Pierce™ DSG, No-Weigh™ Format
Pierce™ DSG, No-Weigh™ Format
Thermo Scientific™

Pierce™ DSG, No-Weigh™ Format

Thermo Scientific Pierce DSG is a water-insoluble, homo-bifunctional N-hydroxysuccinimide ester (NHS-ester) crosslinker often used for conjugating radiolabeled ligands to cell-surfaceRead more
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Catalog NumberQuantity
2059350 mg
A3539210 x 1 mg
Catalog number 20593
Price (EUR)
161,00
Each
Add to cart
Quantity:
50 mg
Request bulk or custom format
Price (EUR)
161,00
Each
Add to cart
Thermo Scientific Pierce DSG is a water-insoluble, homo-bifunctional N-hydroxysuccinimide ester (NHS-ester) crosslinker often used for conjugating radiolabeled ligands to cell-surface receptors. The NHS ester is the simplest and most commonly used reactive group for crosslinking and labeling proteins and peptides. NHS esters react with primary amines on the N-termini of peptides and the  amine of lysine residues, forming a stable, covalent amide bond and releasing the NHS group.

Thermo Scientific No-Weigh products are specialty reagents provided in a pre-aliquoted format. The pre-weighed packaging prevents the loss of reagent reactivity and contamination over time by eliminating the repetitive opening and closing of the vial. The format enables use of a fresh vial of reagent each time, eliminating the hassle of weighing small amounts of reagents and reducing concerns over reagent stability.

Features of disuccinimidyl glutarate:

Reactive groups: NHS ester (both ends)
Reactive towards: amino groups (primary amines)
• Non-cleavable
• Water-insoluble (dissolve first in DMF or DMSO)
• Membrane-permeable, allowing for intracellular crosslinking
• Can increase crosslinking efficiency compared to DSS in some applications

Product References
Crosslinker Application Guide -- search for recent literature references for this product

For Research Use Only. Not for use in diagnostic procedures.
Specifications
Cell PermeabilityYes
FormPowder
Labeling MethodChemical Labeling
Molecular Weight (g/mol)326.26
PEGylatedNo
Product LinePierce
Quantity50 mg
Reactive MoietyNHS Ester
Shipping ConditionAmbient
SolubilityDMF, DMSO
Spacer Arm Length7.7 Å
Water SolubleNo
Chemical ReactivityAmine-Amine
CleavableNo
Crosslinker TypeHomobifunctional
FormatStandard, Single-use
Product TypeCrosslinker
SpacerShort (<10 Å)
Unit SizeEach
Contents & Storage
Upon receipt store desiccated at 4°C.

Frequently asked questions (FAQs)

Can you provide the shelf-life for DSG (disuccinimidyl glutarate)?

DSG (disuccinimidyl glutarate) is covered under our general 1-year warranty and is guaranteed to be fully functional for 12 months from the date of shipment, if stored as recommended. Please see section 8.1 of our Terms & Conditions of Sale (https://www.thermofisher.com/content/dam/LifeTech/Documents/PDFs/Terms-and-Conditions-of-Sale.pdf) for more details.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

How should I dissolve and store DSG, No-Weigh Format?

DSG is an NHS-ester that hydrolyzes easily and is moisture-sensitive. For optimal results, we recommend storing DSG powder desiccated at 4 degrees C. To avoid moisture condensation onto the product, the vial must be equilibrated to room temperature before opening. We recommend resuspending DSG in DMSO, Anhydrous (Cat. No. D12345) right before use and not storing the solution.

Find additional tips, troubleshooting help, and resources within our Protein Assays and Analysis Support Center.

Can NHS-diazirine (Cat. No. 26167) be used for CHIP applications?

NHS-diazirine has not been tested for cross-linking in a ChIP application. EGS (Cat. No. 21565) and DSG (Cat. No. 20593) are not used by themselves in ChIP, but rather in combination with formaldehyde. While formaldehyde is good for crosslinking proteins that are in direct contact with DNA, it cannot trap proteins that may be bound in a complex with other proteins but are not in direct contact. Thus EGS or DSG can cross-link proteins to proteins that are in direct contact with DNA and are crosslinked to it by formaldehyde. See this reference for more information

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

Citations & References (6)

Citations & References
Abstract
The structural basis for the oligomerization of the N-terminal domain of SATB1.
Authors:Wang Z, Yang X, Chu X, Zhang J, Zhou H, Shen Y, Long J
Journal:Nucleic Acids Res
PubMed ID:22241778
Special AT-rich sequence-binding protein 1 (SATB1) is a global chromatin organizer and gene expression regulator essential for T-cell development and breast cancer tumor growth and metastasis. The oligomerization of the N-terminal domain of SATB1 is critical for its biological function. We determined the crystal structure of the N-terminal domain of ... More
Neurotrophin-mediated degradation of histone methyltransferase by S-nitrosylation cascade regulates neuronal differentiation.
Authors:Sen N, Snyder SH
Journal:Proc Natl Acad Sci U S A
PubMed ID:22123949
Epigenetic regulation of histones mediates neurotrophin actions with histone acetylation enhancing cAMP response element-binding (CREB)-associated transcription elicited by brain-derived neurotrophic factor (BDNF) and nerve-growth factor (NGF). Roles for histone methylation in CREB's transcriptional activity have not been well characterized. We show that depletion of the histone methyltransferase suppressor of variegation ... More
Characterizing phospholamban to sarco(endo)plasmic reticulum Ca2+-ATPase 2a (SERCA2a) protein binding interactions in human cardiac sarcoplasmic reticulum vesicles using chemical cross-linking.
Authors:Akin BL, Jones LR
Journal:J Biol Chem
PubMed ID:22247554
Chemical cross-linking was used to study protein binding interactions between native phospholamban (PLB) and SERCA2a in sarcoplasmic reticulum (SR) vesicles prepared from normal and failed human hearts. Lys(27) of PLB was cross-linked to the Ca(2+) pump at the cytoplasmic extension of M4 (at or near Lys(328)) with the homobifunctional cross-linker, ... More
A central role for the T1 domain in voltage-gated potassium channel formation and function.
Authors:Strang C, Cushman SJ, DeRubeis D, Peterson D, Pfaffinger PJ
Journal:J Biol Chem
PubMed ID:11312262
To interpret the recent atomic structures of the Kv (voltage-dependent potassium) channel T1 domain in a functional context, we must understand both how the T1 domain is integrated into the full-length functional channel protein and what functional roles the T1 domain governs. The T1 domain clearly plays a role in ... More
RelA Ser276 phosphorylation-coupled Lys310 acetylation controls transcriptional elongation of inflammatory cytokines in respiratory syncytial virus infection.
Authors:Brasier AR, Tian B, Jamaluddin M, Kalita MK, Garofalo RP, Lu M
Journal:J Virol
PubMed ID:21900162
Respiratory syncytial virus (RSV) is a negative-sense single-stranded RNA virus responsible for lower respiratory tract infections (LRTIs) in humans. In experimental models of RSV LRTI, the actions of the nuclear factor ?B (NF-?B) transcription factor mediate inflammation and pathology. We have shown that RSV replication induces a mitogen-and-stress-related kinase 1 ... More