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Showing 1-30 of 38 results for "P9120" within Papers
Anuradha Gosain et al.
Indian journal of experimental biology, 52(3), 197-206 (2014-03-29)
Peptide: N-glycanase (PNGase) enzyme is found throughout eukaryotes and plays an important role in the misfolded glycoprotein degradation pathway. This communication reports the expression patterns of the pngase transcript (as studied by the analysis of beta-galactosidase reporter driven by the
Yukiko Kamiya et al.
FEBS letters, 586(8), 1141-1146 (2012-05-12)
PUB domains are identified in several proteins functioning in the ubiquitin (Ub)-proteasome system and considered as p97-binding modules. To address the further functional roles of these domains, we herein characterized the interactions of the PUB domain of peptide:N-glycanase (PNGase) with
Anuradha Gosain et al.
BMC biochemistry, 13, 9-9 (2012-06-12)
Peptide: N- glycanase (PNGase) enzyme cleaves oligosaccharides from the misfolded glycoproteins and prepares them for degradation. This enzyme plays a role in the endoplasmic reticulum associated degradation (ERAD) pathway in yeast and mice but its biological importance and role in
Reynald Tremblay et al.
Transgenic research, 20(2), 345-356 (2010-06-19)
Soybean agglutinin (SBA) is a specific N-acetylgalactosamine-binding plant lectin that can agglutinate a wide variety of cells. SBA has great potential for medical and biotechnology-focused applications, including screening and treatment of breast cancer, isolation of fetal cells from maternal blood
John E Bradley et al.
Laboratory investigation; a journal of technical methods and pathology, 93(3), 365-374 (2013-01-30)
Thymocyte differentiation antigen-1 (Thy-1) is a glycosylphosphatidylinositol (GPI)-linked cell surface glycoprotein expressed on numerous cell types, which regulates signals affecting cell adhesion, migration, differentiation, and survival. In addition, Thy-1 has been detected in the serum, cerebral spinal fluid, wound fluid
Anja Lux et al.
Journal of immunology (Baltimore, Md. : 1950), 190(8), 4315-4323 (2013-03-20)
IgG molecules are widely used as therapeutic agents either in the form of intact Abs or as Fc fusion proteins. Although efficient binding of the IgG Fc fragment to cellular FcγRs may be essential to achieve a high cytolytic activity
Hui Zhou et al.
Analytical biochemistry, 427(1), 33-35 (2012-04-21)
Common de-N-glycosylation protocols usually require a lengthy incubation time. Although pressure cycling technology or scientific microwave reactors can accelerate this enzyme reaction, they may not be easily accessible. In this brief report, we employed an alternative strategy using a standard
N Takahashi et al.
Journal of biochemistry, 84(6), 1467-1473 (1978-12-01)
A new type of glycopeptidase hydrolyzing beta-aspartylglycosylamine linkages was partially purified from almond emulsin by chromatography on Sephadex G-200 and DE 52. The enzyme degraded stem bromelain glycopeptide, Asn-Asn(Man3,Xyl1,Fuc1,GlcNAc2)-Glu-Ser-Ser, to yield equimolar amounts of intact oligosaccharide, peptide (Asn-Asp-Glu-Ser-Ser), and ammonia.
Helle Malerod et al.
Journal of proteome research, 12(1), 248-259 (2012-12-05)
The adenocarcinoma cell line HeLa serves as a model system for cancer research in general and cervical cancer in particular. In this study, hydrazide enrichment in combination with state-of-the art nanoLC-MS/MS analysis was used to profile N-linked glycosites in HeLa
Peihan Orestes et al.
Diabetes, 62(11), 3828-3838 (2013-07-10)
It has been established that Ca(V)3.2 T-type voltage-gated calcium channels (T-channels) play a key role in the sensitized (hyperexcitable) state of nociceptive sensory neurons (nociceptors) in response to hyperglycemia associated with diabetes, which in turn can be a basis for
Samnang Tep et al.
Biotechnology and bioengineering, 109(12), 3007-3017 (2012-07-04)
Within the biotechnology industry there is a continuous drive to better and more fully understand the biopharmaceutical process in order to achieve better process control. A method to monitor and quantitate glycomic changes that occur in CHO cells during a
Dolores Linde et al.
Bioresource technology, 109, 123-130 (2012-02-03)
The extracellular β-fructofuranosidase Xd-INV from the yeast Xanthophyllomyces dendrorhous mainly synthesizes the neo-fructooligosaccharides (neo-FOS) neokestose and neonystose. This enzyme is a glycoprotein with a content of 59-67% N-linked carbohydrates and an estimated molecular mass of 160-200 kDa. The extent level
Shengjun Wang et al.
Enzyme and microbial technology, 51(3), 139-142 (2012-07-05)
In many cases, it is desirable to maintain the native status of the target glycoproteins when they are deglycosylated. However, most conventional deglycosylation process often causes the irreversible denaturation of the target glycoproteins. In the present study, we developed a
Teresa R McCurdy et al.
Journal of biomedicine & biotechnology, 2012, 292730-292730 (2012-05-01)
Alpha-1 acid glycoprotein (AGP) is a highly glycosylated plasma protein that exerts vasoprotective effects. We hypothesized that AGP's N-linked glycans govern its rate of clearance from the circulation, and followed the disappearance of different forms of radiolabeled human AGP from
Yashu Liu et al.
