BMPR-IA/ALK-3 Antibody [Unconjugated]

HAF017). A specific band was detected for BMPR-IA/ALK-3 at approximately 60 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." > HAF017). A specific band was detected for BMPR-IA/ALK-3 at approximately 60 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." title="Western blot shows lysates of human skeletal muscle tissue. PVDF membrane was probed with 2 µg/mL of Goat Anti-Human BMPR-IA/ALK-3 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF346) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (HAF017). A specific band was detected for BMPR-IA/ALK-3 at approximately 60 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." />

Western blot shows lysates of human skeletal muscle tissue. PVDF membrane was probed with 2 µg/mL of Goat Anti-Human BMPR-IA/ALK-3 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF346) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (<a class=

VC006). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to epithelial cells and stroma. Staining was performed using our IHC Staining with VisUCyte HRP Polymer Detection Reagents." > VC006). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to epithelial cells and stroma. Staining was performed using our IHC Staining with VisUCyte HRP Polymer Detection Reagents." title="BMPR‑IA/ALK‑3 was detected in immersion fixed paraffin-embedded sections of normal human prostate tissue (negative) and human prostate cancer tissue (positive) using Goat Anti-Human BMPR‑IA/ALK‑3 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF346) at 1 µg/mL for 1 hour at room temperature followed by incubation with the Anti-Sheep IgG VisUCyte™ HRP Polymer Antibody (VC006). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to epithelial cells and stroma. Staining was performed using our IHC Staining with VisUCyte HRP Polymer Detection Reagents." />

BMPR‑IA/ALK‑3 was detected in immersion fixed paraffin-embedded sections of normal human prostate tissue (negative) and human prostate cancer tissue (positive) using Goat Anti-Human BMPR‑IA/ALK‑3 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF346) at 1 µg/mL for 1 hour at room temperature followed by incubation with the Anti-Sheep IgG VisUCyte™ HRP Polymer Antibody (<a class=

cP1P-augmented cardiac differentiation in hESCs is dependent on BMP receptor-mediated SMAD1/5/8 signaling. (A) The activity of BMPR/SMAD signaling with or without cP1P treatment was evaluated by the expression levels of ALK2 and ALK3 by Western blot at the indicated time points along with GAPDH expression as the loading control. (B) Schematic representation of the treatment with BMPR inhibitor LDN during days 3 to 5 of CM differentiation coinciding with IWR1 inhibitor treatment. (C) The activity of BMPR/SMAD signaling was inhibited by the administration of LDN, as shown by the downregulation of ALK3 and p-SMAD 1/5/8, while cP1P treatment could not reverse the inhibitory effect of LDN. The effects of BMPR inhibition by LDN on cardiomyocyte differentiation, shown by (D) the downregulation of NKX2.5 at day 5. (E) Treatment of LDN between day 3 to 5 also downregulated the expression of TNNT2 and MLC2V at day 8 of CM differentiation even upon cP1P treatment, as demonstrated by Western blot. (F) Schematic representation of the treatment with LDN during days 5 to 8 of CM differentiation. (G) Immunoblots of ALK3, p-SMAD1/5/8, SMAD1/5/8, and NKX2.5 at day 5 of LDN treatment in DMSO-treated controls and cP1P-treated CMs. (H) Immunoblots of TNNT2 and MLC2V at day 8 of LDN treatment in DMSO-treated controls and cP1P-treated CMs. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/34209900), licensed under a CC-BY license. Not internally tested by R&D Systems.

