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Human Polyclonal ACVR2B Primary Antibody for IHC (p), WB - ABIN391162
Harrison, Gray, Fischer, Donaldson, Choe, Vale: An activin mutant with disrupted ALK4 binding blocks signaling via type II receptors. in The Journal of biological chemistry 2004
Show all 5 Pubmed References
ActRIIB mRNA but not protein was decreased in skeletal muscle of obese compared with lean animals.
the A allele of genetic variant rs2276541 in ACVR2B is associated with lean muscle mass
TGF-beta (show TGFB1 Antibodies) receptor mediated telomerase inhibition, telomere shortening and breast cancer cell senescence.(
ActR-IIB is expressed in male germ cells and Sertoli cells.
Activin A (show INHBA Antibodies) inhibited signaling by BMP-6 (show BMP6 Antibodies) and BMP-9 (show GDF2 Antibodies) by competing for type 2 receptors ACVR2A (show ACVR2A Antibodies) and ACVR2B.
We found that the AAAAA, AGGAG, and AGGGA haplotypes in ACVR2B were associated with susceptibility to Premature Ovarian Failure when they also had at least one CATAG haplotype in ADAMTS19.
miR (show MLXIP Antibodies)-21 interacts directly with the 3'-untranslated region of ACVR2B mRNA. Mechanical stretch suppressed ACVR2B protein levels in periodontal ligament stem cells. Gain- and loss of function of ACVR2B mediated the osteogenic differentiation of PDLSCs.
Adenomyotic tissues express high levels of myostatin (show MSTN Antibodies), follistatin (show FST Antibodies), and activin (show Actbeta Antibodies) type II receptors.
Activin type IIB receptors are clearly demonstrable throughout the adult human hypothalamus and basal forebrain.
After eccentric exercise, postmenopausal women not using hormone therapy (HT) expressed lower levels of ActRIIb while postmenopausal women using HT showed a heightened response.
The interaction between all five miRNAs and ACVR2B was verified by an in vitro assay.
Roles in hindbrain and neural crest cell (NCC) patterning, in NCC derived pharyngeal arch cartilage and joint formation, and in tooth development.
Data, including data from studies using transgenic mice, suggest that osteoblasts deficient in Acvr2A (show ACVR2A Antibodies) exhibit un-characteristic features; osteoclasts deficient in Acvr2A (show ACVR2A Antibodies) or Acvr2B or both appear normal. Acvr2A (show ACVR2A Antibodies)-deficient mice exhibit significantly increased femoral trabecular bone volume at 6 weeks of age; Acvr2B-deficient mice exhibit no significant change in any bone parameter.
Differential muscle hypertrophy is associated with satellite cell numbers and Akt (show AKT1 Antibodies) pathway activation following activin type IIB receptor inhibition in Mtm1 (show MTM1 Antibodies)
ActRIIB inhibition enhanced energy expenditure only at ambient temperature or in the cold, where nonshivering thermogenesis is minimal, suggesting that brown fat activation plays a prominent role in the metabolic actions of ActRIIB inhibition.
findings best fit a model in which BMP3 (show BMP3 Antibodies), produced by mature bone cells, acts to reduce BMP signaling through Acvr2b in skeletal progenitor cells, limiting their differentiation to mature osteoblasts
Functional redundancy in osteoblast differentiation is observed between bone morphogenetic protein receptor BMPR-II (show BMPR2 Antibodies) and ActR-IIB.
Inhibition of activin receptor type IIB increases strength and lifespan in myotubularin (show MTM1 Antibodies)-deficient mice.
Akt (show AKT1 Antibodies) isoforms are not essential for for the ability of ActRIIB inhibition to regulate muscle size and function .
ActRIIB plays a role in the specification of left-sidedness in developing mice
Activin (show Actbeta Antibodies) type IIB(ActRIIB) and its subfamily receptor, Activin (show Actbeta Antibodies) type IIA (ActRIIA (show ACVR2A Antibodies)), cooperatively mediate the Gdf11 (show GDF11 Antibodies) signal in patterning the axial vertebrae
ActRIIB is expressed in the early development of thymocytes.
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.
activin A receptor, type IIB
, activin receptor type IIB
, activin receptor type-2B-like
, activin type IIB receptor
, activin receptor type-2B
, testicular activin receptor IIB
, ActRIIB type II activin receptor B
, Activine receptor 2b (transmembrane serine kinase)
, activin receptor IIB