Activin Receptor Type IA (ACVR1) Antibody (N-term) Blocking peptide
€293.00
In stock
SKU
AC-BP7101b
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.
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:
The synthetic peptide sequence used to generate the antibody AP7101b was selected from the N-term region of human ACVR1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Type: Synthetic peptide
Primary Accession: Q04771
Gene ID: 90
Gene Name: ACVR1
Format: The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.
Bio 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).
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.
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:
The synthetic peptide sequence used to generate the antibody AP7101b was selected from the N-term region of human ACVR1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Type: Synthetic peptide
Primary Accession: Q04771
Gene ID: 90
Gene Name: ACVR1
Format: The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.
Bio 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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