123590 Results for: "3+ml+k2edta"

Supplier: Promega Corporation

PureYield Plasmid Midiprep System provides a fast method for isolating transfection-quality plasmid DNA. Yields 100-200ug of plasmid DNA from 50ml bacteria culture.

Supplier: MP Biomedicals

MPure Bacterial DNA Extraction Kit is used with the MPure-12 Nucleic Acid Purification System for extraction and purification of genomic DNA from both Gram-positive and Gram-negative bacteria.

Supplier: Restek

Contains: 30439: 502.2 Calibration Mix #1 (gases); Bromomethane (methyl bromide) (74-83-9); Chloroethane (ethyl chloride) (75-00-3); Chloromethane (methyl chloride) (74-87-3); Dichlorodifluoromethane (CFC-12) (75-71-8); Trichlorofluoromethane (CFC-11) (75-69-4); Vinyl chloride (75-01-4);30432: 502.2 MegaMix Standard; Benzene (71-43-2); Bromobenzene (108-86-1); Bromochloromethane (74-97-5); Bromodichloromethane (75-27-4); Bromoform (75-25-2); n-Butylbenzene (104-51-8); sec-Butylbenzene (135-98-8); tert-Butylbenzene (98-06-6); Carbon tetrachloride (56-23-5); Chlorobenzene (108-90-7); Chloroform (67-66-3); 2-Chlorotoluene (95-49-8); 4-Chlorotoluene (106-43-4); Dibromochloromethane (124-48-1); 1,2-Dibromo-3-chloropropane (DBCP) (96-12-8); 1,2-Dibromoethane (EDB) (106-93-4); Dibromomethane (74-95-3); 1,2-Dichlorobenzene (95-50-1); 1,3-Dichlorobenzene (541-73-1); 1,4-Dichlorobenzene (106-46-7); 1,1-Dichloroethane (75-34-3); 1,2-Dichloroethane (107-06-2); 1,1-Dichloroethene (75-35-4); cis-1,2-Dichloroethene (156-59-2); trans-1,2-Dichloroethene (156-60-5); 1,2-Dichloropropane (78-87-5); 1,3-Dichloropropane (142-28-9); 2,2-Dichloropropane (594-20-7); 1,1-Dichloropropene (563-58-6); cis-1,3-Dichloropropene (10061-01-5); trans-1,3-Dichloropropene (10061-02-6); Ethylbenzene (100-41-4); Hexachloro-1,3-butadiene (hexachlorobutadiene) (87-68-3); Isopropylbenzene (cumene) (98-82-8); 4-Isopropyltoluene (p-cymene) (99-87-6); Methylene chloride (dichloromethane) (75-09-2); Naphthalene (91-20-3); n-Propylbenzene (103-65-1); Styrene (100-42-5); 1,1,1,2-Tetrachloroethane (630-20-6); 1,1,2,2-Tetrachloroethane (79-34-5); Tetrachloroethene (127-18-4); Toluene (108-88-3); 1,2,3-Trichlorobenzene (87-61-6); 1,2,4-Trichlorobenzene (120-82-1); 1,1,1-Trichloroethane (71-55-6); 1,1,2-Trichloroethane (79-00-5); Trichloroethene (79-01-6); 1,2,3-Trichloropropane (96-18-4); 1,2,4-Trimethylbenzene (95-63-6); 1,3,5-Trimethylbenzene (108-67-8); m-Xylene (108-38-3); o-Xylene (95-47-6); p-Xylene (106-42-3)

Supplier: SPEX CERTIPREP LLC

CLP Standards for ICP & ICP-MS
Our Contract Laboratory Program (CLP) standards allow you to Calibrate with Confidence®. The standards are to be used in conjunction with the Statement of Work for Inorganic Analysis; Multi-Media/Multi-Concentration Document Number ILM 05.3/ISM 01.2.

The final ICP check, performed in our own laboratories, is your stamp of assurance. We calibrate our instruments with traceable reference materials and show you the actual found value of the solution you receive, not just an ideal, calculated number as so many other standards manufacturers do. The combination of elements, concentrations and matrices listed have been diagnosed by SPEX CertiPrep for convenience of use and stability.

