GeneRulor pG-Transposome

1. Product Introduction

GeneRulor pG-Transposome is a transposome prepared from pG-Transposase. In comparison with GeneRulor pA-Transposome, the design of GeneRulor pG-Transposome further expands the antibody binding range. Its Protein G domain not only has broad affinity for antibodies from multiple species including rabbit, mouse and goat, but also shows significant advantages in binding certain key subtypes, especially mouse IgG1, thus achieving strong and stable binding to a wider range of antibody types. This characteristic makes GeneRulor pG-Transposome have higher versatility and experimental adaptability in targeted chromatin analysis technologies such as CUT&Tag and CUT&RUN.

This tool completely retains the inherent DNA cleavage and ligation functions of transposase, and at the same time, relying on the enhanced antibody binding capacity of Protein G, it can flexibly adapt to antibodies of different host origins and subtypes. Therefore, GeneRulor pG-Transposome provides a more comprehensive and reliable solution for the research on epigenetics, chromatin interactions and transcriptional regulation, and is especially suitable for experimental systems using mouse IgG1 antibodies or requiring cross-species compatibility.

2. Product Features

(1) Broad-spectrum antibody binding: The protein G domain can bind to antibodies of various origins and subtypes;

(2) High binding affinity: It has stronger binding stability to IgG antibodies;

(3) Multifunctional application: Compatible with various epigenetic detection technologies such as CUT&Tag and CUT&RUN;

(4) High specificity: Provides nanoscale resolution analysis of chromatin modifications and protein binding sites;

(5) Low sample requirement: Capable of processing micro-samples with as few as 500 cells.

3. Application

Enhanced CUT&Tag technology: With its excellent antibody affinity, pG-Transposome achieves ultra-precise labeling of regions of interest and efficient library construction. Its working principle is to utilize the strong interaction between protein G and the Fc segment of IgG antibody to guide transposase to the target sites more firmly, realizing highly specific DNA fragmentation and adapter ligation. This technology is particularly suitable for studying extremely low-abundance transcription factor binding sites and rare histone modifications, and can obtain high-quality data with lower cell input, enabling single-cell level epigenomic analysis.

Figure 1. Experimental flow chart of CUT&Tag using pG-Transposase

References

[1] Dancette OP, Taboureau JL, Tournier E, Charcosset C, Blond P. Purification of immunoglobulins G by protein A/G affinity membrane chromatography. J Chromatogr B Biomed Sci Appl. 1999 Feb 19;723(1-2):61-8. doi: 10.1016/s0378-4347(98)00470-8.

[2] Kaya-Okur HS, Wu SJ, Codomo CA, Pledger ES, Bryson TD, Henikoff JG, Ahmad K, Henikoff S. CUT&Tag for efficient epigenomic profiling of small samples and single cells. Nat Commun. 2019 Apr 29;10(1):1930. doi: 10.1038/s41467-019-09982-5.