cP1P-augmented cardiac differentiation in hESCs is dependent on BMP receptor-mediated SMAD1/5/8 signaling. (A) The activity of BMPR/SMAD signaling with or without cP1P treatment was evaluated by the expression levels of ALK2 and ALK3 by Western blot at the indicated time points along with GAPDH expression as the loading control. (B) Schematic representation of the treatment with BMPR inhibitor LDN during days 3 to 5 of CM differentiation coinciding with IWR1 inhibitor treatment. (C) The activity of BMPR/SMAD signaling was inhibited by the administration of LDN, as shown by the downregulation of ALK3 and p-SMAD 1/5/8, while cP1P treatment could not reverse the inhibitory effect of LDN. The effects of BMPR inhibition by LDN on cardiomyocyte differentiation, shown by (D) the downregulation of NKX2.5 at day 5. (E) Treatment of LDN between day 3 to 5 also downregulated the expression of TNNT2 and MLC2V at day 8 of CM differentiation even upon cP1P treatment, as demonstrated by Western blot. (F) Schematic representation of the treatment with LDN during days 5 to 8 of CM differentiation. (G) Immunoblots of ALK3, p-SMAD1/5/8, SMAD1/5/8, and NKX2.5 at day 5 of LDN treatment in DMSO-treated controls and cP1P-treated CMs. (H) Immunoblots of TNNT2 and MLC2V at day 8 of LDN treatment in DMSO-treated controls and cP1P-treated CMs. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/34209900), licensed under a CC-BY license. Not internally tested by R&D Systems.

cP1P-augmented cardiac differentiation in hESCs is dependent on BMP receptor-mediated SMAD1/5/8 signaling. (A) The activity of BMPR/SMAD signaling with or without cP1P treatment was evaluated by the expression levels of ALK2 and ALK3 by Western blot at the indicated time points along with GAPDH expression as the loading control. (B) Schematic representation of the treatment with BMPR inhibitor LDN during days 3 to 5 of CM differentiation coinciding with IWR1 inhibitor treatment. (C) The activity of BMPR/SMAD signaling was inhibited by the administration of LDN, as shown by the downregulation of ALK3 and p-SMAD 1/5/8, while cP1P treatment could not reverse the inhibitory effect of LDN. The effects of BMPR inhibition by LDN on cardiomyocyte differentiation, shown by (D) the downregulation of NKX2.5 at day 5. (E) Treatment of LDN between day 3 to 5 also downregulated the expression of TNNT2 and MLC2V at day 8 of CM differentiation even upon cP1P treatment, as demonstrated by Western blot. (F) Schematic representation of the treatment with LDN during days 5 to 8 of CM differentiation. (G) Immunoblots of ALK3, p-SMAD1/5/8, SMAD1/5/8, and NKX2.5 at day 5 of LDN treatment in DMSO-treated controls and cP1P-treated CMs. (H) Immunoblots of TNNT2 and MLC2V at day 8 of LDN treatment in DMSO-treated controls and cP1P-treated CMs. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/34209900), licensed under a CC-BY license. Not internally tested by R&D Systems.

653-E3) was serially diluted and captured by Mouse Anti-Human CCL26/Eotaxin‑3 Monoclonal Antibody (Catalog # MAB653) coated on a Clear Polystyrene Microplate (Catalog # DY990). Goat Anti-Human BMPR‑IA/ALK‑3 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF346) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998)" > 653-E3) was serially diluted and captured by Mouse Anti-Human CCL26/Eotaxin‑3 Monoclonal Antibody (Catalog # MAB653) coated on a Clear Polystyrene Microplate (Catalog # DY990). Goat Anti-Human BMPR‑IA/ALK‑3 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF346) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998)" title="Recombinant Human CCL26/Eotaxin‑3 (Catalog # 653-E3) was serially diluted and captured by Mouse Anti-Human CCL26/Eotaxin‑3 Monoclonal Antibody (Catalog # MAB653) coated on a Clear Polystyrene Microplate (Catalog # DY990). Goat Anti-Human BMPR‑IA/ALK‑3 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF346) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998)" />

Recombinant Human CCL26/Eotaxin‑3 (Catalog # <a class=

• Reactivity: Hu
• Applications: WB, IHC
• Clonality: Polyclonal
• Host: Goat
• Conjugate: Unconjugated
• Concentration: LYOPH

BMPR-IA/ALK-3 Antibody [Unconjugated] Summary

• Immunogen: Mouse myeloma cell line NS0-derived recombinant human BMPR-IA/AKL-3
  Gln24-Arg152
  Accession # P36894
• Specificity: Detects human BMPR-IA in direct ELISAs and Western blots.
• Source: N/A
• Isotype: IgG
• Clonality: Polyclonal
• Host: Goat
• Gene: BMPR1A
• Purity Statement: Antigen Affinity-purified

