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Serine Endopeptidases

Serine endopeptidases are a class of proteolytic enzymes that cleave peptide bonds within proteins, with a serine residue playing a critical role in the catalytic mechanism.
These enzymes are involved in a variety of biological processes, including digestion, blood coagulation, and the immune response.
They are found in a wide range of organisms, from bacteria to mammals, and have been extensively studied for their therapeutic and industrial applications.
Serine endopeptidases exhibit a diverse range of substrate specifities and catalytic mechanisms, making them an important area of research for understanding protein structure, function, and regulation.

Most cited protocols related to «Serine Endopeptidases»

Statistical Coupling Analysis of Protein Families

Multiple sequence alignments were obtained from previous work [10 (link)] or from the PFAM database (release 27.0, accession codes PF00071 (G proteins), PF00186 (DHFR), and PF13354 (class A β-lactamases)), and were subject to pre-processing with default parameter values as described in Box 1. Reference sequences/structures selected for each family were rat trypsin (PDB 3TGI), human Ras (PDBs 5P21 and 4Q21), E. coli DHFR (PDB 1RX2), and E. coli TEM-1 β-lactamase (PDB 1FQG), and with sub-sampling to the number of effective sequences, yielded the following final alignment statistics: S1A serine proteases (928 effective sequences by 205 positions), G proteins (3366 effective sequences by 158 positions), DHFR (1157 effective sequences by 151 positions), β-lactamase (497 effective sequences by 200 positions). All calculations were carried out using a new python implementation of the statistical coupling analysis (pySCA v6.2), following the algorithms described in Box 1 and in the main text. Step-by-step tutorials for executing the analysis for the four protein families are provided in the S3 Text and accompany the toolbox distribution. The pySCA toolbox is available for download through GitHub (https://github.com/reynoldsk/pySCA), and with online instructions at http://reynoldsk.github.io/pySCA.

Rivoire O., Reynolds K.A, & Ranganathan R. (2016). Evolution-Based Functional Decomposition of Proteins. PLoS Computational Biology, 12(6), e1004817.

Publication 2016

beta-Lactamase beta-lactamase TEM-1 Escherichia coli GTP-Binding Proteins Homo sapiens Proteins Python Sequence Alignment Serine Endopeptidases Trypsin

Identifying Honey Bee Immune Genes Using Bioinformatics

Immune-gene candidates from other insects were used in several ways to query the honey bee genome, primarily using the Blast family of search functions (http://www.ncbi.nlm.nih.gov). Most searches were initiated by BlastP queries against the consensus protein list (GLEAN3, derived from HBGP assembly 2.0) using BlastP and algorithms (BLOSUM and PAM variants) appropriate to gene size and structure. Honey bee orthologues were also identified by searching honey bee genome assemblies 2.0 and 3.0 directly using TBLASTN and either local databases or the BeeBase Blast server (http://racerx00.tamu.edu/blast/blast.html). Searches for missing genes were also carried out a on smaller coverage set of honey bee contigs that were too short to be included in the assembly, as well as the unassembled reads from the project (http://www.hgsc.bcm.tmc.edu/projects/honeybee/).
Given honey bee candidates, searches were repeated in the hope of identifying paralogues missed by interspecific comparisons. PSI-Blast was used to identify honey bee genes on the basis of conserved domains, followed by RPS-Blast to confirm the significance of these domain matches. Putative matches were aligned and, in the case of serine proteases, scavenger receptors and C-type lectins, screened for additional motifs using pfam categories (http://sanger.ac.uk/software/pfam). Tentative matches were aligned and checked for gene-prediction errors (in the case of genes from the official protein list) as part of the annotation of immune candidate genes for the Honey Bee Genome Project (Honey Bee Genome Sequencing Consortium, 2006 ). All protein matches were ported to Apis mellifera assembly 3.0 using the alignment program BLAT (Jim Kent, University California, Santa Cruz) to establish scaffold locations (Supplementary Material Table S1).

Evans J.D., Aronstein K., Chen Y.P., Hetru C., Imler J.L., Jiang H., Kanost M., Thompson G.J., Zou Z, & Hultmark D. (2006). Immune pathways and defence mechanisms in honey bees Apis mellifera. Insect Molecular Biology, 15(5), 645-656.

