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Recombinant expression, purification and characterization of acetylated LysargiNase from Escherichia coli with high activity and stability.

LysargiNase is a novel characterized metalloprotease that can cleave the N-terminii of lysine or arginine residues. The peptides generated by LysargiNase are just mirrors to those generated by trypsin. These characteristics of LysargiNase provide a powerful tool for mass spectrometry (MS)-based proteomics research. A highly active and stable LysargiNase produced by an easy and inexpensive method could greatly benefit proteomics research. Here, we report the soluble recombinant expression, purification and acetyl modification of LysargiNase in Escherichia coli.

1783 related Products with: Recombinant expression, purification and characterization of acetylated LysargiNase from Escherichia coli with high activity and stability.

RANK Ligand Soluble, Huma RANK Ligand Soluble, Huma Recombinant Human Androge Recombinant Mn SOD (Human Recombinant Human MDK [fr ELISA 5α-Androstane-3α, Recombinant Human CTF1 [f Recombinant Human Galecti Recombinant Human CD57 B3 Androgen Receptor (Phosph ∆1-Androstene-3α,17β- Recombinant Human UCHL1 [

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Targeting cell-bound MUC1 on myelomonocytic, monocytic leukemias and phenotypically defined leukemic stem cells with anti-SEA module antibodies.

Cell surface molecules aberrantly expressed or overexpressed by myeloid leukemic cells represent potential disease-specific therapeutic targets for antibodies. MUC1 is a polymorphic glycoprotein, the cleavage of which yields two unequal chains: a large extracellular α subunit containing a tandem repeat array bound in a strong noncovalent interaction to a smaller β subunit containing the transmembrane and cytoplasmic domains. Because the α-chain can be released from the cell-bound domains of MUC1, agents directed against the α-chain will not effectively target MUC1 cells. The MUC1 SEA (a highly conserved protein module so called from its initial identification in a sea urchin sperm protein, in enterokinase, and in agrin) domain formed by the binding of the α and β chains  represents a stable structure fixed to the cell surface at all times. DMB-5F3, a partially humanized murine anti-MUC1 SEA domain monoclonal antibody, was used to examine MUC1 expression in acute myeloid leukemia (AML) and was found to bind acute myelomonocytic and monocytic leukemia (AML-M4 and AML-M5) cell lines. We also examined monocytic neoplasms freshly obtained from patients including chronic myelomonocytic leukemia and juvenile myelomonocytic leukemia, which were found to uniformly express MUC1. CD34/lin/CD38 or CD38 presumed leukemic stem cell populations from CD34 AML and CD34CD38 or CD38 populations from CD34 AML were also found to express MUC1, although at low percentages. Based on these studies, we generated an anti-MUC1 immunotoxin to directly gauge the cytotoxic efficacy of targeting AML-bound MUC1. Using single-chain DMB-5F3 fused to recombinant gelonin toxin, the degree of AML cytotoxicity was found to correlate with MUC1 expression. Our data support the use of an anti-MUC1 SEA module-drug conjugates to selectively target and inhibit MUC1-expressing myelomonocytic leukemic cells.

1328 related Products with: Targeting cell-bound MUC1 on myelomonocytic, monocytic leukemias and phenotypically defined leukemic stem cells with anti-SEA module antibodies.

Goat Anti-Human Androgen Rabbit Anti-Rat Androgen Rat monoclonal anti mouse Mouse Anti-Mouse NC1.1 (N Mouse Anti-Human MUC1 EMA Mouse Anti-Human Prolifer Rat monoclonal anti mouse Mouse Anti-Human CD40 (CD Rabbit Anti-SF9 Insect Ce Rat Anti-Human Endothelia Mouse Anti-Guinea Pig T C Mouse Anti-HPV 18 Oncopro

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Bldesin, the first functionally characterized pathogenic fungus defensin with Kv1.3 channel and chymotrypsin inhibitory activities.

