Activin Receptor Type-2B; Activin Receptor Type IIB; ACTR-IIB; ACVR2B

For Research Use Only. Not for use in diagnostic procedures.

Human Cells

>95% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 mum filtered solution of 20mM PB, 150mM NaCl, pH 7.4.

Lyophilized protein should be stored at < -20 degree C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7 degree C for 2-7 days. Aliquots of reconstituted samples are stable at < -20 degree C for 3 months.

Manufactured in an ISO 9001:2015 Certified Laboratory.

Small volumes of ACVR2B recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Activin proteins that belong to the transforming growth factor-beta (TGF-beta) superfamily, exert their biological actions by binding to heteromeric receptor complexes of type I and type II serine/threonine kinase receptors. On ligand binding, type I and II receptors form a stable complex, resulting in phosphorylation of type I receptors by type II receptors with constitutive kinase activity, and subsequently initiates the activation of downstream molecules including the endogenous Smads. ActRIIB, also known as ActRIIB, is a type II receptor containing an extracellular domain (ECD), a transmembrane segment, and a cytoplasmic region that includes the kinase domain. ActRIIB is a receptor for activin A, activin B and inhibin A. Multiple ActRIIB isoforms can also be generated, which bind activin isoforms with different affinities.

Molecular Mass: 14.4 kDa
Actual Protein Molecular Mass: 33 kDa

activin A receptor type 2B

activin receptor type-2B

Activin receptor type-2B

ACTR-IIB??[Similar Products]

Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I (I and IB) and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding extracellular domain with cysteine-rich region, a transmembrane domain, and a cytoplasmic domain with predicted serine/threonine specificity. Type I receptors are essential for signaling; and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a stable complex after ligand binding, resulting in phosphorylation of type I receptors by type II receptors. Type II receptors are considered to be constitutively active kinases. This gene encodes activin A type IIB receptor, which displays a 3- to 4-fold higher affinity for the ligand than activin A type II receptor. [provided by RefSeq, Jul 2008]

Transmembrane serine/threonine kinase activin type-2 receptor forming an activin receptor complex with activin type-1 serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, the type-2 receptors act as a primary activin receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin-A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor.

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