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Seminal Plasma

Seminal plasma is the fluid portion of semen, excluding the spermatozoa.
It is composed of secretions from the seminal vesicles, prostate, and other accessory genital glands.
Seminal plasma provides a supportive and nutritive environment for the spermatozoa and facilitates their motility and fertilizing capacity.
Analyzing the composition and properties of seminal plasma is crucial for understanding male fertility and reproductive health.
Researchers can utilize PubCompare.ai's AI-driven platform to optimize their seminal plasma studies, locate the best protocols, and enhance reproducibility and accuracy in their work.

Most cited protocols related to «Seminal Plasma»

1
Expanding the Human PeptideAtlas Through Data Integration
We judiciously added publicly available data to PeptideAtlas for the specific purpose of increasing the number of protein identifications. Our aim was to obtain a large number of new identifications by adding a moderate amount of data. First we added two large plasma datasets and one large cell line dataset that had recently been contributed. We then looked for promising data in the GPMDB using two strategies: (a) reviewing Datasets of the Week, which tend to be high quality datasets, and selecting those which were very high quality, used new MS technology, had low-complexity samples due to a filtering method, or used cell types or tissue types not yet in PeptideAtlas, and (b) using an automated process to select GPMDB datasets containing many higher-confidence identifications for proteins not yet in PeptideAtlas. We also considered all articles published in Molecular and Cellular Proteomics that referenced the Tranche data repository 16 in the main text, and selected from these datasets using the same criteria we used for GPM Datasets of the Week.
We selected a total of 27 datasets and were able to obtain 17 in full or almost in full (four from the authors, two from PRIDE, and 11 from Tranche) and four in large part (from Tranche). The remaining six datasets had been deposited in Tranche but could not be retrieved after multiple attempts, emphasizing the need for a stably funded publicly accessible repository for raw mass spectrometry data. One of the 17 full datasets was available only in Scaffold (Proteome Software) format and was not usable in our pipeline. Of the 20 full or partially downloaded datasets, 17 could be processed fully or partially using X!Tandem17 (link) + K-score18 (link). These, along with the two large plasma datasets and the large cell line dataset, were added to the Human PeptideAtlas. All twenty are listed in Table S1, Supporting Information.
Among the added datasets were several that were expected to provide coverage of protein categories shown to be under-represented in PeptideAtlas by Gene Ontology analysis (data not shown), including samples of vitreous humor to increase coverage of proteins of sensory perception, seminal plasma to increase coverage of proteins of the reproductive system, a dataset identifying new integral membrane proteins, and experiments targeting signaling proteins. Other datasets were selected to cover additional sample types not previously included in PeptideAtlas (e.g. mitotic spindle, nucleosome, and colorectal tissue).
These datasets, along with all the datasets we had included in the previous build, were processed through the latest PeptideAtlas build pipeline 19 (link) to produce a final protein set with an FDR close to 1%. Briefly, all datasets were searched against a target-decoy sequence database consisting of the International Protein Index database20 (link) (IPI) and cRAP common contaminants (www.thegpm.org/crap), plus one decoy sequence for each target entry. Results were processed using the Trans-Proteomic Pipeline 10 (link). Identified peptides were mapped to a protein sequence database that included IPI v3.7120 (link), Ensembl v67.3711 , and the 2012_05 release of Swiss-Prot21 (link), 22 (link), including splice variants and representing 20,244 protein-coding genes. A PSM (peptide-spectrum match) FDR threshold of 0.0002 was applied to each dataset to yield a list of 218,799 distinct identified peptides and a protein-level FDR of 0.8% as computed by Mayu13 (link). See Table 1 for comparison with previous build.
12,629 Swiss-Prot entries were found to contain at least one identified peptide in either its canonical form or one of its variant forms. (Thirty-six entries identified only by semi-tryptic or non-tryptic peptides are not included in this tally.) These entries formed the list referred to herein as PA-seen and the remaining 7614 entries formed the list PA-unseen. Note that in some cases two or more proteins in the PA-seen list have identical or overlapping sets of identified peptides. The PA-seen list is not intended to be a parsimonious (minimal-redundancy) protein list, but to contain all Swiss-Prot entries with any peptide evidence in this atlas build.
