EZ-Link™ Maleimide Activated Horseradish Peroxidase
EZ-Link™ Maleimide Activated Horseradish Peroxidase
Thermo Scientific™

EZ-Link™ Maleimide Activated Horseradish Peroxidase

Thermo Scientific Pierce Maleimide Activated Horseradish Peroxidase is for preparation of HRP conjugates with proteins, peptides or other ligands thatRead more
Have Questions?
Catalog NumberQuantity
314855 mg
Catalog number 31485
Price (CLP)
-
Quantity:
5 mg
Request bulk or custom format
Thermo Scientific Pierce Maleimide Activated Horseradish Peroxidase is for preparation of HRP conjugates with proteins, peptides or other ligands that contain sulfhydryl groups, such as reduced cysteines. This product contains 5 mg of conjugated protein and can effectively modify 5 mg of immunoglobulin.

Features of Maleimide Activated Horseradish Peroxidase:

Activated HRP – horseradish peroxidase (HRP) modified with maleimide groups for conjugation to sulfhydryl molecules
Sulfhydryl-reactivemaleimide groups conjugate to reduced thiols (-SH), as in the side-chain of cysteine residues
High activity HRP – enzyme activity is greater than 240 units/mg; lyophilized, activated enzyme is stable for at least 12 months at 4°C
Complete kit – includes the activated HRP as well as two types of reagents for sulfhydryl-ready antibodies (IgG) or proteins for conjugation

This product consists of horseradish peroxidase (HRP) that has been modified with Sulfo-SMCC (Part No. 22322) to attach several maleimide groups per HRP molecule while retaining the peroxidase activity. The activated HRP will covalently attach to proteins or other molecule containing sulfhydryl groups (e.g., cysteines). HRP-conjugates of antibodies, proteins, peptides and other thiol-containing reporter probes are easily made using this method. The complete kit includes the activated HRP as well as two types of reagents for preparing sulfhydryl-ready antibodies (IgG) or proteins for conjugation.

The complete kit for Maleimide Activated Horseradish Peroxidase contains reagents for exposing or added the necessary sulfhydryl groups on antibodies (IgG) or practically any other protein. These general strategies are described briefly in the applications section of our review of Maleimide Reaction Chemistry. Of course, any protein that contains cysteines has sulfhydryl groups (-SH), but they must be reduced (not in the form of disulfide bonds) to be conjugated. Antibodies also contain disulfide bonds that can be targeted as antibody labeling sites; the hinge-region disulfide bonds in IgG can be selectively cleaved with the mild reducing agent 2-Mercaptoethylamine (Part No. 20408), which is included in the complete kit. Alternatively, sulfhydryl groups can be added to proteins (or any amine-containing molecule) using SATA reagent (Part No. 26102), which also is included in the kit.

Related Products
EZ-Link™ Maleimide Activated Horseradish Peroxidase Kit
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Chemical ReactivityThiol
FormulationActivated horseradish peroxidase lyophilized from PBS
Label TypeEnzyme Labeled
Label or DyeHRP (Horseradish Peroxidase)
Quantity5 mg
Reactive MoietyMaleimide
SolubilityWater
FormSolid
Product LineEZ-Link
Unit SizeEach
Contents & Storage
Note: Total weight is ∼25mg as a result of buffer components and salts lyophilized along with the activated protein

Storage: Upon receipt store product at 4°C. Product is shipped at ambient temperature.

Citations & References (8)

Citations & References
Abstract
Probing conformational dynamics of an enzymatic active site by an in situ single fluorogenic probe under piconewton force manipulation.
Authors:Pal N, Wu M, Lu HP
Journal:Proc Natl Acad Sci U S A
PubMed ID:27940917
'Unraveling the conformational details of an enzyme during the essential steps of a catalytic reaction (i.e., enzyme-substrate interaction, enzyme-substrate active complex formation, nascent product formation, and product release) is challenging due to the transient nature of intermediate conformational states, conformational fluctuations, and the associated complex dynamics. Here we report our ... More
Arterial smooth muscle cell PKD2 (TRPP1) channels regulate systemic blood pressure.
Authors:Bulley S, Fernández-Peña C, Hasan R, Leo MD, Muralidharan P, Mackay CE, Evanson KW, Moreira-Junior L, Mata-Daboin A, Burris SK, Wang Q, Kuruvilla KP, Jaggar JH
Journal:Elife
PubMed ID:30511640
'Systemic blood pressure is determined, in part, by arterial smooth muscle cells (myocytes). Several Transient Receptor Potential (TRP) channels are proposed to be expressed in arterial myocytes, but it is unclear if these proteins control physiological blood pressure and contribute to hypertension in vivo. We generated the first inducible, smooth ... More
Endothelin-1 Stimulates Vasoconstriction Through Rab11A Serine 177 Phosphorylation.
Authors:Zhai X, Leo MD, Jaggar JH
Journal:Circ Res
PubMed ID:28696251
Large-conductance calcium-activated potassium channels (BK) are composed of pore-forming BKa and auxiliary ß1 subunits in arterial smooth muscle cells (myocytes). Vasoconstrictors, including endothelin-1 (ET-1), inhibit myocyte BK channels, leading to contraction, but mechanisms involved are unclear. Recent evidence indicates that BKa is primarily plasma membrane localized, whereas the cellular location ... More
Impaired Trafficking of ß1 Subunits Inhibits BK Channels in Cerebral Arteries of Hypertensive Rats.
Authors:Leo MD, Zhai X, Yin W, Jaggar JH
Journal:Hypertension
PubMed ID:30012867
Hypertension is a risk factor for cerebrovascular diseases, including stroke and dementia. During hypertension, arteries become constricted and are less responsive to vasodilators, including nitric oxide (NO). The regulation of arterial contractility by smooth muscle cell (myocyte) large-conductance calcium (Ca ... More
Ca
Authors:Chowdhury D, Turner M, Patriarchi T, Hergarden AC, Anderson D, Zhang Y, Sun J, Chen CY, Ames JB, Hell JW
Journal:EMBO J
PubMed ID:29118000
Postsynaptic density protein-95 (PSD-95) localizes AMPA-type glutamate receptors (AMPARs) to postsynaptic sites of glutamatergic synapses. Its postsynaptic displacement is necessary for loss of AMPARs during homeostatic scaling down of synapses. Here, we demonstrate that upon Ca ... More