Fungus defensin is a kind of important natural peptide resource, such as plectasin from the soil fungus Pseudoplectania nigrella with potential application in the antimicrobial peptide lead drug discovery. Here, a fungus defensin named Bldesin with Kv1.3 channel and serine protease inhibitory activities was first explored. By GST-Bldesin fusion expression and enterokinase cleaving strategy, recombinant Bldesin was obtained successfully. Antimicrobial assays showed that Bldesin had potent activity against Gram-positive Staphylococcus aureus, but had no effect on Gram-negative Escherichia coli. Electrophysiological experiments showed that Bldesin had Kv1.3 channel inhibitory activity. Serine protease inhibitory associated experiments showed that Bldesin had unique chymotrypsin protease inhibitory, elastase protease inhibitory, and serine protease-associated coagulation inhibitory activities. To the best of our knowledge, Bldesin is the first functionally characterized pathogenic fungus defensin with Kv1.3 channel and chymotrypsin inhibitory activities and highlighted novel pharmacological effects of fungus-derived defensin peptides.

2183 related Products with: Bldesin, the first functionally characterized pathogenic fungus defensin with Kv1.3 channel and chymotrypsin inhibitory activities.

AZD-3514 Mechanisms: Andr ∆1-Androstene-3α,17β- 3-(Aminomethyl)pyridine C Cytokine (Human) Antibody Hoechst 33342 *UltraPure (2E)-3-(1,3-Benzodioxol-5 Sheep Anti-Theophylline 3 2-Acetamido-3,4,6-tri-O-b 3-Nitrobenzyl bromide CAS HDAC-1 Blocking Peptide;A 5 Bromoisoquinoline CAS N Mouse Anti-GAPDH(3E12)-Lo

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A Feasibility Study to Evaluate as a Host for Producing Recombinant Human Parathyroid Hormone.

Biosynthetic teriparatide (1-34) (TPD) is a N-terminally truncated version of human parathyroid hormone (hPTH). The recombinant form of this polypeptide has been expressed in and approved as the first anabolic treatment of osteoporosis in the EU and the USA. Feasibility of expression and secretion of a tag- fused form of TPD into was examined due to several advantages of over in production of recombinant proteins with pharmacological activities.

2934 related Products with: A Feasibility Study to Evaluate as a Host for Producing Recombinant Human Parathyroid Hormone.

Recombinant Human ASF1A P Human Growth Hormone anti Bone Morphogenetic Protei MOUSE ANTI HUMAN CD15, Pr Recombinant Human Interfe NATIVE HUMAN PROLACTIN, P Recombinant Human ASF1A P NATIVE HUMAN PROLACTIN, P Human Plasminogen Total A Growth Differentiation Fa Human Vitronectin Total A Human Growth Hormone anti

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Generation of Highly Specific Proteolytic Biocatalysts by Screening Technologies.

We propose a yeast display-based system for screening of proteolytic enzyme libraries that utilizes substrate protein adsorbed on the yeast cell surface and containing a desired cleavage sequence. Specific cleavage of the substrate protein releases its biotin-binding center. The cells carrying the target proteinase can be selected by cytofluorometry due to interaction with biotinylated fluorescent protein. Using human enterokinase light chain as the model proteinase we showed that the proposed screening system highly effectively selects the proteolytic enzymes with preset specificity.

2431 related Products with: Generation of Highly Specific Proteolytic Biocatalysts by Screening Technologies.

Cytokine (Human) Antibody Apoptosis Phospho-Specifi Cytokine (Rat) Antibody A EGF Phospho-Specific Arra Th1 Th2 Th17 (Human) Anti Jak Stat II Phospho-Speci T-Cell Receptor Signaling Cytokine (Human) Antibody Cytokine (Mouse) Antibody Th1 Th2 Th17 (Human) Anti Cytokine (Human) Antibody Apoptosis antibody array

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Large-Scale Generation of Recombinant Granulin Peptides in E. coli.

Generating milligram quantities of correctly folded granulin molecules with properly formed disulfide bonds and biologically relevant activities may represent a considerable challenge. Here I describe a protocol for obtaining well-folded human granulins A, C, and F by expressing them as thioredoxin fusion proteins in Origami (DE3) Escherichia coli cells promoting disulfide bond formation in the cytoplasm environment. The thioredoxin tag is removed by proteolytic cleavage with enterokinase and granulins which are purified by reversed-phase HPLC. Well-folded disulfide species display lower retention time than misfolded species and therefore can be readily purified.

2973 related Products with: Large-Scale Generation of Recombinant Granulin Peptides in E. coli.

