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> Disorders > Congenital Abnormality > Intestinal Atresia, Multiple

Intestinal Atresia, Multiple

Intestinal Atresia, Multiple is a rare congenital condition characterized by the presence of multiple obstructions or narrowings in the small and/or large intestine.
This disorder can lead to complications such as intestinal blockages, malnutrition, and growth delays if left untreated.
Effective research protocols are crucial for advancing our understanding and management of this complex condition.
PubCompare.ai's AI-driven platform helps researchers quickly identify the most accurate and reproducible methods from literature, preprints, and patents, enhancing research effciency and elevating Intestinal Atresia, Multiple studies.

Most cited protocols related to «Intestinal Atresia, Multiple»

1
Tyrosine Kinase Receptor Signaling Assay
697 B-ALL cells
and Molm-14 AML cells were cultured in the presence of 11 or vehicle-only for 1.0 h. Pervanadate solution was prepared fresh
by combining 20 mM sodium orthovanadate in 0.9× PBS in a 1:1
ratio with 0.3% (w/w) hydrogen peroxide in PBS for 15–20 min
at room temperature. Cultures were treated with 120 μM pervanadate
for 3 min prior to collection, and cell lysates were prepared in 50
mM HEPES (pH 7.5), 150 mM NaCl, 10 mM EDTA, 10% glycerol, and 1% Triton
X-100, supplemented with protease inhibitors (Roche Molecular Biochemicals,
no. 11836153001). Mer and Flt3 proteins were immunoprecipitated with
anti-Mer (R&D Systems, no. MAB8912) or anti-Flt3 (Santa Cruz Biotechnology
no. sc-480) antibody and Protein G agarose beads (InVitrogen). Phospho-proteins
were detected by Western blot using an antiphospho-Mer antibody raised
against a peptide derived from the triphosphorylated activation loop
of Mer8 (link) (Phopshosolutions, Inc.) or an
antibody specific for phosphorylated Flt3 (Cell Signaling Technology,
no. 3461). Nitrocellulose membranes were stripped and total proteins
were detected using a second anti-Mer antibody (Epitomics Inc., no.
1633-1) or anti-Flt3 antibody (Santa Cruz Biotechnology no. sc-480).
Relative phosphorylated and total protein levels were determined by
densitometry using ImageJ, and IC50 values were calculated
by nonlinear regression.
32D Cells expressing a chimeric EGFR-Mer,
EGFR-Axl, or EGFR-Tyro3 receptor were cultured in the presence of 11 or vehicle-only for 1.0 h before stimulation with 100 ng/mL
EGF (BD Biosciences no. 354010) for 15 min. Cells were centrifuged
at 1000g for 5 min and washed with 1× PBS. Cell
lysates were prepared in 20 mM HEPES (pH 7.5), 50 mM NaF, 500 mM NaCl,
5.0 mM EDTA, 10% glycerol, and 1% Triton X-100, supplemented with
protease inhibitors (10 μg/mL leupeptin, 10 μg/mL phenylmethylsulfonyl
fluoride, and 20 μg/mL aprotinin) and phosphatase inhibitors
(50 mM NaF and 1.0 mM sodium orthovanadate). Mer protein was immunoprecipitated
using a custom polyclonal rabbit antisera raised against a peptide
derived from the C-terminal catalytic domain of Mer and Protein A
agarose beads (Santa Cruz Biotechnology). Axl and Tyro3 proteins were
immunoprecipitated using an antibody directed against a FLAG epitope
engineered into the chimeric proteins (Sigma-Aldrich, no. F1804).
Phosphotyrosine-containing proteins were detected by Western blot
with a monoclonal HRP-conjugated antiphosphotyrosine antibody (Santa
Cruz Biotechnology, no. sc-508). Antibodies were stripped from membranes,
and total proteins were detected with the same antibodies used for
immunoprecipitation.
Zhang W., DeRyckere D., Hunter D., Liu J., Stashko M.A., Minson K.A., Cummings C.T., Lee M., Glaros T.G., Newton D.L., Sather S., Zhang D., Kireev D., Janzen W.P., Earp H.S., Graham D.K., Frye S.V, & Wang X. (2014). UNC2025, a Potent and Orally Bioavailable MER/FLT3 Dual Inhibitor. Journal of Medicinal Chemistry, 57(16), 7031-7041.