2397 distinct peptides, or about 1% of the total, mapped only to a sequence in either IPI or Ensembl, and not to any Swiss-Prot sequence. A parsimonious mapping of these peptides covers a total of 1291 IPI or Ensembl identifiers.
Farrah T., Deutsch E.W., Hoopmann M.R., Hallows J.L., Sun Z., Huang C.Y, & Moritz R.L. (2012). The state of the human proteome in 2012 as viewed through PeptideAtlas. Journal of proteome research, 12(1), 162-171.
Publication 2012
A 218 Cell Lines Cells Feces Gene Products, Protein Genitalia Histocompatibility Testing Homo sapiens Integral Membrane Proteins Mass Spectrometry Mitotic Spindle Apparatus Nucleosomes Peptides Plasma Proteins Proteome Seminal Plasma Staphylococcal Protein A Strains Tissues Trypsin Vision Vitreous Body
2
Proteomic Analysis of Human Semen
Fresh ejaculate was collected from a healthy, 27-year-old Caucasian male and immediately spun down at 13,000 g for 5 minutes at 4°C to separate seminal fluid from spermatozoa. Phenylmethylsulphonylfluoride (PMSF, 0.2 mM), benzamidine (0.1 mM), and 1 μg/ml each of aprotinin, leupeptin, and pepstatin (Sigma, St. Louis, USA) were added to the sample to avoid digestion by powerful proteases present in seminal fluid. To ensure complete separation of cell debris or occasional spermatozoa from seminal plasma, the sample was centrifuged at 100,000 g for 30 minutes at 4°C. Protein concentration was assessed by Coomassie Plus assay (Pierce, Rockford, USA) and 1 mg protein was resolved on 10% NuPAGE Novex Bis-Tris gel (Invitrogen, Carlsbad, USA). The gel was cut into 14 pieces and subjected to standard in-gel trypsin digestion protocol [39 (link)]. Briefly, the pieces were washed twice with 25 mM ammonium bicarbonate/50% ethanol, dehydrated with absolute ethanol, reduced for 1 hour at 56°C with 10 mM dithiothreitol (DTT), alkylated for 45 minutes in the dark with 55 mM iodoacetamide. After extensive washing with ammonium bicarbonate and dehydratation, the 12.5 ng/μl trypsin solution (modified sequencing grade; Promega, Madison, USA) was added and the enzyme was allowed to function overnight at 37°C. The peptides were extracted with 30% acetonitrile, 3% trifluoroacetic acid (TFA) and the organic solvent was evaporated in a vacuum centrifuge. TFA was added to the final concentration of 2% and stop-and-go extraction tip purification was performed as previously described [40 (link)].
Pilch B, & Mann M. (2006). Large-scale and high-confidence proteomic analysis of human seminal plasma. Genome Biology, 7(5), R40.
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Publication 2006
acetonitrile ammonium bicarbonate Aprotinin benzamidine Biological Assay Bistris Caucasoid Races Cell Separation Digestion Dithiothreitol Endopeptidases Enzymes Ethanol Iodoacetamide leupeptin Males pepstatin Peptides Promega Proteins Seminal Plasma Solvents Sperm Trifluoroacetic Acid Trypsin Vacuum
3
Isolation of Exosomes from Semen
Semen samples were allowed to liquefy for 20 min at room temperature. Seminal plasma, containing exosomes, was separated from the cell fraction by centrifugation at 1000 x g for 10 min. Cell debris was removed by subsequent centrifugation at 2400 x g for 30 min followed by 0.45 μm and 0.22 μm syringe filtration (Millex HA). Exosomes were purified from the entire cell- and debris-free seminal plasma (ranging from 0.9 to 4.0 ml in our donors) by ultracentrifugation over a sucrose cushion using a method adapted from Lamparski et al. (33 (link)). Up to 2.5 ml of supernatant was added to ultracentrifuge tubes and under-layered with 300 μl of a 20 mM Tris/30% sucrose/deuterium oxide (D2O) cushion (pH 7.4) (Sigma). Samples were ultra-centrifuged at 100 000 x g for 90 min at 4°C in an SW 50 swinging bucket rotor (Beckman). The upper layer was collected and ultracentrifuged again at 100 000 x g for 14 h at 4°C over a 20 mM Tris/25% sucrose/D2O cushion (pH 7.4). The upper layer of exosome-depleted seminal plasma was stored at −80°C. The 30% and 25% sucrose cushions containing the exosome fraction were pooled and brought to 15 ml with Dulbecco's phosphate-buffered saline (PBS). The exosomes were washed by centrifuging at 2400 x g through an Amicon Ultracel 100 kDa cellulose centrifugal filter with 10 ml of PBS and concentrated to a final volume of 425 μl–3.2 ml. Exosomes were stored at −80°C.
