some liver diseases. GGT1 is released into the bloodstream after liver damage, and an elevated level of the enzyme may be a useful early sign of hepatocellular carcinoma. GGT5 converts leukotriene C4 to leukotriene D4; it does not, however, convert synthetic substrates that are commonly used to assay GGT. In human serum and in human tissues, there is a marked heterogeneity in GGT, but this heterogeneity can be attributed to different glycosylation of the same peptide rather than to the products of different genes. Belonging to the gamma-glutamyltranspeptidase family, GGT6 (gamma-glutamyltransferase 6), is a 493 amino acid single-pass type II membrane protein that cleaves glutathione conjugates. GGT6 exists as two alternatively spliced isoforms.

Supplier: Bioss

GMEB-2 is a DNA-binding protein that plays a crucial role modulating transcription upon activation by steroid hormones. GMEB-2 is ubiquitously expressed with preferential expression in developmentally important tissues, such as testis, bone marrow, placenta and fetal tissues. It localizes to the nucleus and cytoplasm and contains a SAND domain near its N-terminus and a C-terminal coiled coil structure. GMEB-2 functions as a homodimer or as a heterodimer with GMEB-1. The formed complex specifically binds to glucocorticoid modulatory elements (GME) in the promoter region of target genes and recruits the histone acetylase CREB binding protein (CBP) during glucocorticoid signaling. This acts to increase sensitivity to low concentrations of glucocorticoids. In addition, GMEB-2 functions as an auxiliary factor required for parvovirus replication.

Supplier: Bioss

This gene encodes an enzyme that catalyzes the irreversible and NADPH-dependent reductive deamination of GMP to IMP. The protein also functions in the re-utilization of free intracellular bases and purine nucleosides.[provided by RefSeq, Oct 2009].

Supplier: Bioss

Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis.

Supplier: Bioss

G protein-coupled receptors (GPRs), also known as seven transmembrane receptors, heptahelical receptors or 7TM receptors, comprise a superfamily of proteins that play a role in many different stimulus-response pathways. G protein coupled receptors translate extracellular signals into intracellular signals (G protein activation) and they respond to a variety of signaling molecules, such as hormones and neurotransmitters. GPR101 (G protein-coupled receptor 101), also known as GPCR6, is a 508 amino acid multi-pass membrane protein that belongs to the G-protein coupled receptor 1 family. GPR101 functions as an orphan receptor that is thought to play a role in signaling events throughout the cell. Expressed predominantly in brain, GPR101 participates in a wide range of activities in the CNS via modulation of cAMP levels.

Supplier: Bioss

Betacellulin (BTC), a member of the epidermal growth factor (EGF) family, was originally identified as a growth-promoting factor in the conditioned medium of a mouse pancreatic-cell carcinoma (insulinoma) cell line and has since been identified in humans. BTC is synthesized as a large transmembrane precursor molecule that can be cleaved proteolytically to release the soluble form of BTC or function as membrane-anchored growth factors in juxtacrine signaling. BTC, in addition to stimulating homodimers of ErbB-1 and ErbB-4, is capable of binding and activating all possible combinations of heterodimeric ErbB receptors including the oncogenic ErbB-2/ErbB-3 complex. BTC is also expressed in some human malignancies and may have an important role in tumor growth progression.

Supplier: Bioss

Antiapoptotic factor that may have a role in protein assembly. Negatively regulates ACIN1. By binding to ACIN1, it suppresses ACIN1 cleavage from CASP3 and ACIN1-mediated DNA fragmentation. Also known to efficiently suppress E2F1-induced apoptosis. Its depletion enhances the cytotoxic action of the chemotherapeutic drugs.

Supplier: Bioss

NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage. Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity inducing injurious Ca2+ influx through them, resulting in an irreversible neuronal death (By similarity).

Supplier: Bioss

Phakinin is a membrane-associated and cytoskeletal intermediate filament (IF) protein specific to the eye lens. IFs are cytoskeletal structures that typically contain a head, rod and tail domain. Unlike most IFs, Phakinin completely lacks the C-terminal tail domain thus contributing to the unique structure of the beaded filament that is specific to the lens. Phakinin is required for the assembly of beaded filaments and cytoskeletal networks that are important for the long-term maintenance of optical properties and transparency of the lens. Phakinin copolymerizes with Filensin, another IF protein, to form the 10-nm filamentous structures of the beaded filaments. Phakinin is also capable of self-assembling into filament-like structures that form thicker bundles. Mutations in the gene encoding Phakinin can result in lens cataract.