Publication 2014
Antibodies Antibodies, Anti-Idiotypic Aprotinin Catalytic Domain Cells Chimera Edetic Acid EGFR protein, human FLT3 protein, human G-substrate Glycerin HEPES Immune Sera Immunoglobulins inhibitors Intestinal Atresia, Multiple leupeptin Monoclonal Antibodies Nitrocellulose Orthovanadate Peptides Peroxide, Hydrogen pervanadate Phosphoric Monoester Hydrolases Phosphotyrosine Protease Inhibitors Proteins Rabbits Sepharose Sodium Sodium-20 Sodium Chloride Tissue, Membrane Triton X-100 Western Blotting
2
SARS-CoV-2 CPE Assay in Vero E6 Cells
SARS-CoV-2
CPE assay was conducted at Southern Research Institute (Birmingham,
AL). Briefly, compounds were titrated in DMSO and acoustically dispensed
into 384-well assay plates at 60 nL/well. Cell culture media (MEM,
1% Pen/Strep/GlutaMax, 1% HEPES, 2% HI FBS) was dispensed at 5 μL/well
into assay plates and incubated at room temperature. Vero E6 (selected
for high ACE2 expression) was inoculated with SARS CoV-2 (USA_WA1/2020)
at 0.002 M.O.I. in media and quickly dispensed into assay plates as
4000 cells in 25 μL/well. Assay plates were incubated for 72
h at 37 °C, 5% CO2, 90% humidity. Then, 30 μL/well
of CellTiter-Glo (Promega) was dispensed and incubated for 10 min
at room temperature, and the luminescence signal was read on an EnVision
plate reader (PerkinElmer). The MOI of 0.002 was selected during assay
optimization to achieve 95% cell death at 72 h postinfection. An ATP
content cytotoxicity assay was conducted with the same protocol as
the CPE assay, but without the addition of SARS-CoV-2 virus.
Chen C.Z., Xu M., Pradhan M., Gorshkov K., Petersen J.D., Straus M.R., Zhu W., Shinn P., Guo H., Shen M., Klumpp-Thomas C., Michael S.G., Zimmerberg J., Zheng W, & Whittaker G.R. (2020). Identifying SARS-CoV-2 Entry Inhibitors through Drug Repurposing Screens of SARS-S and MERS-S Pseudotyped Particles. ACS Pharmacology & Translational Science, 3(6), 1165-1175.
Publication 2020
ACE2 protein, human Biological Assay Cell Culture Techniques Cell Death Cells Culture Media Cytotoxin HEPES Humidity Intestinal Atresia, Multiple Luminescence Promega SARS-CoV-2 Severe acute respiratory syndrome-related coronavirus Streptococcal Infections Sulfoxide, Dimethyl
3
Detailed Metabolite Profiling using UPLC-MS
The organic extracts of the tissue
samples were reconstituted in 500 μL of the solvent mixture
of water/ACN/isopropanol (ISP) (1:1:2) and transferred into Total
Recovery vials (Waters Corp, USA), after centrifugation for 10 min
at 5000g and 4 °C.
UPLC separation was
conducted using an Acquity UPLC System (Waters Corp, USA). An Acquity
UPLC CSH C18 2.1 × 100 mm, 1.7 μm, column (Waters Corp,
USA) was used. Column temperature was set at 55 °C and flow rate
at 0.4 mL/min. Mobile phase A consisted of ACN/water (60:40) and mobile
phase B ISP/ACN (90:10). In both solutions ammonium formate was diluted
to 10 mM and formic acid to 0.1%. The elution gradient was set as
follows: 60–57% A (0.0–2.0 min), 57–50% A (2.0–2.1
min; curve 1), 50–46% A (2.1–12.0 min), 46–30%
A (12.0–12.1 min; curve 1), 30–1% A (12.1–18
min), 1–60% A (18.0–18.1 min), 60% A (18.1–20.0
min). Injection volumes of 3 and 7 μL were used for positive
and negative ionization modes, respectively. The autosampler was set
at 4 °C. Mass spectrometry was performed using a Xevo G2 QTof
(Waters MS Technologies, U.K.) with an electrospray ionization (ESI)
source. Both MS and MSE data scans were acquired. MS conditions
can be found in Supporting Information.