Vojtech L., Woo S., Hughes S., Levy C., Ballweber L., Sauteraud R.P., Strobl J., Westerberg K., Gottardo R., Tewari M, & Hladik F. (2014). Exosomes in human semen carry a distinctive repertoire of small non-coding RNAs with potential regulatory functions. Nucleic Acids Research, 42(11), 7290-7304.
Publication 2014
Cells Cellulose Centrifugation Deuterium Oxide Donors Exosomes Filtration Phosphates Saline Solution Semen Seminal Plasma Sucrose Syringes Tromethamine Ultracentrifugation
4
Extraction and HPLC Analysis of Antioxidants
Each SP and serum sample was divided into two aliquots in order to perform separate extractions of water- and fat-soluble antioxidants. The first aliquot of SP and serum (500 μL) was used for the extraction of hydrophilic antioxidants and biomarkers of oxidative/nitrosative stress, as described elsewhere [42 (link)]. Samples were briefly deproteinized by adding 1 mL of HPLC-grade CH3CN (VWR Chemicals, Briare, France) immediately centrifuged to pellet precipitated proteins and supernatants washed with HPLC-grade chloroform to remove organic solvent. The upper aqueous phases of serum and seminal plasma were diluted 3 and 10 times, respectively, with HPLC-grade water and then directly injected (100 μL) onto the HPLC Hypersil C-18, 250 × 4.6 mm, 5 μm particle size column (Thermo Fisher Scientific, Rodano, Milan, Italy), provided with its own guard column, for the analysis of ascorbic acid, GSH, uric acid, MDA, –NO2−, –NO3− and 8-OHdG.
The processing to extract fat-soluble antioxidants was carried out on the second aliquot of SP and serum using a method recently described in detail elsewhere [43 (link)]. SP or serum (500 µL) was added to 1 mL of HPLC-grade CH3CN. After vigorous vortexing for 60 s, these mixtures were incubated at 37 °C for 1 h in a water bath under agitation to allow the full extraction of lipid soluble compounds, and then centrifuged at 20,690× g for 15 min at 4 °C to precipitate proteins. Clear supernatants were directly used for the reversed phase HPLC analysis of all-trans-retinoic acid, all-trans-retinol, astaxanthin, lutein, zeaxanthin, trans-β-apo-8′-carotenal, γ-tocopherol, β-cryptoxanthin, α-tocopherol, lycopene, α-carotene, β-carotene and coenzyme Q10 using a Hypersil Gold RP C18, 150 × 4.6 mm, 5 µm particle size column, provided with its own guard column (Thermo Fisher Scientific, Rodano, Milan, Italy). All the aforementioned procedures were carried out by protecting samples from light in order to avoid the degradation of photo-sensitive molecules.
For both analyses, the HPLC was a Spectra System P4000 pump, equipped with a highly sensitive 5 cm light-path flow cell UV6000LP diode array detector, set up for acquisition between 200 and 550 nm wavelengths (Thermo Fisher Scientific, Rodano, Milan, Italy). Data acquisition and analysis were carried out using the ChromQuest software provided by the HPLC manufacturer.