US EPA SOW ILM 05.3/ISM 01.2 gives specific procedures for the methods of analysis, target elements, and concentrationlevels. Standards are specified not only by the elements present and their relative concentrations, but also the order and frequency of running standards, blanks and samples. Details of these specifications may be found in the US EPA SOW ILM 05.3/ISM 01.2 in the following sections:

• Exhibit C, Inorganic Target Analyte List (TAL)
• Exhibit D, Analytical Methods
• Exhibit E, QA/QC Requirements

Initial Calibration Verification for CLP Methods
The US EPA retains analytical services through the Contract Laboratory Program (CLP). The CLP follows detailed SOPs derived from EPA methods. The CLP methods require calibration of analytical instrumentation whithin the expected quantitative range (ICAL standards) and additional CLP QA standards (ICV standards) to verify the calibration curve at each of the selected wavelengths that wil be used for sample analysis.

Our verification standards contain all of the elements on the TAL list and are independent standards for testing an instruments calibration curve. SPEX CertiPrep's ICV standards are designed to be used with their corresponding instrument calibration standards (ICAL).

We recommend dilution of ICV standards to a range within your instruments calibration curve. A dilution of 20-fold is recommended.

Supplier: Promega Corporation

The PureYield RNA Midiprep System isolates intact, pure total RNA from essentially any sample type for use in a wide range of applications.

Supplier: Restek

Contains: 30042: 502.2 Calibration Mix #1 (gases); Bromomethane (methyl bromide) (74-83-9); Chloroethane (ethyl chloride) (75-00-3); Chloromethane (methyl chloride) (74-87-3); Dichlorodifluoromethane (CFC-12) (75-71-8); Trichlorofluoromethane (CFC-11) (75-69-4); Vinyl chloride (75-01-4);30431: 502.2 MegaMix Standard; Benzene (71-43-2); Bromobenzene (108-86-1); Bromochloromethane (74-97-5); Bromodichloromethane (75-27-4); Bromoform (75-25-2); n-Butylbenzene (104-51-8); sec-Butylbenzene (135-98-8); tert-Butylbenzene (98-06-6); Carbon tetrachloride (56-23-5); Chlorobenzene (108-90-7); Chloroform (67-66-3); 2-Chlorotoluene (95-49-8); 4-Chlorotoluene (106-43-4); Dibromochloromethane (124-48-1); 1,2-Dibromo-3-chloropropane (DBCP) (96-12-8); 1,2-Dibromoethane (EDB) (106-93-4); Dibromomethane (74-95-3); 1,2-Dichlorobenzene (95-50-1); 1,3-Dichlorobenzene (541-73-1); 1,4-Dichlorobenzene (106-46-7); 1,1-Dichloroethane (75-34-3); 1,2-Dichloroethane (107-06-2); 1,1-Dichloroethene (75-35-4); cis-1,2-Dichloroethene (156-59-2); trans-1,2-Dichloroethene (156-60-5); 1,2-Dichloropropane (78-87-5); 1,3-Dichloropropane (142-28-9); 2,2-Dichloropropane (594-20-7); 1,1-Dichloropropene (563-58-6); cis-1,3-Dichloropropene (10061-01-5); trans-1,3-Dichloropropene (10061-02-6); Ethylbenzene (100-41-4); Hexachloro-1,3-butadiene (hexachlorobutadiene) (87-68-3); Isopropylbenzene (cumene) (98-82-8); 4-Isopropyltoluene (p-cymene) (99-87-6); Methylene chloride (dichloromethane) (75-09-2); Naphthalene (91-20-3); n-Propylbenzene (103-65-1); Styrene (100-42-5); 1,1,1,2-Tetrachloroethane (630-20-6); 1,1,2,2-Tetrachloroethane (79-34-5); Tetrachloroethene (127-18-4); Toluene (108-88-3); 1,2,3-Trichlorobenzene (87-61-6); 1,2,4-Trichlorobenzene (120-82-1); 1,1,1-Trichloroethane (71-55-6); 1,1,2-Trichloroethane (79-00-5); Trichloroethene (79-01-6); 1,2,3-Trichloropropane (96-18-4); 1,2,4-Trimethylbenzene (95-63-6); 1,3,5-Trimethylbenzene (108-67-8); m-Xylene (108-38-3); o-Xylene (95-47-6); p-Xylene (106-42-3)

Supplier: MP Biomedicals

Peroxidase-conjugated goat IgG fraction to human IgG Fc is the lyophilized powder of horseradish peroxidase (HRP)-conjugated goat IgG fraction to human IgG Fc and buffer salts.