The same QC strategy was followed as for the HILIC-UPLC-MS analysis.
Vorkas P.A., Isaac G., Anwar M.A., Davies A.H., Want E.J., Nicholson J.K, & Holmes E. (2015). Untargeted UPLC-MS Profiling Pipeline to Expand Tissue Metabolome Coverage: Application to Cardiovascular Disease. Analytical Chemistry, 87(8), 4184-4193.
Publication 2015
Centrifugation formic acid formic acid, ammonium salt Intestinal Atresia, Multiple Isopropyl Alcohol Mass Spectrometry Radionuclide Imaging Solvents
4
Recombinant Expression and Purification of ChdC
CdChdC gene
(DIP1394) was synthesized and subcloned into a pD441-NH vector (ATUM,
Newark, California) containing an N-terminal His-tag. The synthesized
vector was complemented with a HRV 3C protease cleavage site between
the tag and the gene of interest by overlap extension PCR. Recombinant
protein production was performed in E. coli Tuner (DE3) (Merck/Novagen, Darmstadt, Germany) cells in LB-medium
containing 100 μg mL–1 kanamycin. A 500 mL
portion of the medium was inoculated with 1 mL of overnight culture
and cultivated in shaking flasks at 37 °C and 180 rpm for 3 h.
The temperature was lowered to 16 °C prior to induction with
0.5 mM isopropyl-β-d-thiogalactopyranoside (IPTG) and
kept for further cultivation overnight. Cells were harvested by centrifugation
(4 °C, 2700g, 30 min) and resuspended in 50
mL of lysis buffer (50 mM phosphate buffer pH 7.4, with 500 mM NaCl,
5% glycerol, and 0.5% Triton X-100) and lysed by three 1 min cycles
of pulsed ultrasonication (1 s of sonication with 1 s between pulses,
90% power) on ice. The resulting lysate was centrifuged for 30 min
at 38720g and 4 °C, and the supernatant was
filtered (0.45 μm pore sized filter). For purification, the
filtrate was loaded on a His-trap affinity column (5 mL, GE Healthcare)
pre-equilibrated with binding buffer (50 mM phosphate buffer, pH 7.4,
with 500 mM NaCl) on an ÄKTA system. The column was further
washed with binding buffer and equilibrated with cleavage buffer (50
mM Tris-HCl with 150 mM NaCl and 1 mM EDTA). The protein was eluted
with cleavage buffer after on-column cleavage from the His-tag with
a likewise His-tagged HRV 3C PreScission Protease overnight at 4 °C.
The eluate was concentrated using a centrifugal filter unit (Amicon
Ultra-15, Merck Millipore Ltd., Tullagreen, Carrigtwohill Co. Cork,
Ireland, 50 kDa cutoff) by centrifuging at 4500 g for 10–20 min in order to attain a volume of 1–3 mL
for further purification via size exclusion chromatography (SEC) using
a HiLoad 16/600 Superdex 200 pg, GE Healthcare column equilibrated
with 100 mM phosphate buffer pH 7.4, with 100 mM NaCl. The collected
fractions were pooled and again concentrated via a centrifugal filter
unit to a concentration of 750–1000 μM. Finally, the
solution was stored at −80 °C in 20 μL aliquots. CdChdC was produced in its apo form and supplemented with
coproheme directly before analysis in order to avoid unintended decarboxylation
activity during storage.
For crystallization and circular dichroism
experiments, the enzyme was
reconstituted with iron coproporphyrin III chloride (coproheme; Frontier
Scientific, Logan, UT, USA) prior to SEC purification, and the SEC-purified
protein was directly used for experiments. Mutants of CdChdC were produced by site-directed mutagenesis using the previously
described vector as a template and expressed and purified equally
(Table 1).
Michlits H., Lier B., Pfanzagl V., Djinović-Carugo K., Furtmüller P.G., Oostenbrink C., Obinger C, & Hofbauer S. (2020). Actinobacterial Coproheme Decarboxylases Use Histidine as a Distal Base to Promote Compound I Formation. ACS Catalysis, 10(10), 5405-5418.
