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Human and Mouse CD Marker Handbook Human and Mouse CD Marker Key Markers - Human Key Markers - Mouse
Welcome to More Choice CD Marker Handbook For more information, please visit: Human bdbiosciences.com/eu/go/humancdmarkers Mouse bdbiosciences.com/eu/go/mousecdmarkers Human and Mouse CD Marker Handbook Human and Mouse CD Marker Key Markers - Human Key Markers - Mouse CD3 CD3 CD (cluster of differentiation) molecules are cell surface markers T Cell CD4 CD4 useful for the identification and characterization of leukocytes. The CD CD8 CD8 nomenclature was developed and is maintained through the HLDA (Human Leukocyte Differentiation Antigens) workshop started in 1982. CD45R/B220 CD19 CD19 The goal is to provide standardization of monoclonal antibodies to B Cell CD20 CD22 (B cell activation marker) human antigens across laboratories. To characterize or “workshop” the antibodies, multiple laboratories carry out blind analyses of antibodies. These results independently validate antibody specificity. CD11c CD11c Dendritic Cell CD123 CD123 While the CD nomenclature has been developed for use with human antigens, it is applied to corresponding mouse antigens as well as antigens from other species. However, the mouse and other species NK Cell CD56 CD335 (NKp46) antibodies are not tested by HLDA. Human CD markers were reviewed by the HLDA. New CD markers Stem Cell/ CD34 CD34 were established at the HLDA9 meeting held in Barcelona in 2010. For Precursor hematopoetic stem cell only hematopoetic stem cell only additional information and CD markers please visit www.hcdm.org. Macrophage/ CD14 CD11b/ Mac-1 Monocyte CD33 Ly-71 (F4/80) CD66b Granulocyte CD66b Gr-1/Ly6G Ly6C CD41 CD41 CD61 (Integrin b3) CD61 Platelet CD9 CD62 CD62P (activated platelets) CD235a CD235a Erythrocyte Ter-119 CD146 MECA-32 CD106 CD146 Endothelial Cell CD31 CD62E (activated endothelial cells) Epithelial Cell CD236 CD326 (EPCAM1) For Research Use Only. -
Machine-Learning and Chemicogenomics Approach Defi Nes and Predicts Cross-Talk of Hippo and MAPK Pathways
Published OnlineFirst November 18, 2020; DOI: 10.1158/2159-8290.CD-20-0706 RESEARCH ARTICLE Machine -Learning and Chemicogenomics Approach Defi nes and Predicts Cross-Talk of Hippo and MAPK Pathways Trang H. Pham 1 , Thijs J. Hagenbeek 1 , Ho-June Lee 1 , Jason Li 2 , Christopher M. Rose 3 , Eva Lin 1 , Mamie Yu 1 , Scott E. Martin1 , Robert Piskol 2 , Jennifer A. Lacap 4 , Deepak Sampath 4 , Victoria C. Pham 3 , Zora Modrusan 5 , Jennie R. Lill3 , Christiaan Klijn 2 , Shiva Malek 1 , Matthew T. Chang 2 , and Anwesha Dey 1 ABSTRACT Hippo pathway dysregulation occurs in multiple cancers through genetic and non- genetic alterations, resulting in translocation of YAP to the nucleus and activation of the TEAD family of transcription factors. Unlike other oncogenic pathways such as RAS, defi ning tumors that are Hippo pathway–dependent is far more complex due to the lack of hotspot genetic alterations. Here, we developed a machine-learning framework to identify a robust, cancer type–agnostic gene expression signature to quantitate Hippo pathway activity and cross-talk as well as predict YAP/TEAD dependency across cancers. Further, through chemical genetic interaction screens and multiomics analyses, we discover a direct interaction between MAPK signaling and TEAD stability such that knockdown of YAP combined with MEK inhibition results in robust inhibition of tumor cell growth in Hippo dysregulated tumors. This multifaceted approach underscores how computational models combined with experimental studies can inform precision medicine approaches including predictive diagnostics and combination strategies. SIGNIFICANCE: An integrated chemicogenomics strategy was developed to identify a lineage- independent signature for the Hippo pathway in cancers. -
