Anti-Human Activin RIA (Clone 71412)

Sf 21-Derived Recombinant Human Activin Receptor IA Extracellular Domain (Accession # Q04771)

This monoclonal antibody has been 0.2 µm filtered and lyophilized from modified Dulbecco's phosphate buffered saline (1X PBS) pH 7.2 - 7.3 containing 5.0% w/v trehalose with no calcium, magnesium or preservatives present.

The lyophilized antibody can be stored desiccated at -20°C to -70°C for up to twelve months. The reconstituted antibody can be stored for at least four weeks at 2-8°C. For long-term storage of the reconstituted antibody, aseptically aliquot into working volumes and store at -20°C to -70°C in a manual defrost freezer. Avoid repeated freeze thaw cycles. No detectable loss of activity was observed after six months.

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mmunocytochemistry: Suitable for use at concentration of 8-25 µg/mL.

Mouse Anti-Human Activin Receptor IA (Activin RIA) (Clone 71412) recognizes an epitope on Human Activin RIA. This monoclonal antibody was purified using multi-step affinity chromatography methods such as Protein A or G depending on the species and isotype.

The Activin type I receptors transduce signals for a variety of members of the Transforming growth factor beta superfamily of ligands. This family of cytokines and hormones include activin, Anti-müllerian hormone (AMH), bone morphogenetic proteins (BMPs), and Nodal. They are involved in a host of physiological processes including, growth, cell differentiation, homeostasis, osteogenesis, apoptosis and many other functions. There are three type I Activin receptors: ACVR1, ACVR1B, and ACVR1C. Each bind to a specific type II receptor-ligand complex. Despite the large amount of processes that these ligands regulate, they all operate through essentially the same pathway: A ligand binds to a Type two receptor, which recruits and trans-phosphorylate a type I receptor. The type I receptor recruits a receptor regulated SMAD (R-SMAD) which it phosphorylates. The RSMAD then translocates to the nucleus where it functions as a transcription factor.

Activin isoforms and other members of the TGF-β superfamily exert their biological effects by binding to heteromeric complexes of a type I and a type II serine-threonine kinase receptor, both of which are essential for signal transduction. To date, seven type I and five type II receptors, including the two type I and the two type II activin receptors, designated ActR-I(A), ActR-IB, ActR-II(A) and ActR-IIB, have been cloned from mammals. Through alternative mRNA splicing, multiple ActR-IIB isoforms can also be generated, adding to the complexity of the activin receptor system. Different activin isoforms bind with different high-affinities to the various type II isoforms. Type I activin receptors do not bind directly to activin but will associate with the type II receptor-activin complex and initiate signal transduction. Besides the activin isoforms, ActR-II will also bind inhibin, BMP-2 and BMP-7 with lower affinities. ActR-I can also bind and form signaling complexes with the BMP-2/7-bound BMPR-II. Activin type I receptors are highly conserved. Human, mouse and bovine type IA activin receptors share greater than 98% amino acid sequence homology. Recombinant soluble activin type I receptor does not bind activin.