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BSSS
Nom chimique: Bis(sulfosuccinimidyl) suberate sodium salt // Synonymes: Sulfo-DSS, BS3, Suberic acid bis(3-sulfo-N-hydroxysuccinimide ester) sodium salt; Component: CAS 127634-19-9
- n° Art.:RL-2770
- n° CAS:127634-19-9
- Formule:C16H18N2Na2O14S2
- Storage temperature:-20°C
- Masse moléculaire:572,43 g/mol
from 350,00 €
description
This molecule carries amino reactive Sulfo-NHS esters on both ends and is a water soluble, homo-bifunctional protein cross-linker (spacer length: 11.4 Å). Due to its water solubility, conjugation reactions conveniently can take place at physiological conditions. This 8-atom spacer is non-cleavable and the molecule is not cell membrane permeable. It can be used to prepare antibody-protein conjugates, for crosslinking cell surface proteins, and for covalently orienting antibody to an immobilized Protein A or Protein G resin.
General BSSS Cross-linking Protocol:
1. Allow vial of BSSS to fully equilibrate to ambient temperature before opening to prevent condensation inside the vial (BS3 is moisture-sensitive).
2. Immediately before use, prepare a 50mM solution of BSSS, by dissolving 10 mg BSSS in 350 ìL of 25 mM Sodium Phosphate, pH 7.4 (do not use amine containing buffers for the conjugation reaction).
3. Add BSSS solution (20-fold excess cross-linker to protein) to the protein sample so that the final concentration is between 0.5 to 5 mM.
4. Allow the sample to react at room temperature for 45 minutes to 1 hour. Allow slightly longer if reaction must be done on ice (this reaction rate is only slightly slower at low temperatures).
5. Quench and unreacted BSSS with 25 mM to 60 mM Tris and allow to react for 10-15 minutes at room temperature.
6. Desalt sample to remove unreacted BSSS, i.e. gel filtration, dialysis, etc.
references
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The Golgi-associated hook3 protein is a member of a novel family of microtubule-binding proteins; Jason H. Walenta, Aaron J. Didier, Xinran Liu, Helmut Krämer; Journal of Cell Biology 2001; 152(5): 923-934.DOI: .org/10.1083/jcb.152.5.923
Rapamycin Potentiates Transforming Growth Factor -Induced Growth Arrest in Nontransformed, Oncogene-Transformed, and Human Cancer Cells. Brian K. Law, Anna Chytil, Nancy Dumont, Elizabeth G. Hamilton, Mary E. Waltner-Law, Mary E. Aakre, Cassondra Covington, Harold L. Moses; Mol. Cell. Biol. 2002; 22: 8184-8198. DOI: 10.1128/MCB.22.23.8184-8198.2002
Mapping low‐resolution three‐dimensional protein structures using chemical cross‐linking and Fourier transform ion‐cyclotron resonance mass spectrometry. Gry H. Dihazi, Andrea Sinz; Rapid Commun. Mass Spectrom. 2003; 17: 2005-2014. DOI: org/10.1002/rcm.1144
Chemical cross‐linking and mass spectrometry for mapping three‐dimensional structures of proteins and protein complexes. Andrea Sinz; J. Mass Spectrom. 2003; 38(2): 1225-1237. DOI: org/10.1002/jms.559
Mapping the Topology and Determination of a Low-Resolution Three-Dimensional Structure of the Calmodulin−Melittin Complex by Chemical Cross-Linking and High-Resolution FTICRMS: Direct Demonstration of Multiple Binding Modes. Daniela M. Schulz, Christian Ihling, G. Marius Clore, Andrea Sinz; Biochemistry 2004; 43(16): 4703-4715. DOI: org/10.1021/bi036149f
Selective Inactivation of Adrenomedullin over Calcitonin Gene-related Peptide Receptor Function by the Deletion of Amino Acids 14-20 of the Mouse Calcitonin-like Receptor. Daniela Koller, Lars M. Ittner, Roman Muff, Knut Husmann, Jan A. Fischer, Walter Born; J. Biol. Chem. 2004; 279: 20387-20391. DOI: 10.1074/jbc.M313058200