Identification and quantification of the different compounds in chromatographic runs of SP and serum samples were performed by comparing retention times and absorption spectra of the various peaks with those of runs of ultrapure standard mixtures with known concentrations. In the final calculations, the sum of the concentrations of astaxanthin, lutein, zeaxanthin, trans-β-apo-8′-carotenal, β-cryptoxanthin, lycopene, α-carotene and β-carotene was performed, and the fat-soluble antioxidants were reported hereinafter as total carotenoids.
Lazzarino G., Listorti I., Bilotta G., Capozzolo T., Amorini A.M., Longo S., Caruso G., Lazzarino G., Tavazzi B, & Bilotta P. (2019). Water- and Fat-Soluble Antioxidants in Human Seminal Plasma and Serum of Fertile Males. Antioxidants, 8(4), 96.
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Publication 2019
8-Hydroxy-2'-Deoxyguanosine All-Trans-Retinol alpha-Tocopherol Antioxidants Ascorbic Acid astaxanthin Bath Biological Markers Carotene Carotenoids Cells Chloroform Chromatography Cryptoxanthins gamma-Tocopherol Gold High-Performance Liquid Chromatographies Light Lipids Lutein Lycopene Nitrosative Stress Proteins Retention (Psychology) Seminal Plasma Serum Solvents Tretinoin ubidecarenone Uric Acid Zeaxanthin
5
Cryopreserved Seminal Plasma Proteomic Analysis
For proteomic analysis, seminal plasma was separated after cryopreservation. To prepare the samples for proteomic analysis, samples were thawed, and seminal plasma was separated from the sperm pellet by centrifugation at 3,000 g for 30 minutes to ensure complete removal of the cellular components. Seminal plasma samples were pooled and dissolved in 98% acetonitrile containing 0.1% trifluoroacetic acid followed by lyophilization at -80°C under vacuum for 2 days. The lyophilized sample was used to estimate the protein content. The samples were first precipitated in cold acetone, solubilized in 6 M urea, reduced with dithiothreitol and alkylated with iodoacetamide. The samples were subsequently diluted to give a urea concentration <2 M and then digested with trypsin. The tryptic digested products were subjected to a C18 clean up and then brought up in 50 μL of 1% acetic acid.
Sharma R., Agarwal A., Mohanty G., Du Plessis S.S., Gopalan B., Willard B., Yadav S.P, & Sabanegh E. (2013). Proteomic analysis of seminal fluid from men exhibiting oxidative stress. Reproductive Biology and Endocrinology : RB&E, 11, 85.
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Publication 2013
Acetic Acid Acetone acetonitrile Cellular Structures Centrifugation Cold Temperature Cryopreservation Dithiothreitol Freeze Drying Iodoacetamide Proteins Seminal Plasma Sperm Trifluoroacetic Acid Trypsin Urea Vacuum

Most recents protocols related to «Seminal Plasma»

1
Enrichment and Isolation of Extracellular Vesicles from Seminal Plasma
The enrichment of EVs was performed by sequential centrifugation steps. Briefly, seminal plasma samples were centrifuged at 4 °C for 10 min at 1600 × g, and the supernatant was transferred into a new tube, and centrifuged once again at 4 °C for 10 min at 16,000 × g. The collected supernatant was treated with 1% v/v Triton X-100 (Sigma-Aldrich) and incubated on ice for 20 min. Then, each sample was divided into two parts, one part (250 µl) was used to isolate EVs by ultracentrifugation (and subsequently protein and RNAs isolation) and the second part (250 µl) was used to isolate the RNAs including miRNA from the native samples (SF-Native). After ultracentrifugation at 100,000 × g for two hours at 4 °C, two fractions were obtained, the enriched EVs and the EV-depleted seminal plasma fraction. The EV pellets were collected resuspended in PBS and were used to purify the proteins and RNAs including miRNAs.
Abu-Halima M., Becker L.S., Al Smadi M.A., Kunz L.S., Gröger L, & Meese E. (2023). Expression of SPAG7 and its regulatory microRNAs in seminal plasma and seminal plasma-derived extracellular vesicles of patients with subfertility. Scientific Reports, 13, 3645.
