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AB182653

Anti-Caldesmon/CDM (phospho S789) antibody

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(2 Publications)

Rabbit Polyclonal Caldesmon/CDM phospho S789 antibody. Suitable for WB and reacts with Rat samples. Cited in 2 publications. Immunogen corresponding to Synthetic Peptide within Human CALD1 phospho S789 conjugated to Keyhole Limpet Haemocyanin.

View Alternative Names

CAD, CDM, CALD1, Caldesmon

1 Images
Western blot - Anti-Caldesmon/CDM (phospho S789) antibody (AB182653)
  • WB

Supplier Data

Western blot - Anti-Caldesmon/CDM (phospho S789) antibody (AB182653)

All lanes:

Western blot - Anti-Caldesmon/CDM (phospho S789) antibody (ab182653) at 1/500 dilution

Lane 1:

Rat heart tissue extract

Lane 2:

Rat heart tissue extract with antigen-specific peptide

Predicted band size: 93 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Rat

Applications

WB

applications

Immunogen

Synthetic Peptide within Human CALD1 phospho S789 conjugated to Keyhole Limpet Haemocyanin. The exact immunogen used to generate this antibody is proprietary information.

Q05682

Specificity

ab182653 detects endogenous level of Caldesmon only when phosphorylated at Serine 789.

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
ab182653 was purified by affinity-chromatography using epitope-specific phosphopeptide. Non-phospho specific antibodies were removed by chromatography using non-phosphopeptide.
Storage buffer
pH: 7.4 Preservative: 0.02% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.88% Sodium chloride
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
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.

Caldesmon also known as CDM CALD1 and h-caldesmon is a cytoskeletal protein with a molecular mass of approximately 93 to 120 kDa. This protein expresses itself abundantly in smooth muscle tissues yet it can also be found in non-muscle cells like fibroblasts and endothelial cells. Researchers often use specific caldesmon antibodies in immunohistochemistry allowing them to label various cellular components and providing insights into tissue composition. Due to its presence in muscle tissues caldesmon is essential for understanding muscle physiology and pathology.
Biological function summary

Caldesmon interacts with actin and myosin to regulate actomyosin contractility. This protein plays a critical role in controlling the contraction and relaxation processes in smooth muscle cells. Caldesmon forms part of a complex that includes calmodulin and tropomyosin enhancing its ability to stabilize actin filaments. It functions by inhibiting the ATPase activity of myosin therefore influencing cellular motility and shape change mechanisms. Researchers continually study caldesmon to comprehend its interactome and its significance within the larger cellular structure.

Pathways

Caldesmon participates in the regulation of the cytoskeletal dynamics vital for cell motility and structural integrity. In particular it is an important component of the contraction-relaxation cycle pathway in smooth muscle tissues. This protein has connections with pathways involving RhoA-Rho kinase where caldesmon modulates the phosphorylation levels influencing muscle contraction. Additionally proteins like tropomyosin and calmodulin modulate its activity especially under calcium-calmodulin-dependent pathways which further elucidates its regulatory importance.

Caldesmon has associations with conditions like certain types of cancers and cardiovascular diseases. Its expression levels and distribution provide valuable information in identifying smooth muscle tumors and other pathological conditions. In oncology for example h-caldesmon serves as a marker to distinguish leiomyosarcomas from other tumors. Moreover due to its involvement in smooth muscle contractility caldesmon links with proteins such as calmodulin and tropomyosin in diseases where abnormal contraction and cellular motility play significant roles. Understanding these connections is important for developing targeted treatments and improving diagnostic accuracy.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also plays an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity).
See full target information CALD1 phospho S789

Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Translational research : the journal of laboratory and clinical medicine 259:35-45 PubMed37085047

2023

Diabetes mellitus and aortic stenosis head to head: toward personalized medicine in patients with both pathologies.

Applications

Unspecified application

Species

Unspecified reactive species

Nerea Corbacho-Alonso,Tamara Sastre-Oliva,Luis F López-Almodovar,Jorge Solis,Luis R Padial,Teresa Tejerina,Montserrat Carrascal,Laura Mourino-Alvarez,Maria G Barderas

Cytoskeleton (Hoboken, N.J.) 75:201-212 PubMed29466836

2018

TGFβ1-induced expression of caldesmon mediates epithelial-mesenchymal transition.

Applications

Unspecified application

Species

Unspecified reactive species

Sandeep M Nalluri,Joseph W O'Connor,Gage A Virgi,Samantha E Stewart,Dan Ye,Esther W Gomez
View all publications

Product promise

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