Recombinant Human Activin Receptor Type IIB/ACVR2B protein is a Human Fragment protein, in the 19 to 134 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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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.
Activin receptor type-2B, Activin receptor type IIB, ACTR-IIB, ACVR2B
Recombinant Human Activin Receptor Type IIB/ACVR2B protein is a Human Fragment protein, in the 19 to 134 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
pH: 7.4
Constituents: 99% Phosphate Buffer, 0.88% Sodium chloride
Greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE.
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.
Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.
Phosphorylated. Constitutive phosphorylation is in part catalyzed by its own kinase activity.
This product was previously labelled as Activin Receptor Type IIB
Activin receptor type IIB (ACVR2B) also known as activin receptor type 2B or ACTR-IIB is a transmembrane serine/threonine kinase receptor. ACVR2B primarily binds activins though it can also interact with other ligands. This receptor weighs approximately 57 kDa. ACVR2B is widely expressed in various tissues including skeletal muscle heart and nervous tissue. The receptor plays an important role in transmitting signals from extracellular ligands to intracellular pathways influencing development and cellular functions.
Activin receptor type IIB participates in the regulation of muscle growth by controlling the activity of growth inhibitory proteins. The receptor forms complexes with type I receptor kinases initiating signal transduction events. ACVR2B also interfaces with the inhibin α subunit in the context of reproductive biology. Its involvement in these complexes and interactions underlines its significance in modulating physiological processes such as cell proliferation and differentiation.
Activin receptor type IIB plays a significant role in the TGF-beta signaling pathway and the myostatin pathway. These pathways regulate important cellular processes like muscular hypertrophy and tissue homeostasis. In these pathways ACVR2B interacts with proteins such as follistatin and myostatin. Follistatin acts as a binding protein modulating the activity of members in the TGF-beta superfamily including myostatin and activins highlighting ACVR2B's involvement in maintaining cellular equilibrium.
Activin receptor type IIB has links to muscular dystrophy and cancer. In muscular dystrophy the receptor's signaling affects muscle repair and regeneration primarily through its interaction with myostatin a known negative regulator of muscle growth. In cancer aberrant signaling through ACVR2B could contribute to tumor progression by affecting cellular proliferation and differentiation rates. Understanding ACVR2B's involvement in these diseases provides insights into potential therapeutic targets.
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