bioRxiv Science⌕ Search

bioRxiv · 10.1101/221523

Validating Antibodies for Quantitative Western Blot Measurements with Microwestern Array

Abstract

Western blotting is often considered a semi-quantitative or even qualitative assay for assessing changes in protein or protein post-translational modification levels. Fluorescence-based measurement enables acquisition of quantitative data in principal, but requires determining the linear range of detection for each antibody--a labor-intensive task. Here, we describe the use of a high-throughput western blotting technique called microwestern array to more rapidly evaluate suitable conditions for quantitative western blotting with particular antibodies. We can evaluate up to 192 antibody/dilution/replicate combinations on a single standard size gel with a seven-point, two-fold lysate dilution series (~100-fold range). Pilot experiments demonstrate a surprisingly high proportion of investigated antibodies (17/22) are suitable for quantitative use, and that lack of validity might often be a consequence of lysate composition rather than antibody quality. Linear range for all validated antibodies is at least 8-fold, and in some cases nearly two orders of magnitude. That range could be greater as the presented tests did not find a limit for many antibodies. We find that phospho-specific and total antibodies do not have discernable trend differences in linear range or limit of detection, but total antibodies generally required higher working concentrations, suggesting phospho-specific antibodies may be generally higher affinity. Importantly, we demonstrate that results from microwestern analyses scale to normal \"macro\" western for a subset of antibodies. These data indicate that with initial validation, many antibodies can be readily used quantitatively in a reproducible manner. Antibody validation data and standard operating procedures are available online (www.birtwistlelab.com/protocols and www.dtoxs.org).

Source connections

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Koch, R. J., Barrette, A. M., Stern, A. D., Hu, B., Azeloglu, E. U., Iyengar, R., Birtwistle, M. R.. 2017-11-17. Validating Antibodies for Quantitative Western Blot Measurements with Microwestern Array. https://doi.org/10.1101/221523

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

Structure of influenza D virus NS1 reveals a novel Zn-binding site and ssRNA-binding activity

Influenza D virus (IDV) is an emerging pathogen associated with bovine respiratory disease and has potential for zoonotic transmission. Although nonstructural protein 1 (NS1) is a major virulence factor in influenza A and B viruses, the structure and function of IDV NS1 remain poorly defined. Here, we determined crystal structures of the IDV NS1 N-terminal RNA-binding domain (NTD) and C-terminal effector domain (CTD). The NTD retains the conserved homodimeric six-helix fold, whereas the CTD adopts a distinct architecture containing a novel Zn2+-binding site. IDV NS1 CTD preferentially binds single-stranded RNA, and mutagenesis identified lysine and arginine residues critical for this activity. Single-residue substitutions disrupting either the Zn2+-binding site or RNA-binding interface prevented recovery of infectious recombinant IDV. These findings reveal distinct structural and functional features of IDV NS1 and establish the importance of CTD integrity for viral replication. Conservation of key CTD residues in influenza C virus NS1 suggests shared structural features that distinguish influenza C and D virus NS1 proteins from their influenza A and B counterparts.

biochemistry↗

Recognition of the centromere-binding protein Ndc10 by Scm3HJURP directs Cse4CENP-A deposition at native centromeres

Kinetochores connect centromeres to spindle microtubules, ensuring accurate chromosome segregation. Kinetochore assembly at centromeres depends on deposition of CENP-A, a histone H3 variant. Despite considerable progress, how CENP-A is specifically assembled on native centromeres remains an open question. Centromere-specific assembly of CENP-A occurs spontaneously in a cell-free extract system from the yeast Saccharomyces cerevisiae, but with low efficiency, suggesting that one or more factors are limiting. Here, we show Scm3HJURP, a specific chaperone for the centromeric histone Cse4CENP-A, is one such limiting component. The addition of a complex of Scm3, Cse4 and histone H4 strongly stimulates Cse4 assembly in a centromeric DNA sequence- and dose-dependent manner; in addition, improvements in both Cse4 and kinetochore assembly were more prominent in mitotic versus interphase (G1) extracts. Using the complemented cell-free reconstitution system, we show that distinct Scm3 interfaces with Cse4 and with the Ndc10 subunit of the yeast centromere DNA sequence-recognizing CBF3 complex are essential for centromere-specific Cse4 assembly and cell viability. Thus, recognition of Ndc10 directs Scm3-dependent and locus-specific centromeric histone deposition.

biochemistry↗

Heterogeneous primary nucleation determines Aβ42 fibrilstructure.

The current developments in the field of amyloid fibril structure determination has revealed multiple structures for peptides of identical sequence. This may reflect variations in sample environment or similar nucleation barriers for multiple folds. Here we investigate the influence of aggregating surface and during fibril formation from monomeric amyloid {beta} peptide (A{beta}42). The fibril structures formed in identical solutions in glass vials / bottles and PEGylated polystyrene 96-well plates display very different monomer fold within the fibrils. This is a clear indication of extremely slow homogeneous primary nucleation. Instead, heterogeneous primary nucleation at vessel walls or at the three-line interface between air, water and vessel wall dictate the outcome in each solution, where the initially formed structure is propagated through elongation and secondary nucleation. The results further imply that the conversion towards the thermodynamically stable fibril structure one is slow for A{beta}42.

biochemistry↗