Methods in molecular biology (Clifton, N.J.), 951, 69-77 (2013-01-09)
Membrane-associated glycoproteins play critical roles in many biological processes and are often the therapeutic targets for drug discovery. Lectin affinity chromatography is one of the most widely used approaches for enrichment of glycoproteins at the protein level. Here, we describe
Charles C Nwosu et al.
Journal of proteome research, 11(5), 2912-2924 (2012-03-24)
The isolation of whey proteins from human and bovine milks followed by profiling of their entire N-glycan repertoire is described. Whey proteins resulting from centrifugation and ethanol precipitation of milk were treated with PNGase F to release protein-bound N-glycans. Once
Hiroyuki Yoshida et al.
FEBS letters, 588(1), 111-116 (2013-11-26)
Recently, we disclosed that KIAA1199-mediated hyaluronan (HA) depolymerization requires an acidic cellular microenvironment (e.g. clathrin-coated vesicles or early endosomes), but no information about the structural basis underlying the cellular targeting and functional modification of KIAA1199 was available. Here, we show
Thomas C Nesspor et al.
Journal of molecular recognition : JMR, 25(3), 147-154 (2012-03-13)
Immunoglobulin G (IgG) antibodies are an integral part of the adaptive immune response that provide a direct link between humoral and cellular components of the immune system. Insights into relationships between the structure and function of human IgGs have prompted
PrPc activation induces neurite outgrowth and differentiation in PC12 cells: role for caveolin-1 in the signal transduction pathway
Pantera B, et al.
Journal of Neurochemistry, 110(1), 194-207 (2009)
Anna C Need et al.
Journal of medical genetics, 49(6), 353-361 (2012-05-15)
There is considerable interest in the use of next-generation sequencing to help diagnose unidentified genetic conditions, but it is difficult to predict the success rate in a clinical setting that includes patients with a broad range of phenotypic presentations. The
Zhaohai Zhang et al.
The international journal of biochemistry & cell biology, 44(8), 1244-1253 (2012-05-15)
Correlations of disease phenotypes with glycosylation changes have been analyzed intensively in tumor biology field. In this study we describe glycomic alterations of multidrug resistance in human leukemia cell lines. Using multiple glycan profiling tools: real-time PCR for quantification of
Nicholas A Veldhuis et al.
The Journal of biological chemistry, 287(26), 21765-21772 (2012-05-10)
The balance of glycosylation and deglycosylation of ion channels can markedly influence their function and regulation. However, the functional importance of glycosylation of the TRPV1 receptor, a key sensor of pain-sensing nerves, is not well understood, and whether TRPV1 is
Yu-Chen Lee et al.
Methods in molecular biology (Clifton, N.J.), 909, 29-41 (2012-08-21)
Isolation of highly purified plasma membranes is the key step in constructing the plasma membrane proteome. Traditional plasma membrane isolation method takes advantage of the differential density of organelles. While differential centrifugation methods are sufficient to enrich for plasma membranes
Pia H Jensen et al.
Nature protocols, 7(7), 1299-1310 (2012-06-09)
This protocol shows how to obtain a detailed glycan compositional and structural profile from purified glycoproteins or protein mixtures, and it can be used to distinguish different isobaric glycan isomers. Glycoproteins are immobilized on PVDF membranes before the N-glycans are
Ulla-Maja Bailey et al.
Journal of proteome research, 11(11), 5376-5383 (2012-10-09)
Asparagine-linked glycosylation is a common post-translational modification of proteins in eukaryotes. Mutations in the human ALG3 gene cause changed levels and altered glycan structures on mature glycoproteins and are the cause of a severe congenital disorder of glycosylation (CDG-Id). Diverse
Tarlan Mamedov et al.
Bioengineered, 4(5), 338-342 (2013-01-19)
At present, several eukaryotic expression systems including yeast, insect and mammalian cells and plants are used for the production of recombinant proteins. Proteins with potential N-glycosylation sites are efficiently glycosylated when expressed in these systems. However, the ability of the
Hiroyuki Kaji et al.
Methods in molecular biology (Clifton, N.J.), 951, 217-227 (2013-01-09)
Protein glycosylation is one of the most common and crucial post-translational modifications that regulates many biological processes. Because abnormal glycosylation is also associated with various pathologies, including cancer, and inflammatory and degenerative diseases, technology for comprehensive analysis of glycoproteins, or
T H Plummer et al.
The Journal of biological chemistry, 256(20), 10243-10246 (1981-10-25)
Almond emulsin peptide:N-glycosidase has been partially purified by using a new 3H-labeled 5-dimethylaminonaphthalene-1-sulfonyl-octaglycopeptide substrate derived from ovalbumin. The enzyme hydrolyzes the beta-aspartylglycosylamine linkage of both high mannose and biantennary complex glycopeptides, as shown by the isolation of the corresponding carbohydrate-free
Demonstration of a new amidase acting on glycopeptides.
N Takahashi
Biochemical and biophysical research communications, 76(4), 1194-1201 (1977-06-20)
G E Norris et al.
Structure (London, England : 1993), 2(11), 1049-1059 (1994-11-15)
Peptide:N-glycosidase F (PNGase F) is an enzyme that catalyzes the complete removal of N-linked oligosaccharide chains from glycoproteins. Often called an endoglycosidase, it is more correctly termed an amidase or glycosylasparaginase as cleavage is at the asparagine-sugar amide linkage. The
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