Anti-Human secondary antibodies are affinity-purified antibodies with well-characterized specificity for human immunoglobulins and are useful in the detection, sorting or purification of its specified target. Secondary antibodies offer increased versatility enabling users to use many detection systems (e.g. HRP, AP, fluorescence). They can also provide greater sensitivity through signal amplification as multiple secondary antibodies can bind to a single primary antibody. Most commonly, secondary antibodies are generated by immunizing the host animal with a pooled population of immunoglobulins from the target species and can be further purified and modified (i.e. immunoaffinity chromatography, antibody fragmentation, label conjugation, etc.) to generate highly specific reagents.

Peroxidase-conjugated goat IgG fraction to human IgG Fc is used in immunostaining of acetone-fixed frozen and formalin-fixed, paraffin-embedded tissue sections. It is also suitable for use as a reagent in enzyme immunoassays (EIA), cell and tissue staining (for light microscopy), cell and tissue labeling (for electron microscopy), and blot immunostaining. (Note: F(ab')2 fragments are recommended for staining of cells or tissues which contain Fc receptors. Affinity purified antibodies are recommended to avoid non-specific binding from inherent antibodies of host animals.

Antibody and highly purified HRP (Rz>3.0) are conjugated under defined conditions to obtain optimally labeled product. Conjugated protein is purified by salt fractionation. The product is dialyzed into 0.02M sodium phosphate, 0.14M sodium chloride, pH 7.3, with 0.01% thimerosal, adjusted to standard titer, filtered through a 0.22 μm filter, vialed and lyophilized.

The total protein is measured using the Biuret procedure with bovine albumin as the standard. To ensure that the product titer falls within the required range, antibody titer is standardized by microtiter plate ELISA with human IgG. The product is tested for purity and specificity at final concentration by immunoelectrophoresis.

Supplier: Cytiva

The bacteria genomicPrep Mini Spin Kit is designed for the rapid extraction and purification of high quality genomic DNA from gram-positive and gram-negative bacteria. The kit can be used to isolate genomic DNA from a wide range of bacterial strains such as DH5a, TOP10, JM109, Bacillus subtilis, and more. The illustra™ bacteria genomicPrep Mini Spin Kit produces highly pure and intact genomic DNA with A₂₆₀/A₂₈₀ values of 1.75 - 1.85.

Supplier: Genetex

The basic repeating unit of chromatin is the nucleosome, which is composed of a protein octamer containing two each of the core histones H2A, H2B, H3, and H4, surrounded by approximately 146 base pairs of DNA. Reversible acetylation of highly conserved lysine residues in the N-terminal tail domains of core histones plays an important role in transcriptional regulation, cell cycle progression, and development events. Several histone acetyltransferases (HATs) catalyze this acetylation reaction (e.g. GCN5, PCAF, p300/CBP, TAFII250, P/CAF, SRC-1, BRCA-2). Acetylation of the core histones is generally considered to be associated with gene activation, probably through maintenance of the unfolded structure of transcribing nucleosomes. Histone acetylation is a dynamic process in which levels are determined by the net activities of HATs and the competing enzymes histone deacetylases (HDACs). Both activities are associated with the nuclear matrix. Eleven different mammalian HDACs have been described. HDACs 1-3 & 8 (Class I) are similar to yeast Rpd3 protein, while HDACs 4-7, 9 & 10 (Class II) are similar to yeast Hda1 protein. The activities of the histone deacetylases are often, but not always, associated with transcriptional repression and nucleosome condensation. HDAC1, HDAC2 and several others are the catalytic subunits of different multiprotein regulatory complexes. Other components of such complexes may include: corepressors such as mSin3, N-CoR, SMRT, associated proteins such as SAP18, SAP30, RbAp46, RbAp48, and c-Ski oncogenic protein (involved in DNA methylation). Nucleosome remodeling and deacetylation (NRD) complexes containing HDAC1, HDAC2, Mi-2 (CH3, CH4) dermatomyositis specific autoantigen, and MAT2 (metastasis-associated protein) (related to MAT1) have been described. It is therefore assumed that ATP-dependent nucleosome remodeling activity and histone deacetylation may be interconnected or interdependent. Recruitment of the multiprotein complexes to promoter sites occurs by many sequence specific DNA-binding proteins such as unliganded nuclear hormone receptors, DP1-E2F, YY1, and Rb family of transcription factors, transcriptional repressors, and tumor suppressors (e.g. BRCA1). Aberrant recruitment of HDACs by various oncoproteins may occur in certain neoplastic diseases. It has been found that inhibition ofHDAC2 activity by valporic acid induces proteosomal degradation of HDAC2.