Recombinant Human Inhibin Recombinant Human Inhibin Recombinant Human Inhibin Recombinant Human CD63 [f Recombinant Influenza B V Recombinant Human CKB [fr Recombinant Human Interle Recombinant Human DKK1 [f Recombinant E. coli SecB Recombinant Human GPBB PY Recombinant Human Fc-epsi Recombinant Porcine Inter

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Secretion expression of human neutrophil peptide 1 (HNP1) in Pichia pastoris and its functional analysis against antibiotic-resistant Helicobacter pylori.

Human neutrophil peptide 1 (HNP1) is a small (3.44 kDa) cationic peptide that is a distinct member of the defensin family. HNP1 plays a crucial role in controlling bacterial infections, particularly by antibiotic-resistant bacteria, through membrane perforation patterns. The structural characteristics of HNP1's three intramolecular disulfide bridges cause difficulty in its synthesis via chemical methods. In this study, bioactive recombinant HNP1 was produced using the Pichia pastoris (P. Pichia) expression system. HNP1 was fused with the polyhedrin of Bombyx mori and enhanced green fluorescent protein (EGFP) to prevent HNP1 toxicity in yeast host cells under direct expression. An enterokinase protease cleavage site (amino acid sequence DDDDK) was designed upstream of the HNP1 peptide to obtain the antibacterial peptide HNP1 with native structure after it was cleaved by the enterokinase. The fusion HNP1 protein (FHNP1) was successfully expressed and had a molecular mass of approximately 62.6 kDa, as determined using SDS-PAGE and Western blot. Then, the recovered FHNP1 was digested and purified; Tricine-SDS-PAGE results showed that HNP1 was successfully released from FHNP1. Functional analysis of induction against antibiotic-resistant Helicobacter pylori (H. pylori) showed that it was challenging for HNP1 to acquire resistance to the antibiotic-resistant H. pylori. Moreover, in vitro studies showed that HNP1 exerted a strong effect against antibiotic-resistant H. pylori activity. Furthermore, the animal model of H. pylori infection established in vivo showed that HNP1 significantly reduced the colonization of antibiotic-resistant H. pylori in the stomach. Our study indicated that this could be a new potential avenue for large-scale production of HNP1 for therapeutic application against the antibiotic-resistant H. pylori infection in humans.

1605 related Products with: Secretion expression of human neutrophil peptide 1 (HNP1) in Pichia pastoris and its functional analysis against antibiotic-resistant Helicobacter pylori.

Human neutrophil peptide Anti-human C1 Esterase In Rabbit Anti-TNIP2 ABIN2 T Human Helicobacter pylori Rabbit Anti-APIP Apaf1 In Protease Inhibitor 15 ant Inhibitory mouse monoclo Inactivated Human Plasmin Interferon alpha-8 antibo Anti human C1 Esterase In INPP1 antibody Source Rab Interleukin-24 antibody S

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Efficient expression and isolation of recombinant human interleukin-11 (rhIL-11) in Pichia pastoris.

Current source of recombinant human interleukin-11 (rhIL-11) is isolated from a fusion protein expressed by E. coli that requires additional enterokinase to remove linked protein, resulting in product heterogeneity of N-terminal sequence. Due to lack of glycosylation, rhIL-11 is suitable to be expressed by yeast cells. However, the only available yeast-derived rhIL-11 presents an obstacle in low production yield, as well as an unamiable process, such as the use of reverse-phase chromatography employing plenty of toxic organic solvents. Our findings showed that the low yield was due to self-aggregation of rhIL-11. A novel process recovering bioactive rhIL-11 from the yeast secretory medium therefore has been developed and demonstrated, involving fermentation from Pichia pastoris, followed by a two-phase extraction to precipitate rhIL-11. After renaturing, the protein of interest was purified by a two-column step, comprising a cation-exchanger, and a hydrophobic interaction chromatography in tandem at high sample loads that was facile and cost-effective in future scale-up. Identity and quality assessments confirmed the expected amino acid sequence without N-terminal heterogeneity, as well as high quality in potency and purity. Such a process provides an alternative and adequate supply of the starting material for the PEGylated rhIL-11.

1691 related Products with: Efficient expression and isolation of recombinant human interleukin-11 (rhIL-11) in Pichia pastoris.