Applications/Dilutions

• Dilutions:
  • Immunohistochemistry 1-15 ug/mL
  • Western Blot 2 ug/mL

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. See Certificate of Analysis for details.
  *Small pack size (-SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
• Preservative: No Preservative
• Concentration: LYOPH
• Reconstitution Instructions: Reconstitute at 0.2 mg/mL in sterile PBS. For liquid material, refer to CoA for concentration.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for BMPR-IA/ALK-3 Antibody [Unconjugated]

• ACVRLK310q23del
• ALK-3
• ALK3EC 2.7.11.30
• BMP type-1A receptor
• BMPR1A
• BMPR-1A
• BMPRIA
• BMPR-IA
• bone morphogenetic protein receptor type-1A
• bone morphogenetic protein receptor, type IA
• CD292 antigen
• CD292
• EC 2.7.11
• Serine/threonine-protein kinase receptor R5
• SKR5
• type II-like kinase 3

Background

Cellular responses to bone morphogenetic proteins (BMPs) have been shown to be mediated by the formation of hetero-oligomeric complexes of the type I and type II serine/threonine kinase receptors. BMP receptor 1A (BMPR-1A), also known as activin receptor-like kinase (ALK)-3, is one of seven known type I serine/threonine kinases that are required for the signal transduction of TGF-beta family cytokines. In contrast to the TGF-beta receptor system in which the type I receptor does not bind TGF-beta  in the absence of the type II receptor, type I receptors involved in BMP signaling (including BMPR-IA, BMPR-IB/ALK-6, and ActR-I/ALK-2) can independently bind the various BMP family proteins in the absence of type II receptors. Recombinant soluble BMPR-IA binds BMP-4 with high-affinity in solution and is a potent BMP-4 antagonist in vitro. BMPR-IA is ubiquitously expressed during embryogenesis. In adult tissues, BMPR-IA mRNA is also widely distributed with the highest expression levels found in skeletal muscle. The extracellular domain of BMPR-IA shares little amino acid sequence identity with the other mammalian ALK type I receptor kinases, but the cysteine residues are conserved. Human and mouse BMPR-IA are highly conserved and share 98% sequence identity.

1. Kawabata, M. et al. (1998) Cytokine and Growth Factor Reviews 9:49.
2. Ebendal, T. et al. (1998) J. Neuroscience Research 51:139.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Publications for BMPR-IA/ALK-3 Antibody (AF346)(13)