Publication 2020
Buffers Cells Centrifugation Cloning Vectors Complement C3c coproporphyrin III Crystallization Cytokinesis Edetic Acid Enzymes Escherichia coli ferric chloride GE-100 Genes Glycerin Intestinal Atresia, Multiple Kanamycin LB-100 Molecular Sieve Chromatography Mutagenesis, Site-Directed Peptide Hydrolases Phosphates Proteins Pulses Sodium Chloride Triton X-100 Tromethamine
5
Metabolomics Analysis of Leukemic Cells

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Publication 2018
Acetate acetonitrile Ammonium ammonium acetate Buffers Cells Cold Temperature formic acid High-Performance Liquid Chromatographies Intestinal Atresia, Multiple Mass Spectrometry Methanol Stem Cells Tandem Mass Spectrometry

Most recents protocols related to «Intestinal Atresia, Multiple»

1
Protease Activity Measurement at Different pH
The proteolytic activity was measured
by a modification of the method of Anson.21 (link) To test the protease activity at different pH values, 1% (w/v) bovine
serum albumin was diluted in Na acetate buffer (100 mM, pH 5), Na
phosphate buffer (100 mM, pH 7), and Tris-HCl buffer (100 mM, pH 9).
Then, 50 μL of crude extract was added to 500 μL of each
substrate solution and incubated at 37 °C for 2, 4, and 24 h.
The reaction was stopped by adding 500 μL of 10% (w/v) prechilled
trichloroacetic acid (TCA); the mixture was cooled on ice, and the
test tubes were centrifuged at 20,000g for 10 min
at 4 °C to remove the unhydrolyzed protein. The absorbance of
the clear supernatant solution was measured at 280 nm using an ultraviolet–visible
(UV–vis) microplate reader (EnSight multimode reader, PerkinElmer
Waltham). One unit (U) was arbitrarily defined as the amount of enzyme
that produces an increase in absorbance of 0.001 per minute under
the assay condition,22 (link),23 (link) measured as the quantity of TCA-soluble
products.24 (link)
Bulgari D., Alias C., Peron G., Ribaudo G., Gianoncelli A., Savino S., Boureghda H., Bouznad Z., Monti E, & Gobbi E. (2023). Solid-State Fermentation of Trichoderma spp.: A New Way to Valorize the Agricultural Digestate and Produce Value-Added Bioproducts. Journal of Agricultural and Food Chemistry, 71(9), 3994-4004.
Full text: Click here
Publication 2023
Acetate Acids Albumins Biological Assay Buffers Complex Extracts Intestinal Atresia, Multiple Peptide Hydrolases Proteins Proteolysis Tromethamine
2
Synthesis of Bimetallic Ru-Pd/C Catalyst
A 50
mL flask was sequentially loaded with a magnetic stir bar, 5 mg of
carbon support, 50 mL of DI water, and Na2PdCl4 stock solution. The mixture was sonicated for 1 min to disperse
the carbon particles and stirred at 350 rpm for 4 min to allow the
adsorption of PdII. The flask was then capped by a rubber
stopper. A 16 G needle penetrating the stopper was connected to the
H2 gas supply (2–3 mL min–1),
and the needle tip was pushed under water. The other needle had the
tip above the water as the gas outlet to the atmosphere. After 5 min
of H2 sparging at 20 °C, all adsorbed PdII was reduced to Pd0.28 (link) After
that, the Pd0/C suspension was added with RuCl3 stock solution and sparged with H2 for another 10 min
at 20 °C to reduce adsorbed RuIII to Ru0, yielding Ru0–Pd0/C.
Gao J., Xie S., Liu F, & Liu J. (2023). Preparation and Synergy of Supported Ru0 and Pd0 for Rapid Chlorate Reduction at pH 7. Environmental Science & Technology, 57(9), 3962-3970.
Publication 2023
Atmosphere Carbon Intestinal Atresia, Multiple Needles
3
Labeling and Visualizing Cell Coculture on Fibrinogen Scaffolds
To distinguish between both cell types on a fibrinogen scaffold
in the coculture setup, they were labeled with lipophilic cell membrane
dyes before seeding. HDFs were labeled with Invitrogen Vybrant DiI
Cell-Labeling Solution (ThermoFisher), and HaCaTs were labeled with
Invitrogen Vybrant DiO Cell-Labeling Solution (ThermoFisher). Following
trypsination, cells were centrifuged, and the cell pellet was subsequently
resuspended in prewarmed (37 °C) serum-free cell culture medium
DMEM, before diluting the suspensions to a cell density of 60 000
cells/mL. These cells were incubated with 5 μL of the respective
cell labeling solution per milliliter of cell suspension for 15 min
at 37 °C in the dark. The labeled cell suspensions were centrifuged
at 1500 rpm for 5 min, the aspirated supernatant and cell pellet were
then gently resuspended in prewarmed (37 °C) cell culture medium
DMEM with 10% FBS. These centrifugation and resuspension steps were
repeated two more times before the labeled cells were seeded onto
the scaffolds at a density of 30 000 cells/cm2.