Supplier: Invitrogen

Thermo Scientific™ Pierce™ High pH Reversed-Phase Peptide Fractionation Kit increases protein identification from LC/MS analysis through orthogonal peptide fractionation of complex peptide samples.Easy-to-use—resin provided in single-use spin column formatImproved protein identifications—protein identifications increased by ≥50% when compared to unfractionated samplesReproducible—elution profiles and fractional resolution vary by less than 20%Optimized—robust procedure for maximal protein identification and peptide recovery while minimizing fractional overlapCompatible—reagents validated with a variety of complex samples, including TMT™-labeled peptidesIn order to enable deep proteome sequencing, it is often necessary to reduce the sample complexity by fractionation in an orthogonal dimension prior to LC/MS analysis. The Pierce High pH Reversed-Phase Peptide Fractionation Kit utilizes high pH reversed-phase chromatography to separate peptides by hydrophobicity and provides excellent orthogonality to low pH reversed-phase LC-MS gradients.The kit has been designed to improve protein identification through the use of a proprietary reversed-phase resin in an easy-to-use spin column format with a highpH fractionation protocol. In contrast to strong cation exchange (SCX) fractionation, the high-pH reversed-phase fractions do not require an additional desalting step before LC/MS analysis.The High pH Reversed-phase Peptide Fractionation Kit includes a high pH buffer (0.1% triethylamine) and twelve spin columns containing pH-resistant reversed-phase resin. Each reversed-phase fractionation spin column enables fractionation of 10–100 µg of peptide sample using a microcentrifuge.Native, phosphorylated, Tandem Mass TagTM (TMTTM)-labeled, and other complex peptide mixture samples can be fractionated using this kit. Combining the search results generated by the individual fractions helps improve protein sequence coverage and increases the number of identified proteins relative to unfractionated samples.Applications:Reducing sample complexity to identify targets of interestConducting systems biology studiesReducing sample complexity to improve quantitation studies

Supplier: Rockland Immunochemical

Mouse IgG TrueBlot® is a unique DyLight™ 800 conjugated anti-mouse IgG immunoblotting (second step) reagent. Mouse IgG TrueBlot® enables detection of immunoblotted target protein bands, without hindrance by interfering immunoprecipitating immunoglobulin heavy and light chains. It is easy to generate publication-quality IP/Fluorescent Western Blot data with Mouse IgG TrueBlot®, simply substitute the conventional DL800 anti-mouse IgG blotting reagent with Fluorescent Mouse TrueBlot® Antibody DyLight™ 800 and follow the prescribed protocol for sample preparation and immunoblotting.

Mouse IgG TrueBlot® is ideal for use in protocols involving immunoblotting of immunoprecipitated proteins. TrueBlot preferentially detects the non-reduced form of mouse IgG over the reduced, SDS-denatured form of IgG. When the immunoprecipitate is fully reduced immediately prior to SDS-gel electrophoresis, reactivity of Mouse IgG TrueBlot® with the 55 kDa heavy chains and the 23 kDa light chains of the immunoprecipitating antibody is minimized thereby eliminating interference by the heavy and light chains of the immunoprecipitating antibody in IP/Western blotting applications. Applications include studies examining post-translational modification (e.g., phosphorylation or acetylation) or protein-protein interactions. Fluorescent Mouse TrueBlot® Antibody DyLight™ 800 may also be used for detection in immunoassays that do not employ immunoprecipitation.

Supplier: Rockland Immunochemical

Rabbit IgG TrueBlot® is a unique DyLight™ 800 conjugated anti-rabbit IgG immunoblotting (second step) reagent. Rabbit IgG TrueBlot® enables detection of immunoblotted target protein bands, without hindrance by interfering immunoprecipitating immunoglobulin heavy and light chains. It is easy to generate publication-quality IP/Fluorescent Western Blot data with Rabbit IgG TrueBlot®, simply substitute the conventional DL800 anti-rabbit IgG blotting reagent with Fluorescent Rabbit TrueBlot® Antibody DyLight™ 800 and follow the prescribed protocol for sample preparation and immunoblotting. Ideal for Li Cor Odyssey imaging as well as other IR and near IR imaging systems.

Rabbit IgG TrueBlot® is ideal for use in protocols involving immunoblotting of immunoprecipitated proteins. TrueBlot preferentially detects the non-reduced form of rabbit IgG over the reduced, SDS-denatured form of IgG. When the immunoprecipitate is fully reduced immediately prior to SDS-gel electrophoresis, reactivity of Rabbit IgG TrueBlot® with the 55 kDa heavy chains and the 23 kDa light chains of the immunoprecipitating antibody is minimized thereby eliminating interference by the heavy and light chains of the immunoprecipitating antibody in IP/Western blotting applications. Applications include studies examining post-translational modification (e.g., phosphorylation or acetylation) or protein-protein interactions. Fluorescent Rabbit TrueBlot® Antibody DyLight™ 800 may also be used for detection in immunoassays that do not employ immunoprecipitation.