Publication 2006

Apis Gene Annotation Genes Genes, Insect Genome Honey Lectins, C-Type Proteins Scavenger Receptor Serine Endopeptidases

Angiotensin Peptides and Enzyme Assays

Blood was collected from participants in the seated position to obtain plasma renin activity, aldosterone, Ang II, and Ang-(1-7). For the peptide measurements, blood samples were collected immediately in a tube containing a cocktail of inhibitors and plasma was obtained and stored at −80 °C. The plasma was thawed on ice, extracted on Sep-Pak C18 columns (Waters Corp., Milford, Massachusetts, USA), and the eluted fractions assayed by an Ang II radioimmunoassay (RIA, Alpco, Salem, New Hampshire, USA; detection limit 0.8 pmol/l; intra-assay and inter-assay coefficients of variation 12 and 22%) and an Ang-(1-7) RIA (detection limit 2.8 pmol/l; intra-assay and inter-assay coefficients of variation 8 and 20%) [11 (link)]. Aldosterone content was determined in nonextracted plasma samples by RIA (Diagnostics Products, Los Angeles, California, USA; detection limit 28 pmol/l). Renin activity was directly determined in plasma samples using an RIA (Cisbio, Codolet, France; detection limit 4 pmol Ang I/l/hour). We calculated the Ang II-to-Ang-(1-7) ratio and the aldosterone-to-renin ratio for plasma samples.
Spot urine samples were collected, immediately acidified with HCl to prevent peptide degradation, and stored at −80 °C. The urine samples were thawed on ice, extracted on SepPak columns, and the urinary levels of Ang II and Ang-(1-7) quantified by RIAs. For the ACE and ACE2 assays, separate nonacidified urine samples were collected and were concentrated 10-fold on a Millipore 5000-Da cut-off filter with the assay buffer. ACE and ACE2 assays were conducted at 37 °C in 10 mmol/l of HEPES, 125 mmol/l of NaCl, and 10 µmol/l of ZnCl₂ (pH 7.4), with 0.02 ml of urine in a final volume of 0.2 ml with the indicated inhibitors and 0.02 ml of 0.1 mmol/l of either the quenched fluorescent substrate Mca-RPPGFSAFK-DNP for ACE or Mca-APK-DNP for ACE2 in a 96-well black plate. The fluorescence was read in a plate reader at an excitation λ of 328 nm and an emission λ of 393 nm. Blanks consisted of the substrate alone and the addition of the ACE inhibitor lisinopril or the ACE2 inhibitor MLN4760 for the ACE and ACE2 assays, respectively.
As the ACE and ACE2 substrates are not specific, the assays contained inhibitors against aminopeptidases (bestatin 10 µmol/l), carboxypeptidase A (benzyl succinate 10 µmol/l), serine peptidases (chymostatin 10 µmol/l), cysteine peptidases (para-chloro-mercuribenzoic acid 0.5 mmol/l), neprilysin (SCH39370, 10 µmol/l), and lisinopril (10 µmol/l) to measure ACE2 or MLN4760 (10 µmol/l) to measure ACE. ACE and ACE2 protein content (ng/mg creatinine) were based on human ACE and ACE2 standards obtained from R&D Systems (Minneapolis, Minnesota, USA). Standard enzymes were assayed under the same conditions as the urine samples. Fluorescent substrates for ACE and ACE2 were obtained from Enzo Life Sciences (VWR, Atlanta, Georgia, USA).
Creatinine levels in nonextracted urine samples were determined by a modified Jaffe assay traceable to isotope dilution mass spectrometry [11 (link)]. We calculated the urinary Ang II:Ang-(1-7) and ACE:ACE2 ratios and corrected Ang II and Ang-(1-7) concentrations and ACE and ACE2 concentrations by urine creatinine. If blood or urine sample results were below the laboratory’s lower limit of detection, the sample’s measurement was assigned a value calculated as the lower limit of detection divided by the square root of two [31 ].

South A.M., Nixon P.A., Chappell M.C., Diz D.I., Russell G.B., Jensen E.T., Shaltout H.A., O’Shea T.M, & Washburn L.K. (2018). Association between preterm birth and the renin–angiotensin system in adolescence: influence of sex and obesity. Journal of hypertension, 36(10), 2092-2101.

