{"product_id":"chemokine-glycosaminoglycan-interactions-alexandra-r-lucas-9781071628348","title":"Chemokine-Glycosaminoglycan Interactions: Methods and Protocols","description":"\u003cp\u003e\u003cb\u003e1. A Surgical Approach to Hindlimb Suspension: A Mouse Model of Disuse-Induced Atrophy\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Laura Kutz, Tong Zhou, Qi Chen, and Hua Zhu\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e2. Remote Ischemic Pre-Conditioning (RIPC)\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Kyung Eun Lee, Jongsoo Kim, Ki Ho Park, Jianjie Ma, and Hua Zhu\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3. Mouse Corneal Transplantation\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Peng Chen, Ki Ho Park, Liqiang Zhang, Alexandra R. Lucas, Heather L. Chandler, and Hua Zhu\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e4. Analysis of Chemokine-to-GAG Interactions in Model of Donor Renal Allograft Transplant\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Yanlin Ma and Hao Chen\u003c\/p\u003e \u003cp\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5. Mouse Models of Renal Allograft Transplant Rejection: Methods to Investigate Chemokine: GAG Interaction and Therapeutic Blockade\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Isabela R. Zanetti, Liqiang Zhang, Michelle Burgin, Jacquelyn Kilbourne, Jordan R. Yaron, David Fonseca, and Alexandra R. Lucas\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e6. Ex Vivo Perfusion System to Analyze Chemokine-Driven Leukocyte Adhesion\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Sanne L. Maas, Remco T.A. Megens, and Emiel P.C. van der Vorst\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e7. In Vitro (Trans)migration Experiment Using Chemokines as Stimulatory Factor\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Sanne L. Maas and Emiel P.C. van der Vorst\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e8. \u003c\/b\u003e\u003cb\u003eThe Use of Campenot Trichambers for the Study of Peripheral Neuronal Growth and Survival in Presence of Thrombotic Factors and Serpins\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Wesley M. Tierney and Ian B. Hogue\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e9. Flow Cytometry Analysis of Immune Cell Responses\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Kavita R. Manhas and Joseph N. Blattman\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e10. \u003c\/b\u003e\u003cb\u003eDetection of Chemokine Binding Proteins Association to Cell Surface Glycosaminoglycans by Flow Cell Cytometry and Indirect Immunofluorescence\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Bruno Hernaez and Antonio Alcamí\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e11. Protein Microarrays and Their Fabrication\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Mahasish Shome and Joshua LaBaer\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e12. NMR Methods for Characterization of Glycosaminoglycan-Chemokine Interactions\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Vitor H. Pomin and Krishna Rajarathnam\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e13. Glycosaminoglycan Analysis: Purification, Structural Profiling, and GAG-Protein Interactions\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Amrita Basu and Ryan J. Weiss\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e14. Isolation and Compositional Analysis of Glycosaminoglycans\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Stephanie Archer-Hartmann, Lauren E. Pepi, Christian Heiss, and Parastoo Azadi\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e15. How to Design Peptides\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Joseph Dodd-o, Amanda M. Acevedo-Jake, Abdul-Rahman Azizogli, Vikram Khipple Mulligan, and Vivek A. Kumar\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e16. \u003c\/b\u003e\u003cb\u003eMethods to Assess Chemokine Binding and Anti-Chemotactic Activity of Virus Proteins\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e Elham Torbati, Gabriella Stuart, Kurt Krause, Chris Brown, and Lyn Wise\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e\u003cb\u003e17. Producing Biologics with Defined N-Glycosylation in Plants\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cbr\u003e\u003cbr\u003e\u003cb\u003eAuthor:\u003c\/b\u003e Alexandra R. Lucas\u003cbr\u003e\u003cb\u003eISBN-10:\u003c\/b\u003e 1071628348\u003cbr\u003e\u003cb\u003eISBN-13:\u003c\/b\u003e 9781071628348\u003cbr\u003e\u003cb\u003ePublisher:\u003c\/b\u003e Humana\u003cbr\u003e\u003cb\u003eLanguage:\u003c\/b\u003e English\u003cbr\u003e\u003cb\u003ePublished:\u003c\/b\u003e 11\/15\/2022\u003cbr\u003e\u003cb\u003ePages:\u003c\/b\u003e 262\u003cbr\u003e\u003cb\u003eFormat:\u003c\/b\u003e Hardcover\u003cbr\u003e\u003cb\u003eWeight:\u003c\/b\u003e 1.55lbs\u003cbr\u003e\u003cb\u003eSize:\u003c\/b\u003e 10.00h x 7.00w x 0.69d\u003c\/p\u003e","brand":"Alexandra R. 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