GeneBio Systems
Recombinant Human/Cynomolgus monkey Activin receptor type-2B (ACVR2B), partial (Active)
Recombinant Human/Cynomolgus monkey Activin receptor type-2B (ACVR2B), partial (Active)
SKU:Q13705/A0A2K5WUB0
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Size: 100ug. Other sizes are also available.
Activity: Yes
Research Areas: Signal Transduction
Uniprot ID: Q13705/A0A2K5WUB0
Gene Names: ACVR2B
Alternative Name(s): Activin receptor type-2B; EC: 2.7.11.30; Activin receptor type IIB (ACTR-IIB); ACVR2B
Abbreviation: Recombinant Human/Cynomolgus monkey ACVR2B protein, partial (Active)
Organism: Homo sapiens (Human)
Source: Mammalian cell
Expression Region: 19-137aa
Protein Length: Partial
Tag Info: C-terminal hFc1-Flag-tagged
Target Protein Sequence: SGRGEAETRECIYYNANWELERTNQSGLERCEGEQDKRLHCYASWRNSSGTIELVKKGCWLDDFNCYDRQECVATEENPQVYFCCCEGNFCNERFTHLPEAGGPEVTYEPPPTAPTLLT
MW: 43.6 kDa
Purity: Greater than 95% as determined by SDS-PAGE. Greater than 95% as determined by SEC-HPLC.
Endotoxin: Less than 1.0 EU/μg as determined by LAL method.
Biological_Activity: Measured by its binding ability in a functional ELISA.Immobilized Human INHBA(CSB-MP011719HU1b0) at 2 μg/mL can bind Human ACVR2B.The EC50 is 45.93-52.42 ng/mL.
Form: Lyophilized powder
Buffer: Lyophilized from a 0.2 μm sterile filtered PBS, 6% Trehalose, pH 7.4
Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.
Relevance: 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.
Reference: Type I receptor binding of bone morphogenetic protein 6 is dependent on N- glycosylation of the ligand. Saremba S., Nickel J., Seher A., Kotzsch A., Sebald W., Mueller T.D. FEBS J. 275: 172-183 (2008)
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