Publications using AF346

• Ji-Hye Jang, Min-Seong Kim, Ainsley Mike Antao, Won-Jun Jo, Hyung-Joon Kim, Su-Jin Kim et al. Bioactive Lipid O-cyclic phytosphingosine-1-phosphate Promotes Differentiation of Human Embryonic Stem Cells into Cardiomyocytes via ALK3/BMPR Signaling International Journal of Molecular Sciences 6/29/2021 [PMID: 34209900]
• Maëva Chauvin, Véronique Garambois, Sylvie Choblet, Pierre-Emmanuel Colombo, Myriam Chentouf, Laurent Gros et al. Anti-Müllerian hormone concentration regulates activin receptor-like kinase-2/3 expression levels with opposing effects on ovarian cancer cell survival International Journal of Oncology 5/17/2021 [PMID: 34013359]
• T Voeltzel, M Flores-Vio, F Zylberszte, S Lefort, M Billandon, S Jeanpierre, S Joly, G Fossard, M Milenkov, F Mazurier, A Nehme, A Belhabri, E Paubelle, X Thomas, M Michallet, F Louache, FE Nicolini, C Caron de F, V Maguer-Sat A new signaling cascade linking BMP4, BMPR1A, ?Np73 and NANOG impacts on stem-like human cell properties and patient outcome Cell Death Dis, 2018-09-27;9(10):1011. 2018-09-27 [PMID: 30262802] (Flow Cytometry, Functional Assay, Human)
• P Toofan, C Busch, H Morrison, S O'Brien, H Jørgensen, M Copland, H Wheadon Chronic myeloid leukaemia cells require the bone morphogenic protein pathway for cell cycle progression and self-renewal Cell Death Dis, 2018-09-11;9(9):927. 2018-09-11 [PMID: 30206237] (Flow Cytometry, Human)
• Martinez V, Sacedon R, Hidalgo L, Valencia J, Fernandez-Sevilla L, Hernandez-Lopez C, Vicente A, Varas A The BMP Pathway Participates in Human Naive CD4+ T Cell Activation and Homeostasis. PLoS ONE, 2015-06-25;10(6):e0131453. 2015-06-25 [PMID: 26110906] (Flow Cytometry, IHC, Human)
• Cao Y, Slaney C, Bidwell B, Parker B, Johnstone C, Rautela J, Eckhardt B, Anderson R BMP4 inhibits breast cancer metastasis by blocking myeloid-derived suppressor cell activity. Cancer Res, 2014-09-15;74(18):5091-102. 2014-09-15 [PMID: 25224959] (Flow Cytometry, Mouse)
• Robson N, Hidalgo L, McAlpine T, Wei H, Martinez V, Entrena A, Melen G, MacDonald A, Phythian-Adams A, Sacedon R, Maraskovsky E, Cebon J, Ramirez M, Vicente A, Varas A Optimal effector functions in human natural killer cells rely upon autocrine bone morphogenetic protein signaling. Cancer Res, 2014-07-18;74(18):5019-31. 2014-07-18 [PMID: 25038228] (Flow Cytometry, Human)
• Fong D, Bisson M, Laberge G, McManus S, Grenier G, Faucheux N, Roux S Bone morphogenetic protein-9 activates Smad and ERK pathways and supports human osteoclast function and survival in vitro. Cell Signal, 2013-01-08;25(4):717-28. 2013-01-08 [PMID: 23313128] (ICC, Western Blot, Human)
• Lee J, Son MJ, Woolard K, Donin NM, Li A, Cheng CH, Kotliarova S, Kotliarov Y, Walling J, Ahn S, Kim M, Totonchy M, Cusack T, Ene C, Ma H, Su Q, Zenklusen JC, Zhang W, Maric D, Fine HA Epigenetic-mediated dysfunction of the bone morphogenetic protein pathway inhibits differentiation of glioblastoma-initiating cells. Cancer Cell, 2008-01-01;13(1):69-80. 2008-01-01 [PMID: 18167341] (Western Blot, Human)
• Zeisberg M, Yang C, Martino M, Duncan MB, Rieder F, Tanjore H, Kalluri R Fibroblasts derive from hepatocytes in liver fibrosis via epithelial to mesenchymal transition. J. Biol. Chem., 2007-06-11;282(32):23337-47. 2007-06-11 [PMID: 17562716] (IHC-P, Mouse)
• Gossrau G, Thiele J, Konang R, Schmandt T, Brustle O Bone morphogenetic protein-mediated modulation of lineage diversification during neural differentiation of embryonic stem cells. Stem Cells, 2007-01-11;25(4):939-49. 2007-01-11 [PMID: 17218404] (Immunoprecipitation, Mouse)
• Lopez-Coviella I, Mellott TM, Kovacheva VP, Berse B, Slack BE, Zemelko V, Schnitzler A, Blusztajn JK Developmental pattern of expression of BMP receptors and Smads and activation of Smad1 and Smad5 by BMP9 in mouse basal forebrain. Brain Res., 2006-04-13;1088(1):49-56. 2006-04-13 [PMID: 16626664] (Immunoprecipitation, Mouse)
• Bleuming SA, Kodach LL, Garcia Leon MJ, Richel DJ, Peppelenbosch MP, Reitsma PH, Hardwick JC, van den Brink GR Altered bone morphogenetic protein signalling in the Helicobacter pylori-infected stomach. J. Pathol., 2006-06-01;209(2):190-7. 2006-06-01 [PMID: 16550632] (IHC-P, Human)

Bioinformatics

• Gene Symbol: BMPR1A
• Uniprot:
  • P36894()