Publication 2018

ACE2 protein, human Acids Aldosterone Aminopeptidase Angiotensin-Converting Enzyme Inhibitors Angiotensin Converting Enzyme 2 angiotensin I (1-7) Biological Assay BLOOD Buffers Carboxypeptidase A chymostatin Creatinine Cysteine Proteases DA10 Diagnosis Enzymes Fluorescence HEPES Homo sapiens inhibitors Isotopes Lisinopril Mass Spectrometry MLN 4760 Neprilysin Peptides Plant Roots Plasma Radioimmunoassay Renin Sep-Pak C18 Serine Endopeptidases Sitting Sodium Chloride Succinate Technique, Dilution ubenimex Urine

SARS-CoV-2 Isolate Propagation and Titration

SARS-CoV-2 isolate Fin/25/20 (Gisaid: EPI_ISL_412971) from lineage B.1 was isolated from the nasopharyngeal sample of COVID-19 patient in Finland in February 2020. Swab sample in transport medium was inoculated onto African green monkey kidney epithelial VeroE6 cells at +37 °C and 5% CO₂ in culture medium (Eagle’s minimum essential medium (EMEM) supplemented with 2% fetal bovine serum (FBS), 0.6 μg/mL penicillin, 60 μg/mL streptomycin, 2 mM l-glutamine, 20 mM HEPES). Virus was propagated in VeroE6 cells for a total of three times. Subsequently, a VeroE6 clone expressing TMPRSS2, a serine protease essential for SARS-CoV-2 spike protein integrity, was generated (VeroE6-TMPRSS2-H10)⁴⁴. Fin/25/20 was further propagated twice in VeroE6-TMPRSS2-H10 cell line (virus isolate named FIN-25). Another 2020 isolate, SR121 from lineage B.1.463, isolated from a patient in Finland in September 2020, was isolated and propagated only in VeroE6-TMPRSS2-H10 cells⁴⁴. Variants 85HEL of B.1.1.7 lineage and HEL12-102 of B.1.351 lineage were isolated from patients in Finland as described²³ and further propagated only in VeroE6-TMPRSS2-H10 cells. VeroE6-TMPRSS2-H10 cells were maintained in D-MEM (Lonza) supplemented with 10% FBS, 2 mM l-glutamine (Gibco), and penicillin/streptomycin. For virus propagation in VeroE6-TMPRSS2-H10 cells, D-MEM supplemented with 2% FBS, 2 mM l-glutamine, and penicillin/streptomycin was used. Supernatants containing viruses were harvested, cell debris removed with centrifugation at 500×g for 5 min, and aliquots stored at −80 °C.
Fifty-percent tissue culture infective dose (TCID₅₀) of virus stocks was determined with endpoint dilution assay in VeroE6-TMPRSS2-H10 cells. Briefly, 50,000 cells per well were plated on 96-well tissue culture plates (Sarstedt), and the next day media was changed to infection media (2% FBS). Ten-fold virus dilutions in infection media were applied onto cells, and the plates were incubated for 3 days at +37 °C and 5% CO₂. Cells were fixed with 4% formaldehyde and stained with crystal violet. Virus dilution resulting in 50% cell death was determined to represent TCID₅₀ value of the stock virus. Virus propagations and end-point dilution assays were done in BSL-3 laboratory conditions.

Jalkanen P., Kolehmainen P., Häkkinen H.K., Huttunen M., Tähtinen P.A., Lundberg R., Maljanen S., Reinholm A., Tauriainen S., Pakkanen S.H., Levonen I., Nousiainen A., Miller T., Välimaa H., Ivaska L., Pasternack A., Naves R., Ritvos O., Österlund P., Kuivanen S., Smura T., Hepojoki J., Vapalahti O., Lempainen J., Kakkola L., Kantele A, & Julkunen I. (2021). COVID-19 mRNA vaccine induced antibody responses against three SARS-CoV-2 variants. Nature Communications, 12, 3991.