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Publication 2023
Centrifugation isolation MicroRNAs Pellets, Drug Proteins RNA Seminal Plasma Triton X-100 Ultracentrifugation
2
Exosome Isolation from Seminal Plasma
Exosomes were purified from the entire cell- and debris-free seminal plasma (ranging from 0.9 to 4.0 ml in our donors) by ultracentrifugation over a sucrose cushion, as previously described (Vojtech et al., 2014 (link)). Up to 2.5 ml of supernatant was added to ultracentrifuge tubes and under-layered with 300 μl of a 20 mM Tris/30% sucrose/deuterium oxide (D2O) cushion (pH 7.4) (Sigma, St. Louis, MO, USA). Samples were ultra-centrifuged at 100 000 ×g for 90 min at 4°C in an SW 50 swinging bucket rotor (Beckman, Brea, CA, USA). The upper layer was collected and ultracentrifuged again at 100 000 ×g for 14 h at 4°C over a 20 mM Tris/25% sucrose/D2O cushion (pH 7.4). The upper layer of exosome-depleted seminal plasma was stored at −80°C. The 30% and 25% sucrose cushions containing the exosome fraction were pooled and brought to 15 ml with Dulbecco’s PBS (DPBS, GIBCO Thermo Fisher Scientific, Bothell, WA, USA). The exosomes were washed by centrifuging at 2400 ×g at 20°C through an Amicon Ultracel 100 kDa cellulose centrifugal filter (Millipore Sigma, St. Louis, MO, USA) with 10 ml of PBS and concentrated to a final volume of 425 μl–3.2 ml. Exosomes were stored at −80°C.
Gornalusse G., Spengler R.M., Sandford E., Kim Y., Levy C., Tewari M., Hladik F, & Vojtech L. (2023). Men who inject opioids exhibit altered tRNA-Gly-GCC isoforms in semen. Molecular Human Reproduction, 29(3), gaad003.
Publication 2023
Cells Cellulose Deuterium Oxide Donors Exosomes Seminal Plasma Sucrose Tromethamine Ultracentrifugation
3
Semen Exosome Isolation and Sperm Purification
Semen samples were allowed to liquefy for 20 min at room temperature. Seminal plasma, containing exosomes, was separated from the cell fraction by centrifugation at 1000 ×g for 10 min at 20°C. Cell debris was removed by subsequent centrifugation at 2400×g for 30 min at 20°C followed by 0.45 and 0.22 μm syringe filtration (Millex HA, Darmstadt, Germany). The cell pellet was cryopreserved (both in PWID and control semen samples) in 1 ml of freezing medium containing 90% heat-inactivated fetal bovine serum (Nucleus Biologics, San Diego, CA, USA) and 10% dimethyl sulfoxide. Cryovials were placed in a –80°C freezer in a Mr. Frosty™ freezing device containing isopropanol; the approximate freezing rate was –1°C/min. For long-term storage, cryovials were transferred to vapor-phase nitrogen.
Mature spermatozoa were purified using an adapted Percoll gradient protocol (Claassens et al., 1998 (link)). Isotonic Percoll solution was prepared by mixing 9 ml of Percoll (Sigma-Aldrich, St. Louis, MO, USA) with 1 ml of 10× concentrated Ham’s F10 solution (MP Biomedicals, Solon, OH, USA). The bottom fraction of the Percoll gradient (90%) contained 1 ml of 90% isotonic Percoll mixed with 10% X-VIVO 15 (Lonza, Basel, Switzerland) or human tubal fluid ‘HTF’ culture media (in-house). The upper fraction (45%) contained 1 ml of 45% isotonic Percoll mixed with 55% X-VIVO 15 (Lonza, Basel, Switzerland) or HTF culture media (in-house). The gradient was prepared in 15 ml Falcon conical tubes. Semen samples from both groups (PWID and controls) were thawed quickly in a 37°C water bath and 1 ml of X-VIVO 15 was added dropwise to each cryovial. Thawed semen samples were washed in 25 ml of X-VIVO 15, centrifuged at 400×g for 10 min at 20°C, resuspended in ∼500 µl of X-VIVO15 and layered on top of the gradient and centrifuged again at 400×g for 20 min (brake off). After centrifugation, ∼1.5 ml of the supernatant was aspirated off and discarded. The pellet and remaining ∼1 ml of Percoll were washed with 14 ml of X-VIVO 15 or PBS and spun down (400×g for 10 min at 20°C). The final pellet was resuspended in 500 µl of X-VIVO 15 and used to prepare smears on coverslips for Wright and hematoxylin and eosin (H&E) staining and/or aliquoted and frozen at –80°C for later RNA purification. Both stainings were performed at the Histology and Imaging Core (HIC) of the University of Washington, South Lake Union campus (Seattle, WA, USA).
