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AB233987

Anti-Caldesmon/CDM antibody [h-CALD]

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(1 Publication)

Mouse Monoclonal Caldesmon/CDM antibody. Suitable for IHC-P and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Tissue preparation containing CALD1 protein.

View Alternative Names

CAD, CDM, CALD1, Caldesmon

1 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Caldesmon/CDM antibody [h-CALD] (AB233987)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Caldesmon/CDM antibody [h-CALD] (AB233987)

Formalin-fixed, paraffin-embedded Human uterus tissue stained for Caldesmon/CDM using ab233987 at 0.5 μg/ml in immunohistochemical analysis.

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

h-CALD

Isotype

IgG1

Light chain type

kappa

Carrier free

No

Reacts with

Human

Applications

IHC-P

applications

Immunogen

Tissue preparation containing CALD1 protein. The exact immunogen used to generate this antibody is proprietary information.

Q05682

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "IHCP" : {"fullname" : "Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections)", "shortname":"IHC-P"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "IHCP-species-checked": "testedAndGuaranteed", "IHCP-species-dilution-info": "0.25-0.5 µg/mL", "IHCP-species-notes": "<p>Primary incubation for 30 minutes at room temperature.</p> Perform heat-mediated antigen retrieval with Tris/EDTA buffer pH 9.0 before commencing with IHC staining protocol." } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A/G
Purification notes
Purified from Bioreactor Concentrate by Protein A/G.
Storage buffer
pH: 7.2 - 7.4 Preservative: 0.05% Sodium azide Constituents: PBS, 0.05% BSA
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

Publications (1)

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

Oncology letters 23:9 PubMed34820008

2021

Role of Lamin A and emerin in maintaining nuclear morphology in different subtypes of ovarian epithelial cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Shiori Watabe,Sayaka Kobayashi,Mizuho Hatori,Yoshimi Nishijima,Naoki Inoue,Hayato Ikota,Akira Iwase,Hideaki Yokoo,Masanao Saio
View all publications

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