Publication 2021

Cell Death Cell Lines Cells Centrifugation Cercopithecus aethiops Clone Cells COVID 19 Eagle Epithelial Cells Fetal Bovine Serum Formaldehyde Genes, Viral Germ Cells Glutamine HEPES Infection Kidney Nasopharynx Patients Penicillins SARS-CoV-2 Serine Endopeptidases spike protein, SARS-CoV-2 Streptomycin Technique, Dilution Tissues TMPRSS2 protein, human Violet, Gentian Virus Virus Diseases

Extraction and Purification of Crotalus Venom

CEVAP maintains a serpentarium for the breeding and milking of specimens with authorization and registration as a scientific breeder for research purposes at the Brazilian Institute of the Environment and Natural Resources (IBAMA) (protocol number 02001.005670/90–77), in addition to having authorization for the management of wild fauna (no. 3507.7263/2012-SP). Standard operational protocols (SOPs) are followed rigidly in environments where Crotalus durissus terrificus snakes are housed for venom production, according to the international good management practices to ensure the quality and purity required for the production of biopharmaceuticals (17 (link), 24 (link)). Further information on CEVAP is provided at https://youtu.be/CPcs4ity-Uw.
First, the venom was extracted and filtered. Then, the protein dosage was evaluated, followed by lyophilization and storage in a refrigerator between +4 and +8°C. Subsequently, the venom was subjected to fractionation via high-performance liquid chromatography (HPLC). Lastly, the purity of the thrombin-like enzyme (serine protease, gyroxin) component was evaluated using sequencing and mass spectrometry as described by Barros et al. (25 (link)). Further information on HFS is provided at https://youtu.be/y6ho6M0amA8.

Abbade L.P., Barraviera S.R., Silvares M.R., Lima A.B., Haddad G.R., Gatti M.A., Medolago N.B., Rigotto Carneiro M.T., dos Santos L.D., Ferreira RS J.r, & Barraviera B. (2021). Treatment of Chronic Venous Ulcers With Heterologous Fibrin Sealant: A Phase I/II Clinical Trial. Frontiers in Immunology, 12, 627541.

Publication 2021

Biological Factors Crotalus Enzymes Fractionation, Chemical Freeze Drying gyroxin High-Performance Liquid Chromatographies Mass Spectrometry Proteins Serine Endopeptidases Snakes Thrombin Venoms

Most recents protocols related to «Serine Endopeptidases»

Reproductive Organ Protease and Phenoloxidase Regulation in Leafhopper

The reproductive organs were individually dissected from the newly emerged male adults of RdFV and RGDV co-positive R. dorsalis population, and the relative transcript levels of clip-domain serine protease genes and PPO were examined by RT-qPCR assays. The male reproductive organs were also examined to determine the conversion of PPO to PO in western blot assays using PPO and histone H3 antibodies (0.5 μg/μl). A pool of 30 RGDV-positive males was used for each replicate in RT-qPCR and western blot assays, respectively. The experiment was conducted in at least three replicates for RT-qPCR and western blot assays. To analyze effect of RGDV infection on PO activity, the reproductive organs dissected from approximate 100 newly emerged males were homogenized with the His-Mg buffer (0.1 M histidine, 0.01 M MgCl₂, pH 6.2) buffer in liquid nitrogen. The supernatant was gently mixed with 1 mM dopamine in 10 mM Tris-HCl buffer (pH 8.0) in a 96-well plate at room temperature for 5 min. Enzyme activity was measured using the phenoloxidase kit (Geruisi, G0146W) according to the manufacturer’s protocol. To analyze the effect of M. luteus infection on PO activity, freeze-dried M. luteus was dissolved in water, and then microinjected in dose of ~23 ng/leafhopper into newly emerged males. At 24-h post microinjection, the reproductive organs of approximate 100 RGDV-infected or M. luteus-treated males were dissected and tested for PO activity.
We then tested the effect of knockdown of PPO or HongrES1 expression on PO activity and RGDV infection. The newly emerged male adults of RdFV and RGDV co-positive R. dorsalis population were microinjected with dsGFP, dsPPO or dsHongrES1 (~200 ng/leafhopper). The male reproductive organs of these tested leafhoppers were individually collected and dissected for RT-qPCR and western blot assays to determine the effect of dsRNAs on the expression levels of HongrES1, PPO, or RGDV P8, and the conversion of PPO to active PO, as well as PO activity. A pool of 30 males was used for each replicate in RT-qPCR and western blot assays, respectively. A pool of 100 males was tested for each replicate in PO activity. The experiment was conducted in three replicates for RT-qPCR and western blot assays, as well as PO activity tests.