Gornalusse G., Spengler R.M., Sandford E., Kim Y., Levy C., Tewari M., Hladik F, & Vojtech L. (2023). Men who inject opioids exhibit altered tRNA-Gly-GCC isoforms in semen. Molecular Human Reproduction, 29(3), gaad003.
Publication 2023
Bath Biological Factors Cell Nucleus Cells Centrifugation Culture Media Eosin Exosomes Fetal Bovine Serum Filtration Freezing Hematoxylin Homo sapiens Isopropyl Alcohol Isotonic Solutions Medical Devices Nitrogen Percoll Plant Embryos Seminal Plasma Solon Sperm Staining Sulfoxide, Dimethyl Syringes
4
Comprehensive Semen Analysis Protocol
Fifty-one healthy volunteers aged 21–38 years were recruited for this study. The established criteria for sample inclusion were as follows: (1) normal semen quality according to the sixth edition of the WHO Manual for the Laboratory Examination and Processing of Human Semen [5 ]; (2) no history of reproductive dysfunction; and (3) no current or previous urogenital infection. All volunteers were informed about the aim and expected outcomes of the study and subsequently signed informed consents. All procedures complied with the 1964 Helsinki Declaration and its later amendments or comparable ethical standards.
Prior to semen collection the participants were instructed to urinate, wash their hands and external genitalia with soap and water, and dry them off with disposable paper towels. Two semen samples were collected from each participant by masturbation. The first specimen was obtained following 2 days of sexual abstinence. This was followed by a second semen collection after 2 h of abstinence. All semen samples were collected into sterile containers and subsequently allowed to liquefy for 30 min at 37 °C.
Following liquefaction and volume measurement, each ejaculate was divided into four aliquots. The first aliquot was immediately subjected to the assessment of sperm motility, membrane, acrosome and DNA integrity, ROS production and leukocyte concentration. The second aliquot was transferred to an Eppendorf tube and stored at −80 °C for bacteriological analysis. The third aliquot was centrifuged at 300× g for 10 min to obtain seminal plasma which was subjected to the assessment of protein concentration and subsequently stored at −80 °C for the evaluation of total antioxidant capacity (TAC) and ELISA assays. The final aliquot of native semen was processed with a single layer gradient separation using 80% Percoll® (Sigma-Aldrich, St. Louis, MO, USA) with HEPES-buffered Ham’s F-10 medium (Sigma-Aldrich, St. Louis, MO, USA), according to the protocol established by Sharma et al. [90 (link)]. Obtained spermatozoa were centrifuged (300× g, 7 min) and washed with Dulbecco’s Phosphate Buffered Saline (DPBS; without calcium chloride and magnesium chloride; Sigma-Aldrich, St. Louis, MO, USA) three times. The samples were then solubilized in RIPA lysis buffer (Merck, Darmstadt, Germany) containing a proteinase inhibitor cocktail (Sigma-Aldrich, St. Louis, MO, USA) overnight at 4°C to allow a complete sperm lysis. After centrifugation at 13,000× g for 30 min, the supernatant was aspirated, subjected to the determination of the protein concentration, and stored at −80 °C for later assessment of oxidative damage to the proteins and lipids as well as for Western blot analysis [91 (link)].
