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E. PROTEIN

High throughput E. coli Recombinant human proteome Bioinformatics

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Catalog No Product Name Package Extraction
Buffer Swab CAFL0571 Capilia Flu Neo 10T/Box Yes Yes CAMP1571 Capilia Mycoplasma
10T/Box Yes Yes CAAD0370 Capilia Adeno Neo 20T/Box Yes No CARS0970 Capilia RSV
Neo 20T/Box Yes No CAHM1670 Capilia hMPV 20T/Box Yes No CAST1170 Capilia StrepA
20T/Box Yes No CAAD0371 Capilia Adeno Neo Test Plate 10T/Box No No CARS0971
Capilia RSV Neo Test Plate 10T/Box No No CAHM1671 Capilia hMPV Test Plate
10T/Box No No CATB0870 Capilia TB-Neo 100T/Box No No CATB0871 Capilia TB-Neo
10T/Box No No CATB0877 Capilia TB-Neo Extraction Buffer 20mL/Bottle Yes No
CAMC8170 Capilia MAC Ab Elisa 96T/Box No No

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December 29, 2022 by Jacob1 Min Reading
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EXPRESSION AND PURIFICATION OF A RECOMBINANT ENTEROTOXIN PROTEIN USING DIFFERENT
E. COLI HOST STRAINS AND EXPRESSION VECTORS

Infection by Enterotoxigenic Escherichia coli is a frequent trigger of diarrhea
in animals. The growth of vaccines in opposition to enterotoxins can
successfully management the an infection. We have beforehand constructed a
recombinant antigen SLS fused by STa, LTB and STb enterotoxin and it confirmed a
excessive immunogenicity in mice. Herein, we evaluated the expression of SLS in
three totally different E. coli cells with corresponding plasmids. SLS proteins
expressed in E. coli BL21 (DE3) and Rosetta-gami B (DE3) had been aggregated as
inclusion our bodies, and the proteins solubility weren’t clearly promoted in
low temperature mixed with adjustment of inducer focus. In distinction, SLS
protein with maltose-binding protein (MBP) yielded from TB1 (DE3) cells had been
partially soluble. After growing the IPTG focus within the medium as much as 2
mM and incubating at 37 ℃ for Four h, the soluble protein yield reached the very
best degree (4.533 mg/0.2 L tradition), which was considerably greater than the
expression of SLS protein in Rosetta-gami B (DE3) (P < 0.05). Therefore, the
TB1-pMAL expression system can be utilized for mass extraction and purification
of SLS antigen previous to measuring its immunogenicity in pregnant mammals.


ENDOLYSIN-BASED AUTOLYTIC E. COLI SYSTEM FOR FACILE RECOVERY
OF RECOMBINANT PROTEINS

Recovery of recombinant proteins from the Escherichia coli cytoplasm is
dependent upon cell disruption by mechanical, chemical, and/or enzymatic
strategies, which often trigger incomplete cell breakage or protein
denaturation. Controllable autolytic E. coli strains have been designed to
facilitate the purification of recombinant proteins; nevertheless, these strains
endure from low restoration yield, sluggish cell lysis, or in depth pressure
engineering. Herein, we report an improved, extremely environment friendly
programmable autolytic E. coli platform, wherein cell lysis is initiated upon
the induced expression of T4 lysozyme with N-terminal fusion of a
cell-penetrating peptide. Through the engineering of the peptide sequence and
copy quantity, and by incorporating the fusion lytic gene into the E.
coli genome

, greater than 99.97% of cells could possibly be lysed inside 30 min of
induction regardless of cell age. read more

September 25, 2021July 23, 2021 by Jacob2 Min Reading
Blocking, blocking peptide, DNA, extract, Gene, Goat, Guinea, Hamster, Mink,
Monkey, Mouse, Plant, protein-DNA, Proteins, Reagents, RNA, UPA


IMMOBILIZATION OF RECOMBINANT E. COLI CELLS IN A BACTERIAL CELLULOSE-SILK
COMPOSITE MATRIX TO PRESERVE BIOLOGICAL FUNCTION

Strategies for the encapsulation of cells for the design of cell-based sensors
require environment friendly immobilization procedures whereas preserving
organic exercise of the reporter cells. Here, we introduce an immobilization
method that depends upon the symbiotic relationship between two bacterial
strains: cellulose-producing Gluconacetobacter xylinus cells; and
recombinant Escherichia coli cells harboring recombinase-based dual-color
artificial riboswitch (RS), as a mannequin for cell-based sensor. Following
sequential coculturing of recombinant cells in the cellulose matrix, remaining
immobilization of E. coli cells was accomplished after reconstituted silk
fibroin (SF) protein was added to a “dwelling membrane” producing the composite
bacterial cellulose-silk fibroin (BC-SF) scaffold. By controlling incubation
parameters for each varieties of cells, in addition to the conformations in SF
secondary construction, a selection of strong composite scaffolds have been
ready starting from opaque to clear. The properties of the scaffolds have been
in contrast in phrases of porosity, water capability, distribution of
recombinant cells throughout the scaffolds matrix, onset of cells activation,
and skill to guard recombinant operate of cells towards UV irradiation. The
closer-fitted microstructure of clear BC-SF scaffolds resulted in leakage-free
encapsulation of recombinant cells with preserved RS

operate as a result of of a mixture of a number of parameters that carefully
matched properties of a biofilm setting. read more