Supplier: Genetex

Tau proteins are microtubule-associated proteins that are abundant in neurons in the central nervous system and are less common elsewhere. They were discovered in 1975 in Marc Kirschner's laboratory at Princeton University. Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. The isoforms are a result of alternative splicing in exons 2,3, and 10 of the tau gene. Phosphorylation of tau is regulated by a host of kinases. For example, PKN, a serine/threonine kinase. When PKN is activated, it phosphorylates tau, resulting in disruption of microtubule organization. Hyperphosphorylation of the tau protein (tau inclusions), however, can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other tauopathies. Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are mostly found in neurons compared to non-neuronal cells. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is not present in dendrites and is active primarily in the distal portions of axons where it provides microtubule stabilization but also flexibility as needed. This contrasts with STOP proteins in the proximal portions of axons which essentially lock down the microtubules and MAP2 that stabilizes microtubules in dendrites. The tau gene locates on chromosome 17q21, containing 16 exons. The major tau protein in the human brain is encoded by 11 exons. Exon 2, 3 and 10 are alternative spliced, allowing six combinations (2-3-10-; 2+3-10-; 2+3+10-; 2-3-10+; 2+3-10+; 2+3+10+). Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They differ in either no, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-regions at the C-terminal part exon 10 missing. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). All of the six tau isoforms are present in an often hyperphosphorylated state in paired helical filaments from Alzheimer's Disease brain. In other neurodegenerative diseases, the deposition of aggregates enriched in certain tau isoforms has been reported. When misfolded this otherwise very soluble protein can form extremely insoluble aggregates that contribute to a number of neurodegenerative diseases.

Supplier: Genetex

Tau proteins are microtubule-associated proteins that are abundant in neurons in the central nervous system and are less common elsewhere. They were discovered in 1975 in Marc Kirschner's laboratory at Princeton University. Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. The isoforms are a result of alternative splicing in exons 2,3, and 10 of the tau gene. Phosphorylation of tau is regulated by a host of kinases. For example, PKN, a serine/threonine kinase. When PKN is activated, it phosphorylates tau, resulting in disruption of microtubule organization. Hyperphosphorylation of the tau protein (tau inclusions), however, can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other tauopathies. Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are mostly found in neurons compared to non-neuronal cells. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is not present in dendrites and is active primarily in the distal portions of axons where it provides microtubule stabilization but also flexibility as needed. This contrasts with STOP proteins in the proximal portions of axons which essentially lock down the microtubules and MAP2 that stabilizes microtubules in dendrites. The tau gene locates on chromosome 17q21, containing 16 exons. The major tau protein in the human brain is encoded by 11 exons. Exon 2, 3 and 10 are alternative spliced, allowing six combinations (2-3-10-; 2+3-10-; 2+3+10-; 2-3-10+; 2+3-10+; 2+3+10+). Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They differ in either no, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-regions at the C-terminal part exon 10 missing. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). All of the six tau isoforms are present in an often hyperphosphorylated state in paired helical filaments from Alzheimer's Disease brain. In other neurodegenerative diseases, the deposition of aggregates enriched in certain tau isoforms has been reported. When misfolded this otherwise very soluble protein can form extremely insoluble aggregates that contribute to a number of neurodegenerative diseases.