Semaphorin 4D Promotes Skeletal Metastasis in Breast Cancer
UCLA UCLA Previously Published Works Title Semaphorin 4D Promotes Skeletal Metastasis in Breast Cancer. Permalink https://escholarship.org/uc/item/1vj106ww Journal PloS one, 11(2) ISSN 1932-6203 Authors Yang, Ying-Hua Buhamrah, Asma Schneider, Abraham et al. Publication Date 2016 DOI 10.1371/journal.pone.0150151 Peer reviewed eScholarship.org Powered by the California Digital Library University of California RESEARCH ARTICLE Semaphorin 4D Promotes Skeletal Metastasis in Breast Cancer Ying-Hua Yang1, Asma Buhamrah1, Abraham Schneider1,2, Yi-Ling Lin3, Hua Zhou1, Amr Bugshan1, John R. Basile1,2* 1 Department of Oncology and Diagnostic Sciences, University of Maryland Dental School, Baltimore, Maryland, United States of America, 2 Greenebaum Cancer Center, Baltimore, Maryland, United States of America, 3 Division of Diagnostic and Surgical Sciences, School of Dentistry, University of California Los Angeles, Los Angeles, California, United States of America * [email protected] Abstract Bone density is controlled by interactions between osteoclasts, which resorb bone, and osteoblasts, which deposit it. The semaphorins and their receptors, the plexins, originally shown to function in the immune system and to provide chemotactic cues for axon guid- ance, are now known to play a role in this process as well. Emerging data have identified OPEN ACCESS Semaphorin 4D (Sema4D) as a product of osteoclasts acting through its receptor Plexin-B1 on osteoblasts to inhibit their function, tipping the balance of bone homeostasis in favor of Citation: Yang Y-H, Buhamrah A, Schneider A, Lin Y- resorption. Breast cancers and other epithelial malignancies overexpress Sema4D, so we L, Zhou H, Bugshan A, et al. (2016) Semaphorin 4D Promotes Skeletal Metastasis in Breast Cancer. -
An Extracellular Site on Tetraspanin CD151 Determines Α3 and Α6
JCBArticle An extracellular site on tetraspanin CD151 determines ␣3 and ␣6 integrin–dependent cellular morphology Alexander R. Kazarov, Xiuwei Yang, Christopher S. Stipp, Bantoo Sehgal, and Martin E. Hemler Dana-Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, MA 02115 he ␣31 integrin shows strong, stoichiometric, direct Brij 96–resistant) were independent of the QRD/TS151r lateral association with the tetraspanin CD151. As site, occurred late in biosynthesis, and involved mature T shown here, an extracellular CD151 site (QRD194–196) integrin subunits. Presence of the CD151–QRD194–196→INF is required for strong (i.e., Triton X-100–resistant) ␣31 mutant disrupted ␣3 and ␣6 integrin–dependent formation association and for maintenance of a key CD151 epitope of a network of cellular cables by Cos7 or NIH3T3 cells on (defined by monoclonal antibody TS151r) that is blocked basement membrane Matrigel and markedly altered cell upon ␣3 integrin association. Strong CD151 association spreading. These results provide definitive evidence that with integrin ␣61 also required the QRD194–196 site and strong lateral CD151–integrin association is functionally masked the TS151r epitope. For both ␣3 and ␣6 integrins, important, identify CD151 as a key player during ␣3 and strong QRD/TS151r-dependent CD151 association occurred ␣6 integrin–dependent matrix remodeling and cell spreading, early in biosynthesis and involved ␣ subunit precursor and support a model of CD151 as a transmembrane linker forms. In contrast, weaker associations of CD151 with itself, between extracellular integrin domains and intracellular integrins, or other tetraspanins (Triton X-100–sensitive but cytoskeleton/signaling molecules. -
4-6 Weeks Old Female C57BL/6 Mice Obtained from Jackson Labs Were Used for Cell Isolation