Protein concentration in the seminal plasma and cell lysates was determined using the Total Protein assay commercial kit (Randox, Crumlin, UK) and RX Monaco fully automated clinical chemistry analyzer (Randox, Crumlin, UK) [86 (link)].
Tvrdá E., Ďuračka M., Benko F., Kováčik A., Lovíšek D., Gálová E., Žiarovská J., Schwarzová M, & Kačániová M. (2023). Ejaculatory Abstinence Affects the Sperm Quality in Normozoospermic Men—How Does the Seminal Bacteriome Respond?. International Journal of Molecular Sciences, 24(4), 3503.
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Publication 2023
Acrosome Antioxidants Biological Assay Buffers Calcium chloride Cells Centrifugation Enzyme-Linked Immunosorbent Assay Healthy Volunteers HEPES Homo sapiens Infection Leukocytes Lipids Magnesium Chloride Oxidative Damage Percoll Phosphates Plasma Proteins Protease Inhibitors Proteins Radioimmunoprecipitation Assay Randox Saline Solution Semen Semen Quality Seminal Plasma Serum Proteins Sperm Sperm Motility Sterility, Reproductive System, Genitourinary Tissue, Membrane Voluntary Workers Vulva Western Blot
5
Extracellular Vesicle Isolation from Seminal Plasma
Immediately after CASA analysis, semen samples (10 mL) were centrifuged at 800× g for 20 min at room temperature to collect spermatozoa. Corresponding supernatants were subjected to additional centrifugation (2000× g for 20 min) at 4 °C. The resulting supernatants (seminal plasma), devoid of cell debris and residual sperm cells, were collected and stored at −80 °C until EVs isolation. Frozen-thawed seminal plasma was centrifuged at 16,000× g for one hour at 4 °C. The resulting supernatants were ultracentrifuged (120,000× g for 70 min) at 4 °C. Visible EV pellets were rinsed twice with a high-purified cold PBS (5 mL) by ultracentrifugation (120,000× g for 70 min) at 4 °C. Cleaned EV pellets were resuspended in aliquots of 100 µL cold PBS and stored at −80 °C for further analysis.
Dlamini N.H., Nguyen T., Gad A., Tesfaye D., Liao S.F., Willard S.T., Ryan P.L, & Feugang J.M. (2023). Characterization of Extracellular Vesicle-Coupled miRNA Profiles in Seminal Plasma of Boars with Divergent Semen Quality Status. International Journal of Molecular Sciences, 24(4), 3194.
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Publication 2023
Cells Centrifugation Chaperone-Mediated Autophagy Cold Temperature Frozen Semen G-800 isolation Pellets, Drug Semen Seminal Plasma Sperm Ultracentrifugation

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More about "Seminal Plasma"

Seminal plasma, the fluid portion of semen, plays a crucial role in male fertility and reproductive health.
This complex biological medium is composed of secretions from the seminal vesicles, prostate, and other accessory genital glands.
It provides a supportive and nutritive environment for the spermatozoa, facilitating their motility and fertilizing capacity.
Analyzing the composition and properties of seminal plasma is essential for understanding male infertility and developing effective treatments.
Researchers can utilize advanced tools like PubCompare.ai's AI-driven platform to optimize their seminal plasma studies.
This powerful platform enables researchers to locate the best protocols from literature, preprints, and patents, enhancing the reproducibility and accuracy of their work.
The seminal plasma contains a variety of biomolecules, including proteins, lipids, carbohydrates, and enzymes, such as TRIzol reagent, Luminol, and Trolox.
These components work in synergy to support sperm function and protect the genetic material.
Techniques like SpectraFluor Plus, E-BC-K136, SPECTROstar Nano, and QIAamp DNA Mini Kit can be employed to analyze the composition and properties of seminal plasma samples.
Additionally, the presence of antimicrobial compounds, like Streptomycin, and the use of RNeasy Mini Kit for RNA extraction, further highlight the complexity and importance of seminal plasma in maintaining a healthy reproductive system.
By leveraging the insights gained from seminal plasma research, scientists can develop innovative strategies to address male infertility and enhance overall reproductive wellness.