Mactinin, a fragment of cytoskeletal alpha-actinin, is a novel inducer of heat shock protein (Hsp)-90 mediated monocyte activation; Sharon D Luikart, Angela Panoskaltsis-Mortari, Timothy Hinkel, Robert T Perri, Kalpna Gupta, Theodore R Oegema, Pankaj Gupta; BMC Cell Biology 2009; 10: 60. DOI: org/10.1186/1471-2121-10-60
The program for processing newly synthesized histones H3.1 and H4; Eric I. Campos, Jeffrey Fillingham, Guohong Li, Haiyan Zheng, Philipp Voigt, Wei-Hung W Kuo, Harshika Seepany, Zhonghua Gao, Loren A Day, Jack F Greenblatt, Danny Reinberg; Nature Structural & Molecular Biology 2010; 17(11): 1343-1351. DOI: org/10.1038/nsmb.1911
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Mps1 directs the assembly of Cdc20 inhibitory complexes during interphase and mitosis to control M phase timing and spindle checkpoint signaling; John Maciejowski, Kelly A. George, Marie-Emilie Terret, Chao Zhang, Kevan M. Shokat, Prasad V. Jallepalli; J. Cell. Biol. 2010; 190(1): 89-100. DOI: org/10.1083/jcb.201001050
Protection against protein aggregation by alpha-crystalline as a mechanism of preconditioning; Ferns, J. E., Theisen, C. S., Fibuch, E. E., Seidler, N. W.; Neurochemical research 2012; 37: 244-252. DOI: org/10.1007/s11064-011-0601-4
Identification of IGPR-1 as a novel adhesion molecule involved in angiogenesis. Nader Rahimi, Kobra Rezazadeh, John E. Mahoney, Edward Hartsough, Rosana D. Meyer; Mol Biol Cell. 2012; 23(9): 1646–1656. DOI: 10.1091/mbc.E11-11-0934
TWEAK-Independent Fn14 Self-Association and NF-êB Activation Is Mediated by the C-Terminal Region of the Fn14 Cytoplasmic Domain. Sharron A. N. Brown, Emily Cheng, Mark S. Williams, Jeffrey A. Winkles; PLOS ONE 2013; 8(6): e65248. DOI: org/10.1371/journal.pone.0065248
ZRF1 controls the retinoic acid pathway and regulates leukemogenic potential in acute myeloid leukemia; S. Demajo, I. Uribesalgo, A. Gutiérrez, C. Ballaré, S. Capdevila, M. Roth, J. Zuber, J. Martín-Caballero, L. Di Croce; Oncogene 2014; 33: 5501-5510. DOI: org/10.1038/onc.2013.50
Ubiquitin Associates with the N-Terminal Domain of Nerve Growth Factor: The Role of Copper(II) Ions. Lanza V., Travaglia A., Malgieri G., Fattorusso R., Grasso G., Di Natale G., Zito V., Arena G., Milardi D., Rizzarelli E.; Chemistry 2016; 22(49): 17767-17775. DOI: 10.1002/chem.201603650
Potentiation of Surface Stability of AMPA Receptors by Sulfhydryl Compounds: A Redox-Independent Effect by Disrupting Palmitoylation. Han J., Zhang H., Wang S., Zhou J., Luo Y., Long L.H., Hu Z.L., Wang F., Chen J.G., Wu P.F.; Neurochem Res. 2016; 41(11): 2890-2903. DOI: 10.1007/s11064-016-2006-x
Dramatic Domain Rearrangements of the Cyanobacterial Orange Carotenoid Protein upon Photoactivation. Haijun Liu, Hao Zhang, Gregory S. Orf, Yue Lu, Jing Jiang, Jeremy D. King, Nathan R. Wolf, Michael L. Gross, Robert E. Blankenshipa; Biochemistry 2016; 55(7): 1003–1009. DOI: 10.1021/acs.biochem.6b00013
Nuclear Speckle-related Protein 70 Binds to Serine/Arginine-rich Splicing Factors 1 and 2 via an Arginine/Serine-like Region and Counteracts Their Alternative Splicing Activity. Chang-Hyun Kim, Young-Dae Kim, Eun-Kyung Choi, Hye-Ran Kim, Bo-Ra Na, Sin-Hyeog Im, Chang-Duk Jun; The Journal of Biological Chemistry 2016; 291: 6169-6181. DOI: 10.1074/jbc.M115.689414
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