September 11, 2021August 28, 2021 by Jacob2 Min Reading
Blocking, blocking peptide, DNA, extract, Gene, Goat, Guinea, Hamster, Mink,
Monkey, Mouse, Plant, protein-DNA, Proteins, Reagents, RNA, UPA


STUDY OF THE EFFECTS OF 3.1 THZ RADIATION ON THE EXPRESSION OF RECOMBINANT RED
FLUORESCENT PROTEIN (RFP) IN E. COLI

In current years, many research have been carried out to research the
non-thermal effects of THz radiation on completely different organisms, however
additional research are wanted to totally elucidate the effects, particularly on
the molecular degree. In this research, we explored the effects of at 3.1 THz
radiation on protein expression in Escherichia coli (E. coli) utilizing red
fluorescent protein as a reporter molecule. After Eight hours of steady THz
irradiation of micro organism on LB (Luria-Bertani) strong plates at a median
energy of 33 mW/cm2 and 10 Hz pulse repetition frequency, we discovered that the
plasmid copy quantity, protein expression and fluorescence depth of micro
organism from the irradiated space had been 3.8-, 2.7-, and three. Three
occasions larger than in micro organism from the un-irradiated space,
respectively. These findings counsel that plasmid replication modified
considerably in micro organism uncovered to 3.1 THz radiation, ensuing in
elevated protein expression as evidenced by elevated fluorescence depth of the
RFP reporter.


E. COLI EXPRESSION AND IMMUNOLOGICAL EVALUATION OF
EXPRESSED RECOMBINANT NEWCASTLE ILLNESS VIRUS HEMAGGLUTININ-NEURAMINIDASE
PROTEIN IN CHICKENS

Every 12 months, the poultry business experiences important financial losses
attributable to epidemics of Newcastle illness virus (NDV). Developing new
vaccines by figuring out and utilizing the immunogenic
hemagglutinin-neuraminidase (HN) protein can defend the poultry business. In the
current research, the full-length HN protein was expressed in Escherichia coli
(E. coli) BL21 (DE3) cells, purified by way of affinity chromatography and
detected by way of western blot evaluation utilizing His-specific antibodies.
The purified HN protein was additional evaluated in chickens to check the immune
response in opposition to NDV. The profitable manufacturing of HN-specific IgY
proved the exercise of the purified HN protein. IgY was current in the serum of
immunized chickens. However, the immune response was larger in chickens
immunized with purified HN protein together with full and incomplete adjuvants
than in chickens immunized with solely the HN protein. Keywords: protein;
Newcastle illness virus; poultry; infectious illnesses; vaccines.


HIGH DEGREE EXPRESSION AND PURIFICATION OF RECOMBINANT FLOUNDER DEVELOPMENT
HORMONE IN E. COLI.

Recombinant flounder development hormone was overproduced in E. coli by
utilizing codon optimized artificial gene and optimized expression circumstances
for top degree manufacturing. The gene was cloned into PET-28a expression vector
and remodeled into E. coli BL21 (DE3). Induction at decrease temperature,
decrease IPTG concentrations and richer development media throughout expression
resulted in elevated expression degree. The protein expression profile was
analyzed by SDS-PAGE, the authenticity was confirmed by western blotting and the
focus was decided by Bradford assay. In addition, a number of makes an attempt
had been made to supply soluble product and all resulted in insoluble product.
The overexpressed protein was effectively purified from inclusion our bodies by
reasonable velocity centrifugation after cell lysis. Among the solubilization
buffers examined, buffer with 1% N-lauroylsarcosine in the presence of lowering
agent DTT at alkaline pH resulted in environment friendly solubilization and
restoration. The denaturant was eliminated by filtration and dialysis. The
quantity of the development hormone recovered was considerably larger than
earlier experiences that expressed native development hormone genes in E. coli.
The methodology tailored in this research, can be utilized to supply flounder
development hormone at giant scale degree in order that it may be used in
aquaculture. This method can also apply to different proteins if excessive
degree expression and environment friendly purification is sought in E. coli.


PURIFICATION AND CHARACTERIZATION OF A RECOMBINANT Β-XYLOSIDASE FROM BACILLUS
LICHENIFORMIS ATCC 14580 INTO E. COLI BL21.

Present analysis work is aimed to purify and characterize a recombinant
β-xylosidase enzyme which was beforehand cloned from Bacillus licheniformis ATCC
14580 in to Escherichia coli BL21. Purification of recombinant enzyme was
carried out by utilizing ammonium sulphate precipitation technique adopted by
single step immobilized metallic ion affinity chromatography. Specific exercise
of purified recombinant β-xylosidase enzyme was 20.78 Umg-1 with 2.58
purification fold and 33.75% restoration. SDS-PAGE was used to find out the
molecular weight of recombinant purified β-xylosidase and it was recorded as 52
kDa. Purified enzyme confirmed stability upto 90°C inside a pH vary of 3-Eight
with and optimum temperature and pH, 55ºC and seven.0, respectively. The enzyme
exercise was not significantly affected in the presence of EDTA. An improve in
the enzyme exercise was discovered in the manifestation of Mg+2. Enzyme exercise
was additionally elevated by 6%, 18% and 22% in the presence of 1% Tween 80,
β-mercaptoethanol and DTT, respectively. Higher concentrations (10 – 40%) of
natural solvents didn’t present any impact upon exercise of enzyme. All these
traits of the recombinant enzyme endorsed it as a possible candidate for biofuel
business.

Soluble expression of recombinant midgut zymogen (native propeptide) proteases
from the Aedes aegypti Mosquito Utilizing E. coli as a bunch. read more

August 22, 2021July 23, 2021 by Jacob4 Min Reading
Blocking, blocking peptide, DNA, extract, Gene, Goat, Guinea, Hamster, Mink,
Monkey, Mouse, Plant, protein-DNA, Proteins, Reagents, RNA, UPA


OVERPRODUCTION OF RECOMBINANT E. COLI MALATE SYNTHASE ENHANCES CHLAMYDOMONAS
REINHARDTII BIOMASS BY UPREGULATING HETEROTROPHIC METABOLISM.

High uptake of malate and environment friendly distribution of intracellular
malate to organelles contributed to biomass enhance, decreasing upkeep power. In
this research, transgenic Chlamydomonas reinhardtii was developed that stably
expresses malate synthase within the chloroplast. The strains beneath glyoxylate
remedy confirmed 19% extra enhance in microalgal biomass than wild-type. By RNA
evaluation, transcript ranges of malate dehydrogenase (MDH4) and acetyl-CoA
synthetase (ACS3), isocitrate lyase (ICL1) and malate synthase (MAS1), had been
considerably extra expressed (17%, 42%, 24%, and 18% respectively), which was in

keeping with reported heterotrophic metabolism flux evaluation with the target
perform maximizing biomass. read more

August 11, 2021July 23, 2021 by Jacob1 Min Reading
Blocking, blocking peptide, DNA, extract, Gene, Goat, Guinea, Hamster, Mink,
Monkey, Mouse, Plant, protein-DNA, Proteins, Reagents, RNA, UPA


EXPRESSION AND PURIFICATION OF FUNCTIONAL RECOMBINANT CUL2•RBX1 FROM E. COLI

Cullin-2 (CUL2) primarily based cullin-RING ligases (CRL2s) comprise a household
of ubiquitin E3 ligases that exist solely in multi-cellular organisms and are
essential for mobile processes equivalent to embryogenesis and viral
pathogenesis. CUL2 is the scaffold protein that binds one of the interchangeable
substrate receptor modules, which consists of adaptor proteins and the substrate
receptor protein. The VHL protein is a substrate receptor identified to focus on
hypoxia-inducible issue α (HIF1α) for ubiquitination and degradation. Because of
its essential function within the ubiquitination of necessary mobile components
equivalent to HIF1α, CRL2s have been investigated for his or her organic
features and the event of novel therapeutics towards illnesses. Given the
significance of CRL2s in organic and biomedical analysis, strategies that
effectively produce functional CUL2 proteins will significantly facilitate
research on the mechanism and regulation of CRL2s. Here, we report two
cost-effective programs for the expression and purification of recombinant human
CUL2 from E. coli cells. The purified CUL2

proteins have been ~ 95% pure, may bind their substrate receptor modules, and
have been enzymatically read more

July 22, 2021July 22, 2021 by Jacob1 Min Reading
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 * a universal protein array system for quantitative detection of
   protein-protein
 * Blocking
 * blocking peptide
 * body weight and body mass index on patients with hypercholesterolemia: a
   systematic review and meta-analysis.
 * Cotranslational protein-RNA associations predict protein-protein
   interactions.
 * Diagnostic performance of circulating exosomes in human cancer: A
   meta-analysis.
 * DNA
 * Effects of plant protein and animal protein on lipid profile
 * extract
 * Gene
 * Goat
 * Guinea
 * Hamster
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 * Monkey
 * Mouse
 * Plant
 * Predicting protein-protein binding sites in membrane proteins.
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