Semenogelin II (SEMG2) (NM 003008) Human Recombinant Protein Product Data

Total Page：16

File Type：pdf, Size：1020Kb

Semenogelin II (SEMG2) (NM 003008) Human Recombinant Protein Product Data

OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for TP760462 Semenogelin II (SEMG2) (NM_003008) Human Recombinant Protein Product data: Product Type: Recombinant Proteins Description: Purified recombinant protein of Human semenogelin II (SEMG2), full length, with N-terminal HIS tag, expressed in E.Coli, 50ug Species: Human Expression Host: E. coli Tag: N-His Predicted MW: 62.9 kDa Concentration: >50 ug/mL as determined by microplate BCA method Purity: > 80% as determined by SDS-PAGE and Coomassie blue staining Buffer: 25mM Tris, pH8.0, 150 mM NaCl, 10% glycerol, 1 % Sarkosyl. Storage: Store at -80°C. Stability: Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles. RefSeq: NP_002999 Locus ID: 6407 UniProt ID: Q02383 RefSeq Size: 1982 Cytogenetics: 20q13.12 RefSeq ORF: 1746 Synonyms: SGII Summary: The secreted protein encoded by this gene is involved in the formation of a gel matrix that encases ejaculated spermatozoa. Proteolysis by the prostate-specific antigen (PSA) breaks down the gel matrix and allows the spermatozoa to move more freely. The encoded protein is found in lesser abundance than a similar semenogelin protein. An antibacterial activity has been found for a antimicrobial peptide isolated from this protein. The genes encoding these two semenogelin proteins are found in a cluster on chromosome 20. [provided by RefSeq, Jan 2015] This product is to be used for laboratory only. Not for diagnostic or therapeutic use. View online » ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 1 / 2 Semenogelin II (SEMG2) (NM_003008) Human Recombinant Protein – TP760462 Protein Families: Secreted Protein Product images: This product is to be used for laboratory only. Not for diagnostic or therapeutic use. ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 2 / 2.

Copy Link

Recommended publications

Extinction of Chromosomes Due to Specialization Is a Universal Occurrence Jason Wilson1*, Joshua M
www.nature.com/scientificreports OPEN Extinction of chromosomes due to specialization is a universal occurrence Jason Wilson1*, Joshua M. Staley2 & Gerald J. Wyckof1,2,3 The human X and Y chromosomes evolved from a pair of autosomes approximately 180 million years ago. Despite their shared evolutionary origin, extensive genetic decay has resulted in the human Y chromosome losing 97% of its ancestral genes while gene content and order remain highly conserved on the X chromosome. Five ‘stratifcation’ events, most likely inversions, reduced the Y chromosome’s ability to recombine with the X chromosome across the majority of its length and subjected its genes to the erosive forces associated with reduced recombination. The remaining functional genes are ubiquitously expressed, functionally coherent, dosage-sensitive genes, or have evolved male-specifc functionality. It is unknown, however, whether functional specialization is a degenerative phenomenon unique to sex chromosomes, or if it conveys a potential selective advantage aside from sexual antagonism. We examined the evolution of mammalian orthologs to determine if the selective forces that led to the degeneration of the Y chromosome are unique in the genome. The results of our study suggest these forces are not exclusive to the Y chromosome, and chromosomal degeneration may have occurred throughout our evolutionary history. The reduction of recombination could additionally result in rapid fxation through isolation of specialized functions resulting in a cost-beneft relationship during times of intense selective pressure. Te human Y chromosome has lost its ability to recombine with its once homologous partner, the X chromo- some, except in its pseudoautosomal regions (PARs) at the termini of the X and Y chromosomes1–3.