Wan J., Liang Q., Zhang R., Cheng Y., Wang X., Wang H., Zhang J., Jia D., Du Y., Zheng W., Tang D., Wei T, & Chen Q. (2023). Arboviruses and symbiotic viruses cooperatively hijack insect sperm-specific proteins for paternal transmission. Nature Communications, 14, 1289.

Publication 2023

Adult Antibodies Biological Assay Buffers Clip DNA Replication Dopamine enzyme activity Freezing Genes Genitalia Histidine Histone H3 Infection Leafhoppers Magnesium Chloride Males Microinjections Monophenol Monooxygenase Nitrogen RNA, Double-Stranded Serine Endopeptidases Tromethamine Western Blot

Rice Protein Hydrolysis and Precipitation

Rice protein was obtained through precipitation per the method of Chen et al.^{45 (link)}. In brief, rice protein was enzymatically hydrolyzed with a 2:100 (v/v) enzyme-to-substrate ratio to obtain hydrolysates. Protease (Alcalase, EC 3.4.21.62, serine endo-peptidase, 2.4 AU-A/g; Healthmate, Changhua, Taiwan) was used and the hydrolysis conditions involved setting pH 8.0 at 50 ± 5 °C. After a 4-h reaction period, the protease was inactivated through heating at 85 °C for 15 min. After centrifugation (5000 rpm, 4 °C) for 15 min, the supernatant was lyophilized and stored at − 20 °C before use.

Chen H.J., Dai F.J., Chen C.Y., Fan S.L., Zheng J.H., Chau C.F., Lin Y.S, & Chen C.S. (2023). Effects of molecular weight fraction on antioxidation capacity of rice protein hydrolysates. Scientific Reports, 13, 3464.

Publication 2023

Centrifugation Endometriosis Enzymes Hydrolysis Oryza sativa Peptide Hydrolases Proteins Serine Endopeptidases Subtilisin Carlsberg

Caseinolytic Proteolytic Activity Assay

Total proteolytic activity was analyzed using the caseinolytic activity examination proposed by Kunitz [24 (link)] with some modifications. 4% casein solution was prepared by dissolving 4 g of casein in a mix of 80 ml 0.05 M phosphate buffer (pH 7.4) and 1.6 ml 1 M NaOH. The obtained mixture was left at room temperature for 40 min, and after that it was boiled in a hot water bath. The casein solution was cooled afterwards, pH 7.4 was adjusted by 1 M NaOH, and the total volume of 100 ml was adjusted by phosphate buffer. About 500 μL of homogenate was diluted with 0.05 M phosphate buffer (pH 7.4) to a total volume of 1 mL. After that, 1 mL of 4% casein solution was added, and the obtained mixture was incubated at 37°C for 30 min. The reaction was stopped by a 3 mL addition of 15% TCA, after which samples were centrifuged at 1000 g for 30 min. The supernatant was collected and used for absorbance measurement at 280 nm. The control sample mixture consisted of casein, phosphate buffer, and TCA in identical proportions. In order to evaluate metalloproteases and serine proteases' activities, 0.2 M ethylenediaminetetraacetic acid (EDTA) and 0.2 M phenylmethylsulfonyl fluoride (PMSF), respectively were added to the reaction mixture. Total proteolytic activity was expressed as rel. units·(mg of protein)⁻¹.

Gunas V., Maievskyi O., Raksha N., Vovk T., Savchuk O., Shchypanskyi S, & Gunas I. (2023). The Activity of Metalloproteases and Serine Proteases in Various Organs after Leiurus macroctenus Envenomation. Journal of Toxicology, 2023, 5262729.

Publication 2023

Bath Buffers Caseins Edetic Acid Metalloproteases Phenylmethylsulfonyl Fluoride Phosphates Proteolysis Serine Endopeptidases Synapsin I

Subtilisin-like Serine Protease Activity Assay

The activity of the subtilisin-like serine protease CJPRB was assayed by the Folin phenol method [41 ]. The tyrosine standard curve was obtained according to Zhuang’s method [41 ], with the equation y = 0.0047X + 0.00733, R² = 0.9955. The OD₆₈₀ value after the color development reaction was substituted into the standard curve equation to determine the concentration of tyrosine. Finally, the enzymatic activity of CJPRB was determined based on the tyrosine concentration. One unit of protease activity, expressed in U/mL, was defined as the amount of enzyme that produced 1 µg of tyrosine from the hydrolysis of casein in 1 min at 37 °C and pH 7.2.

