BMH (bismaleimidohexane)
BMH (bismaleimidohexane)
Citations & References (4)
Thermo Scientific™

BMH (bismaleimidohexane)

Thermo Scientific Pierce BMH is a long-arm, maleimide crosslinker for covalent, irreversible conjugation between sulfhydryl groups (e.g., protein or peptideRead more
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Catalog NumberQuantity
2233050 mg
Catalog number 22330
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50 mg
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Thermo Scientific Pierce BMH is a long-arm, maleimide crosslinker for covalent, irreversible conjugation between sulfhydryl groups (e.g., protein or peptide cysteines).

Features of BMH:

• Reactive groups: maleimide (both ends)
• Reactive towards: sulfhydryl groups
• Long (13.0Å), sulfhydryl-to-sulfhydryl crosslinker, composed of maleimide groups and 11-atom spacer arm
• Water-insoluble—dissolve first in DMF or DMSO, then add to aqueous reaction buffers
• Noncleavable

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

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BM(PEG)3 (1,11-bismaleimido-triethyleneglycol)
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Cell PermeabilityYes
DescriptionBMH
FormPowder
Labeling MethodChemical Labeling
Molecular Weight (g/mol)276.29
PEGylatedNo
Product LinePierce
Quantity50 mg
Reactive MoietyMaleimide
Shipping ConditionAmbient
SolubilityDMF, DMSO
Spacer Arm Length13.0 Å
Water SolubleNo
Chemical ReactivitySulfhydryl-Sulfhydryl
CleavableNo
Crosslinker TypeHomobifunctional
FormatStandard
Product TypeCrosslinker
SpacerMedium (10 to 30 Å)
Unit SizeEach
Contents & Storage
Upon receipt store at 4°C.

Frequently asked questions (FAQs)

Can you provide the shelf-life for BMH (bismaleimidohexane)?

BMH (bismaleimidohexane) 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.

Citations & References (4)

Citations & References
Abstract
Membrane curvature induced by Arf1-GTP is essential for vesicle formation.
Authors:Beck R, Sun Z, Adolf F, Rutz C, Bassler J, Wild K, Sinning I, Hurt E, Brügger B, Béthune J, Wieland F
Journal:Proc Natl Acad Sci U S A
PubMed ID:18689681
'The GTPase Arf1 is considered as a molecular switch that regulates binding and release of coat proteins that polymerize on membranes to form transport vesicles. Here, we show that Arf1-GTP induces positive membrane curvature and find that the small GTPase can dimerize dependent on GTP. Investigating a possible link between ... More
The MUC1-C oncoprotein binds to the BH3 domain of the pro-apoptotic BAX protein and blocks BAX function.
Authors:Ahmad R, Alam M, Rajabi H, Kufe D
Journal:J Biol Chem
PubMed ID:22544745
'The pro-apoptotic BAX protein contains a BH3 domain that is necessary for its dimerization and for activation of the intrinsic apoptotic pathway. The MUC1 (mucin 1) heterodimeric protein is overexpressed in diverse human carcinomas and blocks apoptosis in the response to stress. In this study, we demonstrate that the oncogenic ... More
Two translocating hydrophilic segments of a nascent chain span the ER membrane during multispanning protein topogenesis.
Authors:Kida Y, Morimoto F, Sakaguchi M
Journal:J Cell Biol
PubMed ID:18166653
During protein integration into the endoplasmic reticulum, the N-terminal domain preceding the type I signal-anchor sequence is translocated through a translocon. By fusing a streptavidin-binding peptide tag to the N terminus, we created integration intermediates of multispanning membrane proteins. In a cell-free system, N-terminal domain (N-domain) translocation was arrested by ... More
Resveratrol induces p53-independent, X-linked inhibitor of apoptosis protein (XIAP)-mediated Bax protein oligomerization on mitochondria to initiate cytochrome c release and caspase activation.
Authors:Gogada R, Prabhu V, Amadori M, Scott R, Hashmi S, Chandra D
Journal:J Biol Chem
PubMed ID:21712378
Resveratrol, a naturally occurring phytoalexin, is known to induce apoptosis in multiple cancer cell types, but the underlying molecular mechanisms remain unclear. Here, we show that resveratrol induced p53-independent, X-linked inhibitor of apoptosis protein (XIAP)-mediated translocation of Bax to mitochondria where it underwent oligomerization to initiate apoptosis. Resveratrol treatment promoted ... More