Anti-SERPINB10 Produced in Rabbit, Affinity Isolated Antibody Product Number S 9570 Product Description Anti-SERPINB10 Is

Anti-SERPINB10 Produced in rabbit, Affinity Isolated Antibody Product Number S 9570 Product Description Anti-SERPINB10 is produced in rabbit using as Precautions and Disclaimer immunogen a peptide corresponding to the human Due to the sodium azide content a material safety sheet SERPINB10 protein (amino acids 316-330). The (MSDS) for this product has been sent to the attention antibody is affinity-purified using the immunizing of the safety officer of your institution. Consult the peptide immobilized on agarose. MSDS for information regarding hazardous and safe handling practices. Anti-SERPINB10 reacts with amino acid residues 316- 330 (SQSKADFSGMSSARN) of human SERPINB10. Storage/Stability The antibody may be used in immunoblotting Store at -20 °C. The product may be stored at 2-8 °C (~45 kDa). for up to three months. For prolonged storage, freeze in working aliquots at -20 °C. Avoid repeated freezing and Members of the human serpin family regulate a diverse thawing. Do not store in a “frost-free” freezer. array of serine and cysteine proteinases associated with essential biological processes such as fibrinolysis, Product Profile coagulation, inflammation, cell mobility, cellular For immunoblotting, a minimum working antibody differentiation, and apoptosis. Most serpins are dilution of 1:500 is recommended. secreted and attain physiologic concentrations in the blood and extracellular fluids. However, a subset of the Note: In order to obtain the best results in various serpin superfamily, the ov-serpins, also resides techniques and preparations, we recommend deter- intracellularly. A novel serpin gene, SERPINB10, is mining optimal working dilutions by titration. highly expressed in human bone marrow cells and plays a role in the regulation of protease activities References during hematopoiesis. 1. Riewald, M., and Schleef, R.R., J. Biol. Chem., 270, 26754-26757 (1995). Reagent The antibody is supplied as a solution of ~1 mg/mL in phosphate buffered saline containing 0.02% sodium azide. KAA 11/05 Sigma brand products are sold through Sigma-Aldrich, Inc. Sigma-Aldrich, Inc. warrants that its products conform to the information contained in this and other Sigma-Aldrich publications. Purchaser must determine the suitability of the product(s) for their particular use. Additional terms and conditions may apply. Please see reverse side of the invoice or packing slip. .

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Characterisation of Serpinb2 As a Stress Response Modulator
University of Wollongong Research Online University of Wollongong Thesis Collection 1954-2016 University of Wollongong Thesis Collections 2015 Characterisation of SerpinB2 as a stress response modulator Jodi Anne Lee University of Wollongong Follow this and additional works at: https://ro.uow.edu.au/theses University of Wollongong Copyright Warning You may print or download ONE copy of this document for the purpose of your own research or study. The University does not authorise you to copy, communicate or otherwise make available electronically to any other person any copyright material contained on this site. You are reminded of the following: This work is copyright. Apart from any use permitted under the Copyright Act 1968, no part of this work may be reproduced by any process, nor may any other exclusive right be exercised, without the permission of the author. Copyright owners are entitled to take legal action against persons who infringe their copyright. A reproduction of material that is protected by copyright may be a copyright infringement. A court may impose penalties and award damages in relation to offences and infringements relating to copyright material. Higher penalties may apply, and higher damages may be awarded, for offences and infringements involving the conversion of material into digital or electronic form. Unless otherwise indicated, the views expressed in this thesis are those of the author and do not necessarily represent the views of the University of Wollongong. Recommended Citation Lee, Jodi Anne, Characterisation of SerpinB2 as a stress response modulator, Doctor of Philosophy thesis, School of Biological Sciences, University of Wollongong, 2015. https://ro.uow.edu.au/theses/4538 Research Online is the open access institutional repository for the University of Wollongong.
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Serpins—From Trap to Treatment
MINI REVIEW published: 12 February 2019 doi: 10.3389/fmed.2019.00025 SERPINs—From Trap to Treatment Wariya Sanrattana, Coen Maas and Steven de Maat* Department of Clinical Chemistry and Haematology, University Medical Center Utrecht, Utrecht University, Utrecht, Netherlands Excessive enzyme activity often has pathological consequences. This for example is the case in thrombosis and hereditary angioedema, where serine proteases of the coagulation system and kallikrein-kinin system are excessively active. Serine proteases are controlled by SERPINs (serine protease inhibitors). We here describe the basic biochemical mechanisms behind SERPIN activity and identify key determinants that influence their function. We explore the clinical phenotypes of several SERPIN deficiencies and review studies where SERPINs are being used beyond replacement therapy. Excitingly, rare human SERPIN mutations have led us and others to believe that it is possible to refine SERPINs toward desired behavior for the treatment of enzyme-driven pathology. Keywords: SERPIN (serine proteinase inhibitor), protein engineering, bradykinin (BK), hemostasis, therapy Edited by: Marvin T. Nieman, Case Western Reserve University, United States INTRODUCTION Reviewed by: Serine proteases are the “workhorses” of the human body. This enzyme family is conserved Daniel A. Lawrence, throughout evolution. There are 1,121 putative proteases in the human body, and about 180 of University of Michigan, United States Thomas Renne, these are serine proteases (1, 2). They are involved in diverse physiological processes, ranging from University Medical Center blood coagulation, fibrinolysis, and inflammation to immunity (Figure 1A). The activity of serine Hamburg-Eppendorf, Germany proteases is amongst others regulated by a dedicated class of inhibitory proteins called SERPINs Paulo Antonio De Souza Mourão, (serine protease inhibitors).