Recombinant Human Interle Recombinant Human Interle Recombinant Human Interle Recombinant Human Interle Recombinant Human Interle Recombinant Human Interle Recombinant Human Interle Recombinant Human Interle Recombinant Human Interle Recombinant Human Interle Recombinant Human Interle Recombinant Human Interle

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Molecular Farming in Barley: Development of a Novel Production Platform to Produce Human Antimicrobial Peptide LL-37.

The peptide LL-37, a component of the human innate immune system, represents a promising drug candidate. In particular, the development of low-cost production platform technology is a critical bottleneck in its use in medicine. In the present study, a viable approach for the LL-37 production in transgenic barley is developed. First, comparative analyses of the effects of different fused peptide epitope tags applicable for accumulation and purification on LL-37 production yield are performed using transient expression in tobacco leaves. Following the selection of the most yielding fusion peptide strategies, eight different constructs for the expression of codon optimized chimeric LL-37 genes in transgenic barley plants are created. The expression of individual constructs is driven either by an endosperm-specific promoter of the barley B1 hordein gene or by the maize ubiquitin promoter. The transgenes are stably integrated into the barley genome and inherited in the subsequent generation. All transgenic lines show normal phenotypes and are fertile. LL-37 accumulated in the barley seeds up to 0.55 mg per 1 kg of grain. The fused epitope tags are cleaved off by the use of enterokinase. Furthermore, in planta produced LL-37 including the fused versions is biologically active.

2429 related Products with: Molecular Farming in Barley: Development of a Novel Production Platform to Produce Human Antimicrobial Peptide LL-37.

Rabbit Anti-Human Vasoact Recombinant Human Interfe Goat Anti-Human TOM1L1 SR Rabbit Anti-Human Toll In Human Dnak (HSP70) His ta Goat Anti-Human MTHFS, (i Human breast invasive duc Human Antithrombin III to Anti Apoptosis Inducing F Recombinant Human IFN-alp Human Inflammation Array Goat Anti-Human VTI1B, (i

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H, N, and C chemical shift assignments of the micelle immersed FAT C-terminal (FATC) domains of the human protein kinases ataxia-telangiectasia mutated (ATM) and DNA-dependent protein kinase catalytic subunit (DNA-PKcs) fused to the B1 domain of streptococcal protein G (GB1).

FAT C-terminal (FATC) is a circa 33 residue-long domain. It controls the kinase functionality in phosphatidylinositol-3 kinase-related kinases (PIKKs). Recent NMR- and CD-monitored interaction studies indicated that the FATC domains of all PIKKs can interact with membrane mimetics albeit with different preferences for membrane properties such as surface charge and curvature. Thus they may generally act as membrane anchoring unit. Here, we present the H, N, and C chemical shift assignments of the DPC micelle immersed FATC domains of the human PIKKs ataxia-telangiectasia mutated (ATM, residues 3024-3056) and DNA protein kinase catalytic subunit (DNA-PKcs, residues 4096-4128), both fused to the 56 residue long B1 domain of Streptococcal protein G (GB1). Each fusion protein is 100 amino acids long and contains in the linking region between the GB1 tag and the FATC region a thrombin (LVPRGS) and an enterokinase (DDDDK) protease site. The assignments pave the route for the detailed structural characterization of the membrane mimetic bound states, which will help to better understand the role of the proper cellular localization at membranes for the function and regulation of PIKKs. The chemical shift assignment of the GB1 tag is useful for NMR spectroscopists developing new experiments or using GB1 otherwise for case studies in the field of in-cell NMR spectroscopy or protein folding. Moreover it is often used as purification tag. Earlier we showed already that GB1 does not interact with membrane mimetics and thus does not disturb the NMR monitoring of membrane mimetic interactions of attached proteins.

2277 related Products with: H, N, and C chemical shift assignments of the micelle immersed FAT C-terminal (FATC) domains of the human protein kinases ataxia-telangiectasia mutated (ATM) and DNA-dependent protein kinase catalytic subunit (DNA-PKcs) fused to the B1 domain of streptococcal protein G (GB1).

Human Dnak (HSP70) His ta Recombinant Human PKC the to M-Calpain (E.C. 3.4.2 Recombinant Human PKC the Rabbit Anti-IEX1 Differen Recombinant Human MMP14 ( Pfu DNA Polymerase protei Recombinant Human PKC the G Protein Coupled Recepto Rabbit Anti-IEX1 Differen Rabbit Anti-IEX1 Differen Rabbit Anti-IEX1 Differen

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