To obtain a layered skin construct, DiI-HDFs (red) were seeded onto
the scaffolds using the above-described procedure and cultivated at
37 °C and 5% CO2 for 3 days before the seeding of
DiO-HaCaTs (green) by the same procedure on top of HDFs. Six days
after the seeding of HaCaTs, cells on the scaffolds were fixated with
a 2% (v/v) solution of PFA in PBS for 30 min at room temperature.
All samples were subsequently mounted onto glass slides with Prolong
Diamond antifade medium with DAPI and cured overnight at room temperature.
Stained cells on fibrinogen scaffolds were imaged using z-stacking
at 60× magnification in our inverted fluorescence microscope
with appropriate filter settings (λex = 540 nm and λem = 565 nm for DiI
orange-red, λex = 488 nm and λem = 520 nm for DiO green, and λex = 330–380
nm and λem = 435–485 nm for DAPI blue). For
z-stack analysis, we recorded 10 to 12 images over a total z-height
of up to 6 μm with a step size of 500 nm.
Joshi A., Nuntapramote T, & Brüggemann D. (2023). Self-Assembled Fibrinogen Scaffolds Support Cocultivation of Human Dermal Fibroblasts and HaCaT Keratinocytes. ACS Omega, 8(9), 8650-8663.
Publication 2023
Cell Culture Techniques Cells Centrifugation Coculture Techniques DAPI Fibrinogen Fluorescence Intestinal Atresia, Multiple Serum Skin
4
Isolation and Enrichment of Murine Bone Marrow Cells
Mice were handled and euthanized by cervical dislocation according
to guidelines and animal protocols approved by the German authorities.
Using forceps and scissors, the animal’s legs and spines were
dissected. To isolate femurs, tibiae, iliae, and vertebrae, connective
tissue was removed with a scalpel. The isolated bones were then kept
on ice in PBS (Sigma, Cat# D8537)-filled 6-well plates until all bones
were collected.
Note that cells must be kept on ice from the
moment the bones are isolated from the mouse. Bones were gently crushed
twice with 5 mL of ice-cold PBSs using a mortar and pestle until they
turned completely white. The cell suspension was then filtered through
a 40 μm sterile filter (Corning, Cat# 352340) into a 50 mL falcon
tube and kept on ice.
Next, the lysis of erythrocytes was performed.
Briefly, the cell
suspension was centrifuged at 400g for 5 min at 4
°C, followed by the removal of the supernatant. The pellet was
then resuspended into 2 mL of ice-cold ACK lysis buffer (Lonza, Cat#
10-548E) and incubated on ice for 5 min (incubation time may be increased
up to 10 min depending on the size of the pellet). The reaction was
then stopped by adding 10 mL of ice-cold PBS. Then, the cells were
centrifuged at 400g for 5 min at 4 °C, and the
supernatant was discarded.
Lineage negative (Lin−) cells
were enriched using the Dynabeads
Untouched Mouse CD4 Cells Kit (Invitrogen, Cat# 11415D). Briefly,
cells were resuspended in a 500 μL of lineage cocktail (100
μL of the cocktail provided in the kit plus 400 μL of
PBS) and transferred into a 2 mL tube. The incubation step was performed
for 35 min on a rotating wheel at 4 °C. Meanwhile, 400 μL
of Dynabeads were washed twice with 1 mL of PBS on a magnet and resuspended
in 500 μL of PBS.
Next, the cells were washed with 12
mL of ice-cold PBS in a 15
mL falcon tube and centrifuged at 400g for 5 min
at 4 °C. After the removal of the supernatant, cells were resuspended
in 1 mL of ice-cold PBS and incubated together with the prepared Dynabeads
for 20 min on a rotating wheel at 4 °C.
