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Activin Receptor Type IA (ACVR1) Antibody (Center N99)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS: 1
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | Q04771 |
| Other Accession | P37172, Q28041 |
| Reactivity | Human, Mouse |
| Predicted | Bovine |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 57153 Da |
| Antigen Region | 85-123 aa |
| Gene ID | 90 |
|---|---|
| Other Names | Activin receptor type-1, Activin receptor type I, ACTR-I, Activin receptor-like kinase 2, ALK-2, Serine/threonine-protein kinase receptor R1, SKR1, TGF-B superfamily receptor type I, TSR-I, ACVR1, ACVRLK2 |
| Target/Specificity | This Activin Receptor Type IA (ACVR1) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 85-123 amino acids from the Central region of human Activin Receptor Type IA (ACVR1). |
| Dilution | WB~~1:1000 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Activin Receptor Type IA (ACVR1) Antibody (Center N99) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | ACVR1 |
|---|---|
| Synonyms | ACVRLK2 |
| Function | Bone morphogenetic protein (BMP) type I receptor that is involved in a wide variety of biological processes, including bone, heart, cartilage, nervous, and reproductive system development and regulation (PubMed:20628059, PubMed:22977237). As a type I receptor, forms heterotetrameric receptor complexes with the type II receptors AMHR2, ACVR2A or ACVR2B (PubMed:17911401). Upon binding of ligands such as BMP7 or GDF2/BMP9 to the heteromeric complexes, type II receptors transphosphorylate ACVR1 intracellular domain (PubMed:25354296). In turn, ACVR1 kinase domain is activated and subsequently phosphorylates SMAD1/5/8 proteins that transduce the signal (PubMed:9748228). In addition to its role in mediating BMP pathway-specific signaling, suppresses TGFbeta/activin pathway signaling by interfering with the binding of activin to its type II receptor (PubMed:17911401). Besides canonical SMAD signaling, can activate non-canonical pathways such as p38 mitogen-activated protein kinases/MAPKs (By similarity). May promote the expression of HAMP, potentially via its interaction with BMP6 (By similarity). |
| Cellular Location | Membrane; Single-pass type I membrane protein. |
| Tissue Location | Expressed in normal parenchymal cells, endothelial cells, fibroblasts and tumor-derived epithelial cells |
Provided below are standard protocols that you may find useful for product applications.
Background
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. ACVR1 is an activin A type I receptor which signals a particular transcriptional response in concert with activin type II receptors.
References
Kan, L. et al. Stem Cells. January; 27(1): 150?56(2009).
Casagrandi, D., et al., Mol. Hum. Reprod. 9(4):199-203 (2003).
Welt, C.K., Curr Opin Obstet Gynecol 14(3):317-323 (2002).
Schneider-Kolsky, M.E., et al., Placenta 23(4):294-302 (2002).
Chapman, S.C., et al., Mol. Endocrinol. 15(4):668-679 (2001).
Schulte, K.M., et al., Horm. Metab. Res. 32(10):390-400 (2000).
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