Activin Receptor Type IA (ACVR1) Antibody (N-term)
Purified Rabbit Polyclonal Antibody (Pab)
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Application ![]()
| IHC-P, WB, E |
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Primary Accession | Q04771 |
Other Accession | Q28041 |
Reactivity | Human, Rat, Mouse |
Predicted | Bovine |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 57153 Da |
Antigen Region | 6-34 aa |
Gene ID | 90 |
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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 6-34 amino acids from the N-terminal region of human Activin Receptor Type IA (ACVR1). |
Dilution | IHC-P~~1:100~500 WB~~1:1000 E~~Use at an assay dependent concentration. |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
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 (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | ACVR1 |
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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 |
For Research Use Only. Not For Use In Diagnostic Procedures.
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
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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