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Serpinb10, a Serine Protease Inhibitor, Is Implicated in UV-Induced Cellular Response
International Journal of Molecular Sciences Article SerpinB10, a Serine Protease Inhibitor, Is Implicated in UV-Induced Cellular Response Hajnalka Majoros 1, Barbara N. Borsos 1, Zsuzsanna Ujfaludi 1 , Zoltán G. Páhi 1,Mónika Mórocz 2, Lajos Haracska 2, Imre Miklós Boros 3,4 and Tibor Pankotai 1,* 1 Institute of Pathology, Faculty of Medicine, University of Szeged, 1 Állomás utca, H-6725 Szeged, Hungary; [email protected] (H.M.); [email protected] (B.N.B.); [email protected] (Z.U.); [email protected] (Z.G.P.) 2 HCEMM-BRC Mutagenesis and Carcinogenesis Research Group, Institute of Genetics, Biological Research Centre, H-6726 Szeged, Hungary; [email protected] (M.M.); [email protected] (L.H.) 3 Department of Biochemistry and Molecular Biology, Faculty of Science and Informatics, University of Szeged, H-6726 Szeged, Hungary; [email protected] 4 Institute of Biochemistry, Biological Research Centre, H-6726 Szeged, Hungary * Correspondence: [email protected]; Tel.: +36-62-546-164 Abstract: UV-induced DNA damage response and repair are extensively studied processes, as any malfunction in these pathways contributes to the activation of tumorigenesis. Although several proteins involved in these cellular mechanisms have been described, the entire repair cascade has remained unexplored. To identify new players in UV-induced repair, we performed a microarray screen, in which we found SerpinB10 (SPB10, Bomapin) as one of the most dramatically upregulated SPB10 genes following UV irradiation. Here, we demonstrated that an increased mRNA level of is a general cellular response following UV irradiation regardless of the cell type.
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SERPINB10 Contributes to Asthma by Inhibiting the Apoptosis of Allergenic Th2 Cells
SERPINB10 Contributes to Asthma by Inhibiting the Apoptosis of Allergenic Th2 Cells Yuqing Mo Zhongshan Hospital Fudan University https://orcid.org/0000-0002-2185-0552 Ling Ye Zhongshan Hospital Fudan University Hui Cai Zhongshan Hospital Fudan University Guiping Zhu Zhongshan Hospital Fudan University Jian Wang Zhongshan Hospital Fudan University Mengchan Zhu Zhongshan Hospital Fudan University Xixi Song Zhongshan Hospital Fudan University Chengyu Yang Zhongshan Hospital Fudan University Meiling Jin ( [email protected] ) Department of Pulmonary and Critical Care Medicine, Zhongshan Hospital, Fudan University, No.180 Fenglin Road, Xuhui District, Shanghai 200032, China. https://orcid.org/0000-0001-6532-3191 Research Keywords: asthma, SERPINB10, Th2 response, apoptosis Posted Date: December 30th, 2020 DOI: https://doi.org/10.21203/rs.3.rs-135747/v1 License: This work is licensed under a Creative Commons Attribution 4.0 International License. Read Full License Page 1/18 Abstract Background: Serine peptidase inhibitor, clade B, member 10 (SERPINB10) contributes to allergic inammation in asthma. However, its role in the T-helper type 1 (Th1) /Th2 response of allergic asthma is not known. The goal of this study was to unveil the function of SERPINB10 in the Th2 response of allergic asthma and the mechanism by which SERPINB10 affects the viability of Th2 cells. Methods: Th2 cytokines and serum levels of house dust mite (HDM)-specic IgE in bronchoalveolar lavage uid were examined by ELISA in an HDM-induced asthma model. The number and apoptosis of Th1 and Th2 cells in mouse lungs were measured by ow cytometry. Naïve CD4 T cells from patients with asthma were cultured under appropriate polarizing conditions to generate Th1 and Th2 cells.