For depletion of
lineage-positive cells, the suspension was incubated
5 min on ice on the depletion magnet until the solution cleared. The
entire supernatant was then transferred into a new FACS tube and kept
on ice. Then, 1 mL of ice-cold PBS was added to the beads and mixed
by vortexing. The depletion step was then repeated, and the two supernatants
combined. Then, the cell suspension was centrifuged at 400g for 5 min at 4 °C, and the supernatant was removed.
Schönberger K., Mitterer M., Glaser K., Stecher M., Hobitz S., Schain-Zota D., Schuldes K., Lämmermann T., Rambold A.S., Cabezas-Wallscheid N, & Buescher J.M. (2023). LC-MS-Based Targeted Metabolomics for FACS-Purified Rare Cells. Analytical Chemistry, 95(9), 4325-4334.
Full text: Click here
Publication 2023
Animals Bones Buffers CD4 Positive T Lymphocytes Cells Cold Temperature Erythrocytes Femur Forceps Intestinal Atresia, Multiple Joint Dislocations Leg Mus Neck Sterility, Reproductive Tibia Vertebra Vertebral Column
5
Murine Peripheral Blood Cell Isolation
According to guidelines and animal protocols approved by the German
authorities, mice were handled and bled from the cheek vein to withdraw
50 μL of peripheral blood. The blood was collected in an EDTA-coated
2 mL tube and kept on ice. Note that cells must be kept on ice from
the moment of isolation.
Lysis of erythrocytes was performed
by adding 300 μL of ice-cold ACK lysis buffer (Lonza, Cat# 10-548E)
and incubating on ice for 10 min after transferring the cells into
a conical FACS tube. The cells were then centrifuged at 400g for 5 min at 4 °C, and the supernatant was discarded.
A second (and optional third) round of erylysis was performed until
a defined pellet was visible. The reaction was stopped by adding 500
μL of ice-cold PBS (Sigma, Cat# D8537) to each sample. Following
an additional centrifugation step at 400g for 5 min
at 4 °C, and the supernatant was discarded.
Schönberger K., Mitterer M., Glaser K., Stecher M., Hobitz S., Schain-Zota D., Schuldes K., Lämmermann T., Rambold A.S., Cabezas-Wallscheid N, & Buescher J.M. (2023). LC-MS-Based Targeted Metabolomics for FACS-Purified Rare Cells. Analytical Chemistry, 95(9), 4325-4334.
Full text: Click here
Publication 2023
Animals BLOOD Buffers Cells Centrifugation Cheek Cold Temperature Edetic Acid Erythrocytes Intestinal Atresia, Multiple isolation Mus Retinal Cone Veins

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More about "Intestinal Atresia, Multiple"

Intestinal Atresia, Multiple is a rare congenital condition characterized by the presence of multiple obstructions or narrowings in the small and/or large intestine.
This disorder, also known as intestinal atresia or intestinal stenosis, can lead to complications such as intestinal blockages, malnutrition, and growth delays if left untreated.
Effective research protocols are crucial for advancing our understanding and management of this complex gastrointestinal condition.
PubCompare.ai's AI-driven platform helps researchers quickly identify the most accurate and reproducible methods from literature, preprints, and patents, enhancing research efficiency and elevating Intestinal Atresia, Multiple studies.
By leveraging natural language processing and machine learning algorithms, the platform can analyze a vast corpus of scientific publications to uncover the most reliable and effective research protocols for studying this disorder.
Researchers investigating Intestinal Atresia, Multiple may also utilize additional laboratory techniques and tools, such as Bovine serum albumin (BSA) for protein quantification, Phosphate-buffered saline (PBS) for solution preparation, Opti-MEM media for cell culture, DAPI for nuclear staining, Axio Observer Z1 microscope for imaging, Q Exactive mass spectrometer for proteomic analysis, Paraformaldehyde for tissue fixation, and Zetasizer Nano ZS for particle size analysis.
The incorporation of these well-established methods and technologies can further enhance the quality and reproducibility of Intestinal Atresia, Multiple research.
By leveraging PubCompare.ai's AI-powered protocol optimization and the strategic use of complementary laboratory techniques, researchers can elevate their studies on Intestinal Atresia, Multiple, leading to a deeper understanding of this rare but critical condition and, ultimately, improved patient outcomes.