[Show full text]
An “Expressionistic” Look at Serrated Precancerous Colorectal Lesions Giancarlo Marra
Marra Diagnostic Pathology (2021) 16:4 https://doi.org/10.1186/s13000-020-01064-1 RESEARCH Open Access An “expressionistic” look at serrated precancerous colorectal lesions Giancarlo Marra Abstract Background: Approximately 60% of colorectal cancer (CRC) precursor lesions are the genuinely-dysplastic conventional adenomas (cADNs). The others include hyperplastic polyps (HPs), sessile serrated lesions (SSL), and traditional serrated adenomas (TSAs), subtypes of a class of lesions collectively referred to as “serrated.” Endoscopic and histologic differentiation between cADNs and serrated lesions, and between serrated lesion subtypes can be difficult. Methods: We used in situ hybridization to verify the expression patterns in CRC precursors of 21 RNA molecules that appear to be promising differentiation markers on the basis of previous RNA sequencing studies. Results: SSLs could be clearly differentiated from cADNs by the expression patterns of 9 of the 12 RNAs tested for this purpose (VSIG1, ANXA10, ACHE, SEMG1, AQP5, LINC00520, ZIC5/2, FOXD1, NKD1). Expression patterns of all 9 in HPs were similar to those in SSLs. Nine putatively HP-specific RNAs were also investigated, but none could be confirmed as such: most (e.g., HOXD13 and HOXB13), proved instead to be markers of the normal mucosa in the distal colon and rectum, where most HPs arise. TSAs displayed mixed staining patterns reflecting the presence of serrated and dysplastic glands in the same lesion. Conclusions: Using a robust in situ hybridization protocol, we identified promising tissue-staining markers that, if validated in larger series of lesions, could facilitate more precise histologic classification of CRC precursors and, consequently, more tailored clinical follow-up of their carriers.
[Show full text]
WO 2012/174282 A2 20 December 2012 (20.12.2012) P O P C T
(12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date WO 2012/174282 A2 20 December 2012 (20.12.2012) P O P C T (51) International Patent Classification: David [US/US]; 13539 N . 95th Way, Scottsdale, AZ C12Q 1/68 (2006.01) 85260 (US). (21) International Application Number: (74) Agent: AKHAVAN, Ramin; Caris Science, Inc., 6655 N . PCT/US20 12/0425 19 Macarthur Blvd., Irving, TX 75039 (US). (22) International Filing Date: (81) Designated States (unless otherwise indicated, for every 14 June 2012 (14.06.2012) kind of national protection available): AE, AG, AL, AM, AO, AT, AU, AZ, BA, BB, BG, BH, BR, BW, BY, BZ, English (25) Filing Language: CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, DO, Publication Language: English DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, HN, HR, HU, ID, IL, IN, IS, JP, KE, KG, KM, KN, KP, KR, (30) Priority Data: KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, ME, 61/497,895 16 June 201 1 (16.06.201 1) US MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, 61/499,138 20 June 201 1 (20.06.201 1) US OM, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SC, SD, 61/501,680 27 June 201 1 (27.06.201 1) u s SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, TR, 61/506,019 8 July 201 1(08.07.201 1) u s TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, ZW.