Supplier: Genetex

The RNAs that direct protein synthesis in animals and plant cells are synthesized in the nucleus as large precursors (pre-mRNAs). The protein coding sequences in pre-mRNA molecules are arranged in discontinuous segments - exons interspersed with noncoding sequences - introns. In a process termed splicing, these introns are efficiently removed before the pre-mRNA is transported from the nucleus to the cytoplasm, where it is translated into protein. Studies have shown that nuclear pre-mRNA splicing takes place in a multi-component structure termed a spliceosome. The polypyrimidine tract-binding (PTB) protein-associated splicing factor (PSF), which plays an essential role in mammalian spliceosomes, is a ubiquitous nuclear matrix protein. A complex between PTB and PSF is necessary for pre-mRNA splicing. PSF contains two consensus RNA-binding domains and an unusual amino terminus rich in proline and glutamine residues. The RNA-binding properties of PSF are apparently identical to those of PTB. Both proteins, together and independently, bind the polypyrimidine tract of mammalian introns. However, the nuclear localization of PSF and PTB and their distribution in subnuclear fractions differ markedly: isolated nuclear matrices contain a bulk of PSF, but only minor amounts of PTB. In confocal microscopy both proteins appear in speckles, the majority of which do not co-localize. These PTB/PSF complexes, as well as the observed PSF-PTB interaction, may reflect the presence of PTB and PSF in spliceosomal complexes during RNA processing, although other data point to different cellular distribution and nuclear matrix association of the majority of PSF and PTB. The cleavage of PSF during lysis of immature myeloid cells is accompanied by digestion of the PTB splicing regulator but not other proteins tested. In contrast, during apoptosis PTB is degraded while PSF remains intact. Proteolytic degradation of PSF specifically occurs in intact myeloid cells and this process is enhanced upon immature myeloid cell lysis; PSF is completely cleaved to a 47 kDa proteolytic cleavage product (p47), due to potent proteolytic activity found in these cells but rare in other cells and tissues. Furthermore, p47 is abundant in intact normal and tumor myeloid cells while in other cell types it is undetectable. The bone marrow 47 kDa protein is a fragment constituting the N-terminal, protease-resistant half of the splicing factor PSF. PSF is highly basic and migrates anomalously on SDS gels. The 47 kDa protein of mouse cells of immature myeloid origin (bone marrow and acute myeloid leukemia) exhibits a gel migration pattern corresponding to a 49 kDa molecule. In other cell types such as lymphoid cells and in peripheral blood cells, PSF appears as approx. 100 kDa or 75 kDa molecules. The sequence of a fragment of mouse PSF was found to be remarkably similar to that of human PSF ( > 98% homology). Also, the sequences of PSF and the human (h) 100 kDa DNA-pairing protein (hPOMp100) reveals identity. Homologous pairing is a fundamental biological reaction implicated in various cellular processes such as DNA recombination and repair, chromosome pairing, sister chromatid cohesion and chromosome condensation, gene inactivation and initiation of replication. The base pairing is also involved in spliceosome assembly resulting in formation of a dynamic Holliday-like structure within which splicing occurs. Indeed, PSF/hPOMp100 bind both singlestranded (ss) and double-stranded (ds) DNA and facilitates the renaturation of complementary ssDNA molecules. Importantly, PSF/hPOMp100 promotes the formation of D-loops in superhelical duplex DNA. PSF/hPOMp100 also serves as an efficient substrate for protein kinase C (PKC) in vitro. PKC phosphorylation of PSF/hPOMp100 stimulates its DNA binding and D-loop formation activity suggesting a possible regulatory mechanism. PSF has been demonstrated to interact with a variety of cellular targets including the human pro-oncoproteins EWS, hPOMp75/TLS and calmodulin, the RNA/DNAbinding nuclear protein p54nrb/NonO (the homolog of PSF) and DNA topoisomerase. A direct interaction has been observed, between PSF and topoisomerase I which has been implied in DNA recombination, DNA repair, and chromosome formation and may act as a transcription factor and a protein kinase. PSF is also expressed by differentiating neurons in developing mouse brain. Both the expression of PSF mRNA in cortex and cerebellum and PSF immunoreactivity in all brain areas has been found to be high during embryonic and early postnatal life. In adult tissue, only various neuronal populations in the hippocampus and olfactory bulb express PSF. PSF is expressed by differentiating neurons but not by astrocytic cells including radial glia; however oligodendrocytes differentiating in vitro were found to express it. The restricted expression of PSF suggests that it is involved in the control of neuronal-specific splicing events occurring at particular stages of neuronal differentiation and maturation. Monoclonal antibodies reacting specifically with PSF are useful tools for the molecular identification and characterization of the functional activity of PSF.

Supplier: Mettler Toledo

Accessories for Karl Fischer Titrators, EVA V1 and V3

Supplier: G-Biosciences

TRITON X-100 IMMOBILIZED 10ML RESIN

Supplier: United Scientific Supplies

A multifunctional digital scale with removable bowl.

Supplier: G-Biosciences

Immobilized Octylphenolpoly(ethyleneglycolether)x is use for refolding of recombinant proteins that were expressed in aggregated form or as inclusion bodies in genetically engineered cells such as E. coli.

Supplier: Tecniplast Usa

The 1145T Mouse cage can comfortably house four mice of standard size, and is available in polycarbonate or polysulfone materials.