Dynein Intermediate Chain 1, Axonemal (DNAI1) Antibody

Product specifications

Primary Antibodies

Dynein Intermediate Chain 1, Axonemal (DNAI1)

Rabbit

Human, Mouse, Rat

Optimal dilutions/concentrations should be determined by the end user.

Polyclonal

Unconjugated

IgG

Antigen Affinity Chromatography.

100 µl

Liquid

ELISA, WB

PBS, pH 7.3, containing 0.02% Sodium Azide and 50% Glycerol.

Shipped within 5-10 working days.

Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles.

No

Q9UI46

27019

NP_001268357.1, NM_001281428.1, NP_036276.1, NM_012144.3

244400

PCD,DIC1,ICS1,oda6,CILD1,Axonemal dynein intermediate chain 1

Antibody anti-DNAI1

RUO

Descripción

Dynein axonemal intermediate chain 1 (DNAI1) is an essential structural component of the outer dynein arms, which are critical for motility in ciliary and flagellar structures. Mutations in DNAI1 have been strongly linked to primary ciliary dyskinesia (PCD), a disorder characterized by defects in mucociliary clearance, leading to chronic respiratory tract infections, situs inversus, and male infertility. DNAI1 is involved in the regulation of microtubule sliding, a process necessary for the generation of bending motions in cilia. Studies reveal that DNAI1 contains multiple domains responsible for protein-protein interactions, facilitating its integration with other dynein complex components like DNAH5 and DNAH9. It is expressed primarily in ciliated epithelial tissues such as the respiratory epithelium, oviducts, and brain ependyma. Functional analyses indicate that DNAI1 mutations often result in the absence or dysfunction of dynein arms in motile cilia. Structural disruptions in DNAI1 can compromise the attachment of the dynein arm to the A-tubule, impairing the dynein-tubulin interactions essential for efficient motility. Additionally, DNAI1 plays a role in maintaining the assembly of other accessory structures, stabilizing the axonemal dynein complex. Animal models with defective DNAI1 often recapitulate clinical symptoms of PCD, including hydrocephalus and respiratory infections. Its expression is tightly regulated during ciliogenesis, often synchronized with dynein heavy chain proteins. DNAI1 stability also depends on cytoplasmic preassembly, a chaperone-mediated process that is critical before its integration into the axoneme. DNAI1 has been a focus of genetic studies, particularly in identifying variants associated with ciliary ultrastructural abnormalities. Emerging research suggests that targeting DNAI1-related pathways could have therapeutic implications for correcting ciliary dysfunction in related diseases.

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