[Show full text]
Downloaded from the Tranche Distributed File System (Tranche.Proteomecommons.Org) and Ftp://Ftp.Thegpm.Org/Data/Msms
Research Article Title: The shrinking human protein coding complement: are there now fewer than 20,000 genes? Authors: Iakes Ezkurdia1*, David Juan2*, Jose Manuel Rodriguez3, Adam Frankish4, Mark Diekhans5, Jennifer Harrow4, Jesus Vazquez 6, Alfonso Valencia2,3, Michael L. Tress2,*. Affiliations: 1. Unidad de Proteómica, Centro Nacional de Investigaciones Cardiovasculares, CNIC, Melchor Fernández Almagro, 3, rid, 28029, MadSpain 2. Structural Biology and Bioinformatics Programme, Spanish National Cancer Research Centre (CNIO), Melchor Fernández Almagro, 3, 28029, Madrid, Spain 3. National Bioinformatics Institute (INB), Spanish National Cancer Research Centre (CNIO), Melchor Fernández Almagro, 3, 28029, Madrid, Spain 4. Wellcome Trust Sanger Institute, Wellcome Trust Campus, Hinxton, Cambridge CB10 1SA, UK 5. Center for Biomolecular Science and Engineering, School of Engineering, University of California Santa Cruz (UCSC), 1156 High Street, Santa Cruz, CA 95064, USA 6. Laboratorio de Proteómica Cardiovascular, Centro Nacional de Investigaciones Cardiovasculares, CNIC, Melchor Fernández Almagro, 3, 28029, Madrid, Spain *: these two authors wish to be considered as joint first authors of the paper. Corresponding author: Michael Tress, [email protected], Tel: +34 91 732 80 00 Fax: +34 91 224 69 76 Running title: Are there fewer than 20,000 protein-coding genes? Keywords: Protein coding genes, proteomics, evolution, genome annotation Abstract Determining the full complement of protein-coding genes is a key goal of genome annotation. The most powerful approach for confirming protein coding potential is the detection of cellular protein expression through peptide mass spectrometry experiments. Here we map the peptides detected in 7 large-scale proteomics studies to almost 60% of the protein coding genes in the GENCODE annotation the human genome.
[Show full text]
Alterations in Seminal Plasma Proteomic Profile in Men with Primary and Secondary Infertility
www.nature.com/scientificreports OPEN Alterations in seminal plasma proteomic profle in men with primary and secondary infertility Ana D. Martins1,2, Manesh Kumar Panner Selvam1, Ashok Agarwal1 ✉ , Marco G. Alves2 & Saradha Baskaran1 Proteome of seminal plasma provides profound information related to the male reproductive health. This pilot study was conducted to characterize proteomic profle of seminal plasma from men with primary, or secondary infertility and compare it with proven fertile men. Study participants (n = 59) were recruited at the Cleveland Clinic and divided according to their fertility status: proven fertile (n = 39); primary infertility (n = 11) and secondary infertility (n = 9). Proteomic shotgun analysis revealed a total of 515 peptides common to primary infertility and control group; whereas 523 peptides were common to secondary infertility and control group. Bioinformatic analysis revealed dysregulation of biological processes such as cell secretion and vesicle mediated transport in primary infertility, whereas immune system response, regulation of proteolysis and iron homeostasis were dysregulated in secondary infertility. Western blot validation showed overexpression of ANXA2 and CDC42, and underexpression of SEMG2 proteins in primary infertility; and overexpression of ANXA2 and APP proteins in secondary infertility. This study elucidates the potential role of diferentially expressed proteins in the seminal plasma as diagnostic biomarker for primary and secondary infertility. Furthermore, our results suggest maturation failure and immune reaction response as the main cause of infertility in men with primary and secondary infertility, respectively. Additional validation of the proteins involved in the above pathways is warranted. Infertility globally afects 15% of couples and is now classifed as a disease of the reproductive system by the World Health Organization (WHO)1.
[Show full text]
Proteomic Profiling of Two Distinct Populations of Extracellular
International Journal of Molecular Sciences Article Proteomic Profiling of Two Distinct Populations of Extracellular Vesicles Isolated from Human Seminal Plasma Xiaogang Zhang 1, Harmjan R. Vos 2 , Weiyang Tao 3 and Willem Stoorvogel 1,* 1 Department of Biomolecular Health Sciences, Faculty of Veterinary Science, Utrecht University, 3584 CM Utrecht, The Netherlands; [email protected] 2 Center for Molecular Medicine, Molecular Cancer Research Section, University Medical Center, 3584 CX Utrecht, The Netherlands; [email protected] 3 Department of Rheumatology and Clinical Immunology, University Medical Center Utrecht, Utrecht University, 3508 GA Utrecht, Netherlands; [email protected] * Correspondence: [email protected] Received: 1 September 2020; Accepted: 22 October 2020; Published: 26 October 2020 Abstract: Body fluids contain many populations of extracellular vesicles (EV) that differ in size, cellular origin, molecular composition, and biological activities. EV in seminal plasma are in majority originating from prostate epithelial cells, and hence are also referred to as prostasomes. Nevertheless, EV are also contributed by other accessory sex glands, as well as by the testis and epididymis. In a previous study, we isolated EV from seminal plasma of vasectomized men, thereby excluding contributions from the testis and epididymis, and identified two distinct EV populations with diameters of 50 and 100 nm, respectively. In the current study, we comprehensively analyzed the protein composition of these two EV populations using quantitative Liquid Chromatography-Mass Spectrometry (LC-MS/MS). In total 1558 proteins were identified. Of these, 45% was found only in ≈ the isolated 100 nm EV, 1% only in the isolated 50 nm EV, and 54% in both 100 nm and 50 nm EV.
[Show full text]
The DNA Sequence and Comparative Analysis of Human Chromosome 20
articles The DNA sequence and comparative analysis of human chromosome 20 P. Deloukas, L. H. Matthews, J. Ashurst, J. Burton, J. G. R. Gilbert, M. Jones, G. Stavrides, J. P. Almeida, A. K. Babbage, C. L. Bagguley, J. Bailey, K. F. Barlow, K. N. Bates, L. M. Beard, D. M. Beare, O. P. Beasley, C. P. Bird, S. E. Blakey, A. M. Bridgeman, A. J. Brown, D. Buck, W. Burrill, A. P. Butler, C. Carder, N. P. Carter, J. C. Chapman, M. Clamp, G. Clark, L. N. Clark, S. Y. Clark, C. M. Clee, S. Clegg, V. E. Cobley, R. E. Collier, R. Connor, N. R. Corby, A. Coulson, G. J. Coville, R. Deadman, P. Dhami, M. Dunn, A. G. Ellington, J. A. Frankland, A. Fraser, L. French, P. Garner, D. V. Grafham, C. Grif®ths, M. N. D. Grif®ths, R. Gwilliam, R. E. Hall, S. Hammond, J. L. Harley, P. D. Heath, S. Ho, J. L. Holden, P. J. Howden, E. Huckle, A. R. Hunt, S. E. Hunt, K. Jekosch, C. M. Johnson, D. Johnson, M. P. Kay, A. M. Kimberley, A. King, A. Knights, G. K. Laird, S. Lawlor, M. H. Lehvaslaiho, M. Leversha, C. Lloyd, D. M. Lloyd, J. D. Lovell, V. L. Marsh, S. L. Martin, L. J. McConnachie, K. McLay, A. A. McMurray, S. Milne, D. Mistry, M. J. F. Moore, J. C. Mullikin, T. Nickerson, K. Oliver, A. Parker, R. Patel, T. A. V. Pearce, A. I. Peck, B. J. C. T. Phillimore, S. R. Prathalingam, R. W. Plumb, H. Ramsay, C. M.
[Show full text]
Update on the Proteomics of Male Infertility: a Systematic Review
Arab Journal of Urology (2018) 16, 103–112 Arab Journal of Urology (Official Journal of the Arab Association of Urology) www.sciencedirect.com DIAGNOSIS ORIGINAL ARTICLE Update on the proteomics of male infertility: A systematic review Manesh Kumar Panner Selvam, Ashok Agarwal * American Centre for Reproductive Medicine, Cleveland Clinic, Cleveland, OH, USA Received 28 October 2017, Received in revised form 17 November 2017, Accepted 19 November 2017 Available online 29 December 2017 KEYWORDS Abstract Objective: To assess the role of differentially expressed proteins as a resource for potential biomarker identification of infertility, as male infertility is Sperm proteomics; of rising concern in reproductive medicine and evidence pertaining to its aetiology Male infertility; at a molecular level particularly proteomic as spermatozoa lack transcription and Spermatozoa; translation. Proteomics is considered as a major field in molecular biology to vali- Varicocele; date the target proteins in a pathophysiological state. Differential expression analy- Biomarkers sis of sperm proteins in infertile men and bioinformatics analysis offer information about their involvement in biological pathways. Materials and methods: Literature search was performed on PubMed, Medline, and Science Direct databases using the keywords ‘sperm proteomics’ and ‘male infer- tility’. We also reviewed the relevant cross references of retrieved articles and included them in the review process. Articles written in any language other than Eng- lish were excluded. Results: Of 575 articles identified, preliminary screening for relevant studies elim- inated 293 articles. At the next level of selection, from 282 studies only 80 articles related to male infertility condition met the selection criteria and were included in this review.
[Show full text]
A Locus on Human Chromosome 20 Contains Several Genes Expressing Protease Inhibitor Domains with Homology to Whey Acidic Protein
A locus on human chromosome 20 contains several genes expressing protease inhibitor domains with homology to whey acidic protein. Clauss, Adam; Lilja, Hans; Lundwall, Åke Published in: Biochemical Journal DOI: 10.1042/BJ20020869 2002 Link to publication Citation for published version (APA): Clauss, A., Lilja, H., & Lundwall, Å. (2002). A locus on human chromosome 20 contains several genes expressing protease inhibitor domains with homology to whey acidic protein. Biochemical Journal, 368(Pt 1), 233-242. https://doi.org/10.1042/BJ20020869 Total number of authors: 3 General rights Unless other specific re-use rights are stated the following general rights apply: Copyright and moral rights for the publications made accessible in the public portal are retained by the authors and/or other copyright owners and it is a condition of accessing publications that users recognise and abide by the legal requirements associated with these rights. • Users may download and print one copy of any publication from the public portal for the purpose of private study or research. • You may not further distribute the material or use it for any profit-making activity or commercial gain • You may freely distribute the URL identifying the publication in the public portal Read more about Creative commons licenses: https://creativecommons.org/licenses/ Take down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim. LUND UNIVERSITY PO Box 117 221 00 Lund +46 46-222 00 00 Biochem. J. (2002) 368, 233–242 (Printed in Great Britain) 233 A locus on human chromosome 20 contains several genes expressing protease inhibitor domains with homology to whey acidic protein Adam CLAUSS, Hans LILJA and AH ke LUNDWALL1 Wallenberg Laboratory, Department of Laboratory Medicine, University Hospital MAS, Lund University, S-205 02 Malmo$ , Sweden A locus containing 14 genes, encoding protein domains that have nucleotides.
[Show full text]
Semenogelin II (SEMG2) (NM 003008) Human Tagged ORF Clone Product Data
OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for RC210006 Semenogelin II (SEMG2) (NM_003008) Human Tagged ORF Clone Product data: Product Type: Expression Plasmids Product Name: Semenogelin II (SEMG2) (NM_003008) Human Tagged ORF Clone Tag: Myc-DDK Symbol: SEMG2 Synonyms: SGII Vector: pCMV6-Entry (PS100001) E. coli Selection: Kanamycin (25 ug/mL) Cell Selection: Neomycin This product is to be used for laboratory only. Not for diagnostic or therapeutic use. View online » ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 1 / 4 Semenogelin II (SEMG2) (NM_003008) Human Tagged ORF Clone – RC210006 ORF Nucleotide >RC210006 representing NM_003008 Sequence: Red=Cloning site Blue=ORF Green=Tags(s) TTTTGTAATACGACTCACTATAGGGCGGCCGGGAATTCGTCGACTGGATCCGGTACCGAGGAGATCTGCC GCCGCGATCGCC ATGAAGTCCATCATCCTCTTTGTCCTTTCCCTGCTCCTTATCTTGGAGAAGCAAGCAGCTGTGATGGGAC AAAAAGGTGGATCAAAAGGCCAATTGCCAAGCGGATCTTCCCAATTTCCACATGGAAAAAAGGGCCAGCA CTATTTTGGACAAAAAGACCAACAACATACTAAATCCAAAGGCAGTTTTTCTATTCAACACACATATCAT GTAGACATCAATGATCATGACTGGACCCGAAAAAGTCAGCAGTATGATTTGAATGCCCTACATAAGGCGA CAAAATCAAAACAACACCTAGGTGGAAGTCAACAACTGCTCAATTATAAACAAGAAGGCAGAGACCATGA TAAATCAAAAGGTCATTTTCACATGATAGTTATACATCATAAAGGAGGCCAAGCTCATCATGGGACACAA AATCCTTCTCAAGATCAGGGGAATAGCCCATCTGGAAAGGGATTATCCAGTCAATGTTCAAACACAGAAA AAAGGCTATGGGTTCATGGACTAAGTAAAGAACAAGCTTCAGCCTCTGGTGCACAAAAAGGTAGAACACA AGGTGGATCCCAAAGCAGTTATGTTCTCCAAACTGAAGAACTAGTAGTTAACAAACAACAACGTGAGACT
[Show full text]
Genetic Resistance to DEHP-Induced Transgenerational
bioRxiv preprint doi: https://doi.org/10.1101/474155; this version posted November 19, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY 4.0 International license. 1 Genetic resistance to DEHP-induced 2 transgenerational endocrine disruption 3 Ludwig Stenz1*, Rita Rahban1, Julien Prados2,3, Serge Nef1, Ariane Paoloni- 4 Giacobino1 5 1 Department of Genetic Medicine and Development, 6 2 Department of Microbiology and Molecular Medicine, 7 3 Department of Neuroscience, 8 University of Geneva Faculty of Medicine, Geneva, Switzerland 9 Short title: Transgenerational endocrine disruption 10 11 *Corresponding author: 12 E-mail: [email protected] (LS) 13 14 1 bioRxiv preprint doi: https://doi.org/10.1101/474155; this version posted November 19, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY 4.0 International license. 15 Abstract 16 Di(2-ethylhexyl)phthalate (DEHP) interferes with sex hormones signaling pathways 17 (SHP). C57BL/6J mice prenatally exposed to DEHP develop a testicular dysgenesis 18 syndrome (TDS) at adulthood, but similarly-exposed FVB/N mice are not affected. 19 Here we aim to understand the reasons behind this drastic difference that should 20 depend on the genome of the strain. In both backgrounds, pregnant female mice 21 received per os either DEHP or corn oil vehicle and the male filiations were 22 examined.
[Show full text]
Rabbit Anti-SEMG2/FITC Conjugated Antibody-SL4488R-FITC
SunLong Biotech Co.,LTD Tel: 0086-571- 56623320 Fax:0086-571- 56623318 E-mail:[email protected] www.sunlongbiotech.com Rabbit Anti-SEMG2/FITC Conjugated antibody SL4488R-FITC Product Name: Anti-SEMG2/FITC Chinese Name: FITC标记的精液凝固蛋白2抗体 Alias: Semenogelin 2; Semenogelin II; Semenogelin-2; SEMG2; SEMG2_HUMAN; SGII. Organism Species: Rabbit Clonality: Polyclonal React Species: Human, ICC=1:50-200IF=1:50-200 Applications: not yet tested in other applications. optimal dilutions/concentrations should be determined by the end user. Molecular weight: 65kDa Form: Lyophilized or Liquid Concentration: 2mg/1ml immunogen: KLH conjugated synthetic peptide derived from human SEMG2 Lsotype: IgG Purification: affinity purified by Protein A Storage Buffer: 0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. The lyophilized antibodywww.sunlongbiotech.com is stable at room temperature for at least one month and for greater than a year Storage: when kept at -20°C. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C. background: The secreted protein encoded by this gene is involved in the formation of a gel matrix that encases ejaculated spermatozoa. Proteolysis by the prostate-specific antigen (PSA) breaks down the gel matrix and allows the spermatozoa to move more freely. The encoded protein is found in lesser abundance than a similar semenogelin protein. An Product Detail: antibacterial activity has been found for a antimicrobial peptide isolated from this protein. The genes encoding these two semenogelin proteins are found in a cluster on chromosome 20.
[Show full text]