Wang W, & Chen F. (2023). Role of the Subtilisin-like Serine Protease CJPRB from Cordyceps javanica in Eliciting an Immune Response in Hyphantria cunea. International Journal of Molecular Sciences, 24(4), 4170.

Publication 2023

Caseins enzyme activity Enzymes folin Hydrolysis Peptide Hydrolases Phenol Serine Endopeptidases Subtilisin Tyrosine

Docking Trypsin with Benzylic Inhibitor

A protein data bank (PDB) file of bovine trypsin complexed with a meta-cyano-benzylic inhibitor (1AUJ) served as the starting point for docking the selected compound to the most abundant serine peptidase protein [5 (link)]. After the PDB file was loaded into the PyMOL, the inhibitor and water molecules were removed, leaving the crystal structure of bovine trypsin ready for docking. After the ligands was imported into PyMOL as a mol.2 file, the sequence of 1AUJ was searched for the key amino acid residues of the active site. Both the protein and the ligand were added to the DockingPie 1.0.1. The Vina plugin console and the grid for docking were set with the appropriate coordinates (x = 24.98, y = 15.34, z = 20.88). The ligands were docked to the selected active site in 20 poses to obtain more accurate results of the binding energy.

Odžak R., Crnčević D., Sabljić A., Primožič I, & Šprung M. (2023). Synthesis and Biological Evaluation of 3-Amidoquinuclidine Quaternary Ammonium Compounds as New Soft Antibacterial Agents. Pharmaceuticals, 16(2), 187.

Publication 2023

Amino Acids Bos taurus Ligands Proteins Serine Endopeptidases Staphylococcal Protein A Trypsin

Top products related to «Serine Endopeptidases»

Trypsin by Merck Group

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Trypsin is a serine protease enzyme that is commonly used in cell biology and biochemistry laboratories. Its primary function is to facilitate the dissociation and disaggregation of adherent cells, allowing for the passive release of cells from a surface or substrate. Trypsin is widely utilized in various cell culture applications, such as subculturing and passaging of adherent cell lines.

293a cells by Thermo Fisher Scientific

Sourced in United States, Switzerland

293A cells are a type of human embryonic kidney cell line that are commonly used in cell biology research and the production of recombinant proteins. They are derived from human embryonic kidney cells and have been immortalized through the introduction of the adenovirus E1A and E1B genes. 293A cells have the ability to be easily transfected and can be used to produce high levels of recombinant proteins.

Streptomycin by Thermo Fisher Scientific

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Streptomycin is a broad-spectrum antibiotic used in laboratory settings. It functions as a protein synthesis inhibitor, targeting the 30S subunit of bacterial ribosomes, which plays a crucial role in the translation of genetic information into proteins. Streptomycin is commonly used in microbiological research and applications that require selective inhibition of bacterial growth.

Sodium hydroxide (naoh) by Merck Group

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Sodium hydroxide is a chemical compound with the formula NaOH. It is a white, odorless, crystalline solid that is highly soluble in water and is a strong base. It is commonly used in various laboratory applications as a reagent.

Trizol reagent by Thermo Fisher Scientific

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TRIzol reagent is a monophasic solution of phenol, guanidine isothiocyanate, and other proprietary components designed for the isolation of total RNA, DNA, and proteins from a variety of biological samples. The reagent maintains the integrity of the RNA while disrupting cells and dissolving cell components.

Bicinchoninic acid protein assay kit by Thermo Fisher Scientific

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The Bicinchoninic acid (BCA) protein assay kit is a colorimetric detection and quantification method used to measure the total protein concentration in a sample. The kit utilizes the reduction of Cu2+ to Cu+ by protein in an alkaline medium, and the subsequent colorimetric detection of the Cu+ by bicinchoninic acid.

Transit lt1 by Mirus Bio

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TransIT-LT1 is a cationic lipid-based transfection reagent designed for efficient delivery of DNA, RNA, and other macromolecules into a variety of cell types. It is a versatile and reliable tool for research applications.

Dq gelatin by Thermo Fisher Scientific

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DQ gelatin is a laboratory product used for the measurement and quantification of enzymatic activity. It is a substrate that can be cleaved by specific enzymes, allowing for the assessment of their catalytic properties and function.