Methods Mice: 4-6 weeks old female C57BL/6 mice obtained from Jackson labs were used for cell isolation. Female Foxp3-IRES-GFP reporter mice (1), backcrossed to B6/C57 background for 10 generations, were used for the isolation of naïve CD4 and naïve CD8 cells for the RNAseq experiments. The mice were housed in pathogen-free animal facility in the La Jolla Institute for Allergy and Immunology and were used according to protocols approved by the Institutional Animal Care and use Committee. Preparation of cells: Subsets of thymocytes were isolated by cell sorting as previously described (2), after cell surface staining using CD4 (GK1.5), CD8 (53-6.7), CD3ε (145- 2C11), CD24 (M1/69) (all from Biolegend). DP cells: CD4+CD8 int/hi; CD4 SP cells: CD4CD3 hi, CD24 int/lo; CD8 SP cells: CD8 int/hi CD4 CD3 hi, CD24 int/lo (Fig S2). Peripheral subsets were isolated after pooling spleen and lymph nodes. T cells were enriched by negative isolation using Dynabeads (Dynabeads untouched mouse T cells, 11413D, Invitrogen). After surface staining for CD4 (GK1.5), CD8 (53-6.7), CD62L (MEL-14), CD25 (PC61) and CD44 (IM7), naïve CD4+CD62L hiCD25-CD44lo and naïve CD8+CD62L hiCD25-CD44lo were obtained by sorting (BD FACS Aria). Additionally, for the RNAseq experiments, CD4 and CD8 naïve cells were isolated by sorting T cells from the Foxp3- IRES-GFP mice: CD4+CD62LhiCD25–CD44lo GFP(FOXP3)– and CD8+CD62LhiCD25– CD44lo GFP(FOXP3)– (antibodies were from Biolegend). In some cases, naïve CD4 cells were cultured in vitro under Th1 or Th2 polarizing conditions (3, 4). -
Retinoid X Receptor Suppresses a Metastasis-Promoting Transcriptional Program in Myeloid Cells Via a Ligand-Insensitive Mechanism
Retinoid X receptor suppresses a metastasis-promoting transcriptional program in myeloid cells via a ligand-insensitive mechanism Mate Kissa, Zsolt Czimmerera,b, Gergely Nagyb, Pawel Bieniasz-Krzywiecc,d, Manuel Ehlingc,d, Attila Papa, Szilard Poliskaa,e, Pal Botof, Petros Tzerpose, Attila Horvatha, Zsuzsanna Kolostyaka, Bence Danielg, Istvan Szatmarif, Massimiliano Mazzonec,d, and Laszlo Nagya,b,g,1 aNuclear Receptor Research Laboratory, Department of Biochemistry and Molecular Biology, University of Debrecen, 4032 Debrecen, Hungary; bMTA-DE “Lendület” Immunogenomics Research Group, University of Debrecen, 4032 Debrecen, Hungary; cLaboratory of Tumor Inflammation and Angiogenesis, Center for Cancer Biology, VIB, 3000 Leuven, Belgium; dLaboratory of Tumor Inflammation and Angiogenesis, Department of Oncology, KU Leuven, 3000 Leuven, Belgium; eUD-GenoMed Ltd., 4032 Debrecen, Hungary; fStem Cell Differentiation Laboratory, Department of Biochemistry and Molecular Biology, University of Debrecen, 4032 Debrecen, Hungary; and gGenomic Control of Metabolism Program, Sanford Burnham Prebys Medical Discovery Institute at Lake Nona, Orlando, FL 32827 Edited by Bert W. O’Malley, Baylor College of Medicine, Houston, TX, and approved August 18, 2017 (received for review January 18, 2017) Retinoid X receptor (RXR) regulates several key functions in myeloid and identified a network of RXR-bound enhancers that control cells, including inflammatory responses, phagocytosis, chemokine angiogenic genes including Vegfa, Hbegf, Litaf,andHipk2 (9). secretion, and proangiogenic activity. Its importance, however, in Activation of these enhancers by RXR induced a proangiogenic tumor-associated myeloid cells is unknown. In this study, we transcriptional program and phenotype (9). Interestingly, we demonstrate that deletion of RXR in myeloid cells enhances lung found that half of the 5,200 RXR-occupied genomic sites were metastasis formation while not affecting primary tumor growth. -
Oestrogen Receptor α AF-1 and AF-2 Domains Have Cell
