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Mouse Anti-BMP10 Recombinant Antibody (CBYY-0656) (CBMAB-0659-YY)

This product is mouse antibody that recognizes BMP10. The antibody CBYY-0656 can be used for immunoassay techniques such as: Neut, WB
See all BMP10 antibodies

Summary

Host Animal
Mouse
Specificity
Human, Mouse
Clone
CBYY-0656
Antibody Isotype
IgG2a
Application
N, WB

Basic Information

Immunogen
Chinese hamster ovary cell line CHO-derived recombinant human BMP-10 Asn317-Arg424.
Host Species
Mouse
Specificity
Human, Mouse
Antibody Isotype
IgG2a
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1 µg/ml
Neutralization0.15-0.9 µg/ml

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Lyophilized
Buffer
PBS, Trehalose
Preservative
None
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 35-84

Target

Full Name
Bone Morphogenetic Protein 10
Introduction
This gene encodes a secreted ligand of the TGF-beta (transforming growth factor-beta) superfamily of proteins. Ligands of this family bind various TGF-beta receptors leading to recruitment and activation of SMAD family transcription factors that regulate gene expression. The encoded preproprotein is proteolytically processed to generate the mature protein, which binds to the activin receptor-like kinase 1 (ALK1) and plays important roles in cardiovascular development including cardiomyocyte proliferation and regulation of heart size, closure of the ductus arteriosus, angiogenesis and ventricular trabeculation. [provided by RefSeq, Aug 2016]
Entrez Gene ID
27302
UniProt ID
O95393
Alternative Names
Bovinene Morphogenetic Protein 10; BMP-10;
Function
Required for maintaining the proliferative activity of embryonic cardiomyocytes by preventing premature activation of the negative cell cycle regulator CDKN1C/p57KIP and maintaining the required expression levels of cardiogenic factors such as MEF2C and NKX2-5. Acts as a ligand for ACVRL1/ALK1, BMPR1A/ALK3 and BMPR1B/ALK6, leading to activation of SMAD1, SMAD5 and SMAD8 transcription factors. Inhibits endothelial cell migration and growth. May reduce cell migration and cell matrix adhesion in breast cancer cell lines.
Biological Process
Activin receptor signaling pathway Source: BHF-UCL
Adult heart development Source: BHF-UCL
Atrial cardiac muscle tissue morphogenesis Source: BHF-UCL
BMP signaling pathway Source: BHF-UCL
Cardiac muscle cell proliferation Source: UniProtKB
Cell adhesion Source: UniProtKB-KW
Heart trabecula formation Source: BHF-UCL
Kidney development Source: Ensembl
Negative regulation of cardiac muscle hypertrophy Source: BHF-UCL
Negative regulation of cell growth Source: UniProtKB
Negative regulation of cell migration Source: UniProtKB
Negative regulation of endothelial cell migration Source: BHF-UCL
Pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
Positive regulation of cardiac muscle cell proliferation Source: BHF-UCL
Positive regulation of cardiac muscle hypertrophy Source: BHF-UCL
Positive regulation of cartilage development Source: Ensembl
Positive regulation of cell proliferation involved in heart morphogenesis Source: BHF-UCL
Positive regulation of gene expression Source: Ensembl
Positive regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
Positive regulation of sarcomere organization Source: BHF-UCL
Positive regulation of transcription, DNA-templated Source: BHF-UCL
Regulation of cardiac muscle contraction Source: BHF-UCL
Regulation of cardiac muscle hypertrophy in response to stress Source: BHF-UCL
Sarcomere organization Source: BHF-UCL
SMAD protein signal transduction Source: GO_Central
Ventricular cardiac muscle cell development Source: BHF-UCL
Ventricular cardiac muscle tissue morphogenesis Source: BHF-UCL
Cellular Location
Secreted

Owen, N. E., Nyimanu, D., Kuc, R. E., Upton, P. D., Morrell, N. W., Alexander, G. J., ... & Davenport, A. P. (2021). Plasma levels of apelin are reduced in patients with liver fibrosis and cirrhosis but are not correlated with circulating levels of bone morphogenetic protein 9 and 10. Peptides, 136, 170440.

Hu, Y., Yu, L., Xia, F., Liang, F., Cheng, C., Huang, Y., & Xiao, L. (2021). Expression of bone morphogenetic protein 10 in cases with endometrial carcinoma and its clinical significance. Clinical and Translational Oncology, 1-6.

Hirono, K., Saito, K., Munkhsaikhan, U., Xu, F., Wang, C., Lu, L., ... & Purevjav, E. (2019). Familial left ventricular non-compaction is associated with a rare p. V407I variant in bone morphogenetic protein 10. Circulation Journal, 83(8), 1737-1746.

Jin, