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ortion of positive CD86 and CD206 expression among groups (
= 24 004.33 and 832.50,
< 0.001). Higher IL-1β and TNF-α levels were measured in the LPS + IFN-γ group than in the IL-4 + IL-13 group, the L3 protein group and the L5 protein group (
< 0.001), and greater TGF-β1 and IL-10 levels were seen in the IL-4 + IL-13 group, the L3 protein group and the L5 protein group than in the negative control group and the LPS + IFN-γ group (
< 0.05).
Both L3 and L5 proteins of
may induce the polarization of THP-1-derived macrophages to M2 type
.
Both L3 and L5 proteins of N. brasiliensis may induce the polarization of THP-1-derived macrophages to M2 type in vitro.
To investigate the protective effect of recombinant adult serine protease inhibitor from
(
adSPI) on sepsis-associated acute kidney injury in mice.
A total of 18 male BALB/c mice were randomly divided into the sham-operation group, the model group, and the
adSPI treatment group, of 6 mice in each group. Sepsis-associated acute kidney injury was modeled in the model group and
adSPI treatment group by cecal ligation puncture (CLP), while mice in the sham-operation group were only given exploratory laparotomy without ligation or perforation of the cecum. After 30 min of CLP, mice in the sham-operation group and the model group were intraperitoneally injected with PBS (100 μL), and mice in the
adSPI treatment group were intraperitoneally injected with PBS (100 μL) containing
adSPI (2 μg). At 12 h following modeling, the serum levels of alanine aminotransferase (ALT), aspartate aminotransferase (AST), creatinine (Cr) and urea nitrogen (BUN) were measured to assess the liver and kidney functions, anines, thereby protecting sepsis-associated acute kidney injury.
TsadSPI may reduce the MyD88 expression and nuclear positive rate of NF-κB p65 in mouse kidney tissues to up-regulate the expression of immunomodulatory factors and down-regulate the expression of pro-inflammatory cytokines, thereby protecting sepsis-associated acute kidney injury.
To investigate the biological properties of
SjGrpE protein, and to express and purify the recombinant SjGrpE protein and test its immunogenicity.
The amino acid composition, molecular weight, hydrophilicity and hydrophobicity, transmembrane region, signal peptide, localization, phosphorylation site, ubiquitination site, glycosylation site, secondary and tertiary structures and B cell epitopes of the SjGrpE protein were predicted using bioinformatics analyses. The
gene was amplified using PCR assay using
cDNA as a template, double enzyme-digested and linked to the pET28a vector to yield the recombinant plasmid pET28a-SjGrpE. The recombinant plasmid pET28a-SjGrpE was transformed into
BL21, and then IPTG was employed to induce the expression of the target protein, which was purified by nickel ion affinity chromatography. Heparan research buy After mice were immunized with the recombinant SjGrpE protein, mouse sera were collected, and the polyclonal antibody against the SjGrpE protein was characterized.
SjGrpE protedate for S. japonicum infections.
To establish a recombinase-aided isothermal amplification (RAA) assay for the nucleic acid detection of
.
The internal transcribed spacer-1 (
) gene sequence of
was used as the detection target sequence, and the specific primers and probes were designed and synthesized, followed by screening of the primers and probes with the highest specificity, to establish the basic and fluorescent RAA assay for nucleic acid detection of
. The sensitivity of the fluorescent RAA assay was evaluated by using the target gene fragment sequence-contained recombinant plasmids at various copy numbers and the genomic DNA from
as the template DNA samples, and the specificity of the fluorescent RAA assay was evaluated by using the genomic DNA from
,
,
,
,
and
, as well as
and
snail tissues as the template DNA samples.
A fluorescent RAA assay was successfully established for nucleic acid detection of
, which achieved real-time amplification of the specific DNA fragment of
within 20 min at 37 ℃. By using the target gene fragment sequence-contained recombinant plasmids at various copy numbers and the genomic DNA from
as the DNA templates, the lowest detection limits of the fluorescent RAA assay were 10 copies/μL of recombinant plasmids and 100 pg/μL of genomic DNA, respectively. The fluorescent RAA assay was negative for detection of the genomic DNA from
,
,
,
,
,
, and
and
snail tissues.
A simple, rapid fluorescent RAA assay has been successfully established, which has a high sensitivity and specificity for the nucleic acid detection of
.
A simple, rapid fluorescent RAA assay has been successfully established, which has a high sensitivity and specificity for the nucleic acid detection of A. cantonensis.
To establish a novel nucleic acid assay for detection of
based on the recombinase-aided isothermal amplification (RAA) assay, and evaluate its sensitivity and specificity for detection of
.
The specific primer sequences and florescent probes were designed and synthesized based on the
gene as the target gene, and a fluorescent RAA assay was established. The recombinant plasmids at various copies (containing the
gene target sequence) and the genomic DNA of
at various concentrations were used as templates for the fluorescent RAA assay to assess the sensitivity, and the genomic DNA from
,
,
,
,
,
and
was used as templates to assess the specificity of the fluorescent RAA assay.
A novel fluorescent RAA assay was successfully established for detection of
, which allowed the rapid and specific amplification of the target gene fragments at 39 ℃ within 20 min. The sensitivities of the fluorescent RAA assay were 102 copies/μL and 1 pg/μL for detection of the recombinant plasmid and
genomic DNA, respectively, and the fluorescent RAA assay was negative for detection of the genomic DNA from
,
,
,
,
and
, which showed a high specificity.
A fluorescent RAA assay, which is simple, sensitive and specific, is successfully established for nucleic acid detection of
.
A fluorescent RAA assay, which is simple, sensitive and specific, is successfully established for nucleic acid detection of G. lamblia.
Website: https://www.selleckchem.com/products/heparan-sulfate.html
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