Site-Specific Immobilization of Antibodies to Protein G-Derivatized Solid Supports

2000 ◽  
pp. 41-48 ◽  
Author(s):  
Frank J. Podlaski ◽  
Alvin S. Stern
Keyword(s):  
Protein G ◽  
Solid Supports ◽  
Site Specific

Comparison of site-specific coupling chemistry for antibody immobilization on different solid supports

1991 ◽  
Vol 542 ◽  
pp. 41-54 ◽  
Author(s):  
Lin Jinn-Nan ◽  
Chang I-Nan ◽  
Joseph D. Andrade ◽  
James N. Herron ◽  
Douglas A. Christensen
Keyword(s):  
Antibody Immobilization ◽  
Solid Supports ◽  
Site Specific

DNAzyme-powered nucleic acid release from solid supports

2020 ◽  
Vol 56 (4) ◽  
pp. 647-650 ◽  
Author(s):  
Ting Cao ◽  
Yongcheng Wang ◽  
Ye Tao ◽  
Lexiang Zhang ◽  
Ying-Lin Zhou ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Polyacrylamide Gel ◽  
Solid Supports ◽  
Site Specific ◽  
Gel Beads ◽  
Acid Release ◽  
Dependent Site

Here, we demonstrate use of a Mg2+-dependent, site-specific DNA enzyme (DNAzyme) to cleave oligos from polyacrylamide gel beads, which is suitable for use in drop-based assays.

Site-Specific Photolabeling of the IgG Fab Fragment Using a Small Protein G Derived Domain

2016 ◽  
Vol 27 (9) ◽  
pp. 2095-2102 ◽  
Author(s):  
Sara Kanje ◽  
Emma von Witting ◽  
Samuel C. C. Chiang ◽  
Yenan T. Bryceson ◽  
Sophia Hober
Keyword(s):  
Protein G ◽  
Fab Fragment ◽  
Site Specific ◽  
Small Protein

Large-cluster and combined fluorescent and gold immunoprobes

1996 ◽  
Vol 54 ◽  
pp. 892-893
Author(s):  
Richard D. Powell ◽  
James F. Hainfeld ◽  
Carol M. R. Halsey ◽  
David L. Spector ◽  
Shelley Kaurin ◽  
...  
Keyword(s):  
Metal Cluster ◽  
Sulfonyl Chloride ◽  
Gel Filtration ◽  
Cross Linking ◽  
Site Specific ◽  
Fab Fragments ◽  
Cluster Label ◽  
Covalently Linked ◽  
Texas Red ◽  
Fold Excess

Two new types of covalently linked, site-specific immunoprobes have been prepared using metal cluster labels, and used to stain components of cells. Combined fluorescein and 1.4 nm “Nanogold” labels were prepared by using the fluorescein-conjugated tris (aryl) phosphine ligand and the amino-substituted ligand in the synthesis of the Nanogold cluster. This cluster label was activated by reaction with a 60-fold excess of (sulfo-Succinimidyl-4-N-maleiniido-cyclohexane-l-carboxylate (sulfo-SMCC) at pH 7.5, separated from excess cross-linking reagent by gel filtration, and mixed in ten-fold excess with Goat Fab’ fragments against mouse IgG (obtained by reduction of F(ab’)2 fragments with 50 mM mercaptoethylamine hydrochloride). Labeled Fab’ fragments were isolated by gel filtration HPLC (Superose-12, Pharmacia). A combined Nanogold and Texas Red label was also prepared, using a Nanogold cluster derivatized with both and its protected analog: the cluster was reacted with an eight-fold excess of Texas Red sulfonyl chloride at pH 9.0, separated from excess Texas Red by gel filtration, then deprotected with HC1 in methanol to yield the amino-substituted label.

The challenge of detecting modifications on proteins

2020 ◽  
Vol 64 (1) ◽  
pp. 135-153 ◽  
Author(s):  
Lauren Elizabeth Smith ◽  
Adelina Rogowska-Wrzesinska
Keyword(s):  
Mass Spectrometry ◽  
Protein Function ◽  
Chemical Properties ◽  
Lysine Acetylation ◽  
Mass Determination ◽  
Post Translational Modifications ◽  
Site Specific ◽  
The Common

Abstract Post-translational modifications (PTMs) are integral to the regulation of protein function, characterising their role in this process is vital to understanding how cells work in both healthy and diseased states. Mass spectrometry (MS) facilitates the mass determination and sequencing of peptides, and thereby also the detection of site-specific PTMs. However, numerous challenges in this field continue to persist. The diverse chemical properties, low abundance, labile nature and instability of many PTMs, in combination with the more practical issues of compatibility with MS and bioinformatics challenges, contribute to the arduous nature of their analysis. In this review, we present an overview of the established MS-based approaches for analysing PTMs and the common complications associated with their investigation, including examples of specific challenges focusing on phosphorylation, lysine acetylation and redox modifications.

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