Thermo Scientific Pierce DTME is a mid-length, maleimide crosslinker for reversible covalent conjugation between sulfhydryl groups (e.g., protein or peptideRead more
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Catalog Number
Quantity
22335
50 mg
Catalog number 22335
Price (EUR)
400,00
Each
Add to cart
Quantity:
50 mg
Request bulk or custom format
Price (EUR)
400,00
Each
Add to cart
Thermo Scientific Pierce DTME is a mid-length, maleimide crosslinker for reversible covalent conjugation between sulfhydryl groups (e.g., protein or peptide cysteines) by reduction of the disulfide bond in the center of the spacer arm.
Features of DTME:
• Reactive groups:maleimide (both ends) • Reactive towards: sulfhydryl groups • Long (13.3A), cleavable, sulfhydryl-to-sulfhydryl crosslinker, composed of maleimide groups and 11-atom disulfide spacer arm • Water-insoluble—dissolve first in DMF or DMSO, then add to aqueous reaction buffers • Cleavable by reduction of disulfide spacer arm with DTT, TCEP or other reducing agent
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
DescriptionDTME
FormSolid
Labeling MethodChemical Labeling
Molecular Weight (g/mol)312.36
PEGylatedNo
Product LinePierce
Quantity50 mg
Reactive MoietyMaleimide
Shipping ConditionAmbient
SolubilityDMF, DMSO
Spacer Arm Length13.3 Å
Water SolubleNo
Chemical ReactivitySulfhydryl-Sulfhydryl
CleavableBy Thiols
Crosslinker TypeHomobifunctional
FormatStandard
Product TypeCrosslinker
SpacerMedium (10 to 30 Å)
Unit SizeEach
Contents & Storage
Upon receipt store desiccated at 4°C.
Frequently asked questions (FAQs)
Can you provide the shelf-life for DTME (dithiobismaleimidoethane)?
DTME (dithiobismaleimidoethane) 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.
Nedd4-1 and beta-arrestin-1 are key regulators of Na+/H+ exchanger 1 ubiquitylation, endocytosis, and function.
Authors:Simonin A, Fuster D
Journal:J Biol Chem
PubMed ID:20855896
'The ubiquitously expressed mammalian Na(+)/H(+) exchanger 1 (NHE1) controls cell volume and pH but is also critically involved in complex biological processes like cell adhesion, cell migration, cell proliferation, and mechanosensation. Pathways controlling NHE1 turnover at the plasma membrane, however, are currently unclear. Here, we demonstrate that NHE1 undergoes ubiquitylation ... More
The extreme C terminus of the ABC protein DrrA contains unique motifs involved in function and assembly of the DrrAB complex.
Authors:Zhang H, Pradhan P, Kaur P
Journal:J Biol Chem
PubMed ID:20876527
'Two novel regulatory motifs, LDEVFL and C-terminal regulatory Glu (E)-rich motif (CREEM), are identified in the extreme C terminus of the ABC protein DrrA, which is involved in direct interaction with the N-terminal cytoplasmic tail of the membrane protein DrrB and in homodimerization of DrrA. Disulfide cross-linking analysis showed that ... More
Association of Rho-associated protein kinase 1 with E-cadherin complexes is mediated by p120-catenin.
Authors:Smith AL, Dohn MR, Brown MV, Reynolds AB
Journal:Mol Biol Cell
PubMed ID:22031287
The dynamic functional linkage of cadherins with the underlying actin cytoskeleton is tightly regulated to achieve proper cell-cell adhesion. p120-catenin (p120) regulates both cadherin stability and actin dynamics, but the relationship between these two functions remains unclear. Using a novel proteomic approach called reversible cross-link immunoprecipitation, or ReCLIP, we previously ... More
Claudin-2 forms homodimers and is a component of a high molecular weight protein complex.
Authors:Van Itallie CM, Mitic LL, Anderson JM
Journal:J Biol Chem
PubMed ID:21098027
Tight junctions are multiprotein complexes that form the fundamental physiologic and anatomic barrier between epithelial and endothelial cells, yet little information is available about their molecular organization. To begin to understand how the transmembrane proteins of the tight junction are organized into multiprotein complexes, we used blue native-PAGE (BN-PAGE) and ... More
Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis.
Authors:Auclair JR, Boggio KJ, Petsko GA, Ringe D, Agar JN
Journal:Proc Natl Acad Sci U S A
PubMed ID:21098299
Amyotrophic lateral sclerosis (ALS) is a disorder characterized by the death of both upper and lower motor neurons and by 3- to 5-yr median survival postdiagnosis. The only US Food and Drug Administration-approved drug for the treatment of ALS, Riluzole, has at best, moderate effect on patient survival and quality ... More