ARTICLE DOI: 10.1038/s41467-018-07175-0 OPEN Oestrogen receptor α AF-1 and AF-2 domains have cell population-specific functions in the mammary epithelium Stéphanie Cagnet1, Dalya Ataca 1, George Sflomos1, Patrick Aouad1, Sonia Schuepbach-Mallepell2, Henry Hugues3, Andrée Krust4, Ayyakkannu Ayyanan1, Valentina Scabia1 & Cathrin Brisken 1 α α 1234567890():,; Oestrogen receptor (ER ) is a transcription factor with ligand-independent and ligand- dependent activation functions (AF)-1 and -2. Oestrogens control postnatal mammary gland development acting on a subset of mammary epithelial cells (MECs), termed sensor cells, which are ERα-positive by immunohistochemistry (IHC) and secrete paracrine factors, which stimulate ERα-negative responder cells. Here we show that deletion of AF-1 or AF-2 blocks pubertal ductal growth and subsequent development because both are required for expres- sion of essential paracrine mediators. Thirty percent of the luminal cells are ERα-negative by IHC but express Esr1 transcripts. This low level ERα expression through AF-2 is essential for cell expansion during puberty and growth-inhibitory during pregnancy. Cell-intrinsic ERα is not required for cell proliferation nor for secretory differentiation but controls transcript levels of cell motility and cell adhesion genes and a stem cell and epithelial mesenchymal transition (EMT) signature identifying ERα as a key regulator of mammary epithelial cell plasticity. 1 Swiss Institute for Experimental Cancer Research, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland. 2 Department of Biochemistry, University of Lausanne, CH-1066 Epalinges, Switzerland. 3 Centre Hospitalier Universitaire Vaudois, Department of Laboratory Medecine, University Hospital of Lausanne, CH-1011 Lausanne, Switzerland. -
Page 1 Supplemental Table I Upin WTVG Upin Humlowfb FAR1
Supplemental Table I UPinWTvG UPinHuMlowFB overlap FAR1 CD209 PLEKHO2 B2M IL27 GCLC CALR HMGN2P46 ME1 XPO1 CLEC1A NEK6 PDIA3 HSD17B14 TMEM106A SERPINH1 NSUN7 KCNJ15 PLEKHO2 SEMA6B SH3PXD2B HSPD1 BAALC RHOU SYVN1 CEACAM4 TGFBI DNAJB9 KATNAL2 CTSZ SLC25A19 CCDC175 SULF2 MHCII CARD14 P2RY6 MDN1 TDO2 CD74 GCLC FCAR HLA-DQB1 PTPN2 GLDN CD14 CHORDC1 MMP7 CSF2RB LOX CLEC5A MRC1 STIP1 ZMYND15 ITGAX BPIFB1 ITLN1 SLAMF7 ME1 DKK2 CD84 PDIA6 FAM124A FCGR2A HYOU1 F3 CLEC10A NLRC5 DZIP1L IFI30 NEK6 CECR6 CLEC4A SLC39A14 NDP CLEC7A TMEM106AFCGR1A TFEC KCNJ15 CCL7 C1QC SH3PXD2B CRABP2 C1QA RHOU PIPOX FOLR2 LRP2 CCL2 CH25H MVD VSIG4 C1QB TGFBI LINC01010 SIGLEC1 NFKB2 DPRXP4 CTSS C5 FAM20A CCR1 HSP90B1 ANKRD29 SLAMF8 ALDH18A1 OCSTAMP MS4A7 EDEM1 TGM2 HK3 CTSZ TM4SF19 CXCL10 C6 TRPV4 CTSK AACS CCL8 MSR1 PPA1 CCL1 STEAP4 PIK3R5 KCNE1 CXCL9 RASAL3 SLC9A7P1 MS4A6A DOCK11 CHI3L1 TIMP1 BHLHE40 LOC731424 CD209 HCLS1 DCSTAMP CCL7 FASN MSR1 PDCD1LG2 PDIA4 IL31RA CCL2 ITK CXCL3 CXCL2 CRELD2 TREM2 C15orf48 SFTPD MGST1 GPR84 BCL3 METTL7B CXCL5 SULF2 TMEM86A OCSTAMP CYP51A1 A2M SERPINA1 CREB3L1 AQP9 MMP12 DUSP2 NUPR1 CCL8 ADAM8 FHAD1 CCL24 P2RY6 YPEL4 FBP1 KCNAB2 FBP1 NA NFKBIE LOC100506585 NA FSCN1 CXCL16 NA MANF RAB13 NA SLC5A3 LOC391322 NA CTSC IL8 NA COTL1 MS4A4A NA HSPA5 SERPING1 NA MUC5B PLA2G4C NA CD74 CA12 NA HLA-DQB1 GBP1P1 NA SLC7A2 C11orf45 NA FABP5 ACVRL1 NA CIITA SPP1 NA RAB3IL1 TLN2 NA HSPE1 NDRG2 NA SCD C15orf48 NA ITIH4 KCNJ15 NA SERPINA3 MEIS3P1 NA LAG3 IL1RN NA FOXM1 HNMT NA CD14 CYP27B1 NA RRM2 CDCP1 NA ABCD2 FOLR2 NA FCRL2 ECM1 NA PDE3B ADAMDEC1 -
Supplementary Material DNA Methylation in Inflammatory Pathways Modifies the Association Between BMI and Adult-Onset Non- Atopic