Platinum gp cells by Cell Biolabs

Sourced in United States

Platinum-GP cells are a stable packaging cell line designed for the production of retroviral vectors. They express gag, pol, and env genes necessary for the assembly and release of retroviral particles.

Dulbecco modified eagle medium (dmem) by Merck Group

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DMEM (Dulbecco's Modified Eagle's Medium) is a commonly used cell culture medium formulated to support the growth and maintenance of various cell lines. It provides a balanced salt solution and essential nutrients required for cell proliferation. DMEM is suitable for use in a wide range of cell culture applications.

What are the main functions and roles of serine endopeptidases in biological processes?

Serine endopeptidases play crucial roles in a variety of biological processes, such as digestion, blood coagulation, and immune response. They are involved in the cleavage of peptide bonds within proteins, with a serine residue playing a critical part in the catalytic mechanism. These enzymes exhibit a diverse range of substrate specificities, making them important for understanding protein structure, function, and regulation.

What are some common challenges or limitations researchers may face when working with serine endopeptidases?

Researchers may encounter challenges in identifying the most effective protocols and products for their specific serine endopeptidase studies. With the vast amount of literature, pre-prints, and patents available, it can be time-consuming and difficult to pinpoint the most relevant and reliable information. Additionally, the diverse catalytic mechanisms and substrate specificities of serine endopeptidases can make it challenging to ensure reproducibility and accuracy in experimental results.

How can PubCompare.ai help optimize serine endopeptidase research?

PubCompare.ai is an AI-driven platform that can assist researchers in their serine endopeptidase studies. It allows you to screen protocol literature more efficiently and leverage AI to pinpoint critical insights. The platform's AI-driven analysis can help identify the most effective protocols related to serine endopeptidases, enabling you to choose the best option for your research goals and enhance reproducibility and accurracy. This innovative tool can save time and improve the quality of your serine endopeptidase research.

Are there different types or variations of serine endopeptidases, and how do they differ?

Yes, serine endopeptidases exhibit a diverse range of substrate specifities and catalytic mechanisms. Some common variations include digestive enzymes like trypsin and chymotrypsin, which are involved in food digestion, as well as blood clotting factors like thrombin and plasmin, which play a role in the coagulation process. Additionally, serine protease inhibitors, such as serpins, regulate the activity of serine endopeptidases and are important for maintaining homeostasis. Understaning these variations is crucial for targeting specific serine enpoptidases in therapeutic and industrial applications.

What are some key applications of serine endopeptidases?

Serine endopeptidases have a wide range of applications, both in theruapetic and industrial settings. In medicine, they are used in the treatment of blood clotting disorders, inflammatory conditions, and even certain cancers. In the food industry, they are employed in cheese production and meat tenderization. Additionally, serine endopeptidases have potential applications in the development of novel biocatalysts and biosensors for various biotechnological processes. The versatility of these enzymes makes them an important area of research and development.

More about "Serine Endopeptidases"

Serine proteases, serine peptidases, and serine endopeptidases are a class of proteolytic enzymes that play critical roles in a variety of biological processes, including digestion, blood coagulation, and the immune response.
These enzymes are characterized by the presence of a serine residue in their active site, which is essential for their catalytic mechanism.
Serine proteases are found across a wide range of organisms, from bacteria to mammals, and have been extensively studied for their therapeutic and industrial applications.
They exhibit a diverse range of substrate specificities and catalytic mechanisms, making them an important area of research for understanding protein structure, function, and regulation.
Some common examples of serine proteases include trypsin, which is involved in the digestion of proteins, and thrombin, which plays a key role in blood clotting.
Serine proteases can also be found in the venom of certain animals, such as snakes, where they contribute to the toxic effects.
In research settings, serine proteases are often studied using cell lines like 293A cells, which are known to express these enzymes.
Researchers may utilize various techniques and reagents, such as streptomycin, sodium hydroxide, TRIzol reagent, bicinchoninic acid protein assay kits, TransIT-LT1 transfection reagent, and DQ gelatin, to investigate the structure, function, and regulation of serine proteases.
Advances in the understanding of serine proteases have led to the development of therapeutic and industrial applications, including the use of serine protease inhibitors in the treatment of various diseases and the utilization of these enzymes in the production of pharmaceutical and industrial products.
The versatility and importance of serine proteases make them a crucial area of research in the fields of biochemistry, molecular biology, and biotechnology.