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Suppression of the Invasion and Migration of Cancer Cells by SERPINB Family Genes and Their Derived Peptides
238 ONCOLOGY REPORTS 27: 238-245, 2012 Suppression of the invasion and migration of cancer cells by SERPINB family genes and their derived peptides RUEY-HWANG CHOU1-4, HUI-CHIN WEN1,7, WEI-GUANG LIANG1,5, SHENG-CHIEH LIN1,5, HSIAO-WEI YUAN1, CHENG-WEN WU1,5,6 and WUN-SHAING WAYNE CHANG1 1National Institute of Cancer Research, National Health Research Institutes, Miaoli 35053; 2Center for Molecular Medicine, China Medical University Hospital, Taichung 40402; 3China Medical University, Taichung 40402; 4Department of Biotechnology, Asia University, Taichung 41354; 5College of Life Science, National Tsing Hua University, Hsinchu 30013; 6Institute of Biochemistry and Molecular Biology, National Yang Ming University, Taipei 11221, Taiwan, R.O.C. Received June 28, 2011; Accepted August 17, 2011 DOI: 10.3892/or.2011.1497 Abstract. Apart from SERPINB2 and SERPINB5, the roles SERPINB RCL-peptides may provide a reasonable strategy of the remaining 13 members of the human SERPINB family against lethal cancer metastasis. in cancer metastasis are still unknown. In the present study, we demonstrated that most of these genes are differentially Introduction expressed in tumor tissues compared to matched normal tissues from lung or breast cancer patients. Overexpression of Cancer metastasis is the leading cause of morbidity and each SERPINB gene effectively suppressed the invasiveness mortality in cancer patients. It is a highly complex process, and motility of malignant cancer cells. Among all of the genes, including cell detachment, migration, invasion, circulation in the SERPINB1, SERPINB5 and SERPINB7 genes were more blood vessels, adhesion, colonization at other sites and forma- potent, and the inhibitory effect was further enhanced by tion of secondary tumors (1).
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A peer-reviewed version of this preprint was published in PeerJ on 16 June 2015. View the peer-reviewed version (peerj.com/articles/1026), which is the preferred citable publication unless you speciﬁcally need to cite this preprint. Kumar A. 2015. Bayesian phylogeny analysis of vertebrate serpins illustrates evolutionary conservation of the intron and indels based six groups classiﬁcation system from lampreys for ∼500 MY. PeerJ 3:e1026 https://doi.org/10.7717/peerj.1026 Bayesian phylogeny analysis of vertebrate serpins illustrates evolutionary conservation of the intron and indels based six groups classification system from lampreys for ~500 MY Abhishek Kumar The serpin superfamily is characterized by proteins that fold into a conserved tertiary structure and exploits a sophisticated and irreversible suicide-mechanism of inhibition. Vertebrate serpins can be conveniently classified into six groups (V1-V6), based on three independent biological features - genomic organization, diagnostic amino acid sites and rare indels. However, this classification system was based on the limited number of mammalian genomes available. In this study, several non-mammalian genomes are used to validate this classification system, using the powerful Bayesian phylogenetic method. PrePrints This method supports the intron and indel based vertebrate classification and proves that serpins have been maintained from lampreys to humans for about 500 MY. Lampreys have less than 10 serpins, which expanded into 36 serpins in humans. The two expanding groups V1 and V2 have SERPINB1/SERPINB6 and SERPINA8/SERPIND1 as the ancestral serpins, respectively. Large clusters of serpins are formed by local duplications of these serpins in tetrapod genomes. Interestingly, the ancestral HCII/SERPIND1 locus (nested within PIK4CA) possesses group V4 serpin (A2APL1, homolog of α2-AP/SERPINF2 ) of lampreys; hence, pointing to the fact that group V4 might have originated from group V2.
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SERPINB10 Contributes to Asthma by Inhibiting the Apoptosis of Allergenic Th2 Cells
Mo et al. Respir Res (2021) 22:178 https://doi.org/10.1186/s12931-021-01757-1 RESEARCH Open Access SERPINB10 contributes to asthma by inhibiting the apoptosis of allergenic Th2 cells Yuqing Mo†, Ling Ye†, Hui Cai, Guiping Zhu, Jian Wang, Mengchan Zhu, Xixi Song, Chengyu Yang and Meiling Jin* Abstract Background: Serine peptidase inhibitor, clade B, member 10 (SERPINB10) contributes to allergic infammation in asthma. However, its role in the T-helper type 2 (Th2) response of allergic asthma is not known. The goal of this study was to unveil the function of SERPINB10 in the Th2 response of allergic asthma and the mechanism by which SER- PINB10 afects the viability of Th2 cells. Methods: Th2 cytokines and serum levels of house dust mite (HDM)-specifc IgE in bronchoalveolar lavage fuid were examined by ELISA in an HDM-induced asthma model. The number and apoptosis of Th1 and Th2 cells in mouse lungs were measured by fow cytometry. Naïve CD4 T cells from patients with asthma were cultured under appropriate polarizing conditions to generate Th1 and Th2 cells. SERPINB10 expression in polarized Th1 and Th2 cells was quantifed by real-time reverse transcription-quantitative polymerase chain reaction. SERPINB10 expression was knocked down in human CD4 T cells with lentivirus. Results: Knockdown of SERPINB10 expression signifcantly diminished HDM-induced Th2 cytokine secretion and level of HDM-specifc IgE. After HDM exposure, SERPINB10-knockdown mice had diminished numbers of Th2 cells, but similar numbers of Th1 cells, compared with those in negative-control mice. Th2 cells of SERPINB10-knockdown mice were more susceptible to apoptosis than that of control mice.
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Understanding the Role of Plasminogen Activator Inhibitor Type-2 (PAI-2, Serpinb2)
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