Supplementary Material DNA Methylation in Inflammatory Pathways Modifies the Association between BMI and Adult-Onset Non- Atopic Asthma Ayoung Jeong 1,2, Medea Imboden 1,2, Akram Ghantous 3, Alexei Novoloaca 3, Anne-Elie Carsin 4,5,6, Manolis Kogevinas 4,5,6, Christian Schindler 1,2, Gianfranco Lovison 7, Zdenko Herceg 3, Cyrille Cuenin 3, Roel Vermeulen 8, Deborah Jarvis 9, André F. S. Amaral 9, Florian Kronenberg 10, Paolo Vineis 11,12 and Nicole Probst-Hensch 1,2,* 1 Swiss Tropical and Public Health Institute, 4051 Basel, Switzerland; [email protected] (A.J.); [email protected] (M.I.); [email protected] (C.S.) 2 Department of Public Health, University of Basel, 4001 Basel, Switzerland 3 International Agency for Research on Cancer, 69372 Lyon, France; [email protected] (A.G.); [email protected] (A.N.); [email protected] (Z.H.); [email protected] (C.C.) 4 ISGlobal, Barcelona Institute for Global Health, 08003 Barcelona, Spain; [email protected] (A.-E.C.); [email protected] (M.K.) 5 Universitat Pompeu Fabra (UPF), 08002 Barcelona, Spain 6 CIBER Epidemiología y Salud Pública (CIBERESP), 08005 Barcelona, Spain 7 Department of Economics, Business and Statistics, University of Palermo, 90128 Palermo, Italy; [email protected] 8 Environmental Epidemiology Division, Utrecht University, Institute for Risk Assessment Sciences, 3584CM Utrecht, Netherlands; [email protected] 9 Population Health and Occupational Disease, National Heart and Lung Institute, Imperial College, SW3 6LR London, UK; [email protected] (D.J.); [email protected] (A.F.S.A.) 10 Division of Genetic Epidemiology, Medical University of Innsbruck, 6020 Innsbruck, Austria; [email protected] 11 MRC-PHE Centre for Environment and Health, School of Public Health, Imperial College London, W2 1PG London, UK; [email protected] 12 Italian Institute for Genomic Medicine (IIGM), 10126 Turin, Italy * Correspondence: [email protected]; Tel.: +41-61-284-8378 Int. -
PRODUCT SPECIFICATION Anti-TSPAN3
Anti-TSPAN3 Product Datasheet Polyclonal Antibody PRODUCT SPECIFICATION Product Name Anti-TSPAN3 Product Number HPA015996 Gene Description tetraspanin 3 Clonality Polyclonal Isotype IgG Host Rabbit Antigen Sequence Recombinant Protein Epitope Signature Tag (PrEST) antigen sequence: NGTNPDAASRAIDYVQRQLHCCGIHNYSDWENTDWFKETKNQSVPLSCCR ETASNCNGSLAHPSDLYAEGCEALVVKKLQEI Purification Method Affinity purified using the PrEST antigen as affinity ligand Verified Species Human Reactivity Recommended IHC (Immunohistochemistry) Applications - Antibody dilution: 1:20 - 1:50 - Retrieval method: HIER pH6 ICC-IF (Immunofluorescence) - Fixation/Permeabilization: PFA/Triton X-100 - Working concentration: 0.25-2 µg/ml Characterization Data Available at atlasantibodies.com/products/HPA015996 Buffer 40% glycerol and PBS (pH 7.2). 0.02% sodium azide is added as preservative. Concentration Lot dependent Storage Store at +4°C for short term storage. Long time storage is recommended at -20°C. Notes Gently mix before use. Optimal concentrations and conditions for each application should be determined by the user. For protocols, additional product information, such as images and references, see atlasantibodies.com. Product of Sweden. For research use only. Not intended for pharmaceutical development, diagnostic, therapeutic or any in vivo use. No products from Atlas Antibodies may be resold, modified for resale or used to manufacture commercial products without prior written approval from Atlas Antibodies AB. Warranty: The products supplied by Atlas Antibodies are warranted to meet stated product specifications and to conform to label descriptions when used and stored properly. Unless otherwise stated, this warranty is limited to one year from date of sales for products used, handled and stored according to Atlas Antibodies AB's instructions. Atlas Antibodies AB's sole liability is limited to replacement of the product or refund of the purchase price. -
Complexes of Tetraspanins with Integrins: More Than Meets the Eye
COMMENTARY 4143 Complexes of tetraspanins with integrins: more than meets the eye Fedor Berditchevski CRC Institute for Cancer Studies, The University of Birmingham, Edgbaston, Birmingham, B15 2TA, UK Author for correspondence (e-mail: [email protected]) Journal of Cell Science 114, 4143-4151 (2001) © The Company of Biologists Ltd Summary The transmembrane proteins of the tetraspanin membrane, integrin-tetraspanin signalling complexes superfamily are implicated in a diverse range of biological are partitioned into specific microdomains proximal to phenomena, including cell motility, metastasis, cell cholesterol-rich lipid rafts. A substantial fraction of proliferation and differentiation. The tetraspanins are tetraspanins colocalise with integrins in various associated with adhesion receptors of the integrin family intracellular vesicular compartments. It is proposed that and regulate integrin-dependent cell migration. In cells tetraspanins can influence cell migration by one of the attached to the extracellular matrix, the integrin- following mechanisms: (1) modulation of integrin tetraspanin adhesion complexes are clustered into a distinct signalling; (2) compartmentalisation of integrins on the cell type of adhesion structure at the cell periphery. Various surface; or (3) direction of intracellular trafficking and tetraspanins are associated with phosphatidylinositol 4- recycling of integrins. kinase and protein kinase C isoforms, and they may facilitate assembly of signalling complexes by tethering these enzymes to integrin heterodimers. At the plasma Key words: Tetraspanin, Integrin, Migration, Signalling Introduction relatively well conserved among tetraspanins (Fig. 1). A Tetraspanins (also referred to as tetraspans or TM4SF proteins) combination of all the above features distinguishes tetraspanins are a family of widely expressed four-transmembrane-domain from a diverse group of proteins that have four transmembrane proteins. -
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UC Berkeley UC Berkeley Electronic Theses and Dissertations Title Chemical glycoproteomics for identification and discovery of glycoprotein alterations in human cancer Permalink https://escholarship.org/uc/item/0t47b9ws Author Spiciarich, David Publication Date 2017 Peer reviewed|Thesis/dissertation eScholarship.org Powered by the California Digital Library University of California Chemical glycoproteomics for identification and discovery of glycoprotein alterations in human cancer by David Spiciarich A dissertation submitted in partial satisfaction of the requirements for the degree Doctor of Philosophy in Chemistry in the Graduate Division of the University of California, Berkeley Committee in charge: Professor Carolyn R. Bertozzi, Co-Chair Professor David E. Wemmer, Co-Chair Professor Matthew B. Francis Professor Amy E. Herr Fall 2017 Chemical glycoproteomics for identification and discovery of glycoprotein alterations in human cancer © 2017 by David Spiciarich Abstract Chemical glycoproteomics for identification and discovery of glycoprotein alterations in human cancer by David Spiciarich Doctor of Philosophy in Chemistry University of California, Berkeley Professor Carolyn R. Bertozzi, Co-Chair Professor David E. Wemmer, Co-Chair Changes in glycosylation have long been appreciated to be part of the cancer phenotype; sialylated glycans are found at elevated levels on many types of cancer and have been implicated in disease progression. However, the specific glycoproteins that contribute to cell surface sialylation are not well characterized, specifically in bona fide human cancer. Metabolic and bioorthogonal labeling methods have previously enabled enrichment and identification of sialoglycoproteins from cultured cells and model organisms. The goal of this work was to develop technologies that can be used for detecting changes in glycoproteins in clinical models of human cancer.