Abcam, ab174640, Anti-heavy chain cardiac Myosin antibody [BA-G5] - BSA and Azide free

Size: 100µg
Mouse Monoclonal MYH6 antibody. Carrier free. Suitable for WB and reacts with Mouse, Rat samples. Cited in 2 publications.
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:BA-G5,
Isotype:IgG2b,
Carrier free:Yes,
Reacts with:Mouse, Rat,
Applications:WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.

Product details:
ab174640 is the carrier-free version of
ab50967
Want a custom formulation?
This antibody clone is manufactured by Abcam. If you require a custom buffer formulation or conjugation for your experiments, please contact orders@abcam.com
Conjugation ready
Our carrier-free antibodies are typically supplied in a PBS-only formulation, purified and free of BSA, sodium azide and glycerol. This conjugation-ready format is designed for use with fluorochromes, metal isotopes, oligonucleotides, and enzymes, which makes them ideal for antibody labelling, functional and cell-based assays, flow-based assays (e.g. mass cytometry) and Multiplex Imaging applications.
Use our
conjugation kits
for antibody conjugates that are ready-to-use in as little as 20 minutes with 1 minute hands-on-time and 100% antibody recovery: available for fluorescent dyes, HRP, biotin and gold.
Compatibility
This product is compatible with the Maxpar
Antibody Labeling Kit from Fluidigm, without the need for antibody preparation. Maxpar
is a trademark of Fluidigm Canada Inc.

Properties and Storage Information:
Form-Liquid, Purity-IgG fraction, Storage buffer-pH: 7.4Constituents: PBS, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Heavy chain cardiac myosin also known as cardiac myosin heavy chain or MYH7 is a critical structural and functional component of cardiac muscle. It plays a significant role in the contractile mechanism of the heart by interacting with actin filaments. The known mass for the heavy chain cardiac myosin is approximately 223 kDa. This protein is mainly expressed in the cardiac muscle tissue where it contributes to the contractile apparatus that enables heart muscle contraction and relaxation essential for pumping blood throughout the body.
Biological function summary
Heavy chain cardiac myosin functions as part of the thick filament within the sarcomere which is the basic contractile unit of muscle cells. It forms a complex with other proteins such as myosin light chains and the protein titin to generate force through ATP hydrolysis. This interaction with actin within the sarcomere underlies muscle contraction with energy provided by ATP. Regulation of contraction and relaxation allows the heart to maintain rhythmic and forceful pumping critical for efficient blood circulation.
Pathways
Heavy chain cardiac myosin plays an integral role in the excitation-contraction coupling pathway. This pathway links the electrical signal of the heartbeat to the mechanical contraction of the heart muscles governed by a sequence of depolarization and subsequent release of calcium ions. Heavy chain cardiac myosin also interacts with related proteins such as tropomyosin and troponin which modulate the exposure of myosin binding sites on actin filaments and thereby regulate heart muscle contraction.
Mutations or abnormalities in the heavy chain cardiac myosin gene have strong associations with hypertrophic cardiomyopathy and dilated cardiomyopathy. These disorders result in changes to the structure and function of the heart potentially leading to heart failure. Heavy chain cardiac myosin mutations can further affect protein interactions like those with the aforementioned troponin complex altering contractility and impacting the heart's ability to pump efficiently. Researchers study these interactions to understand the mechanisms of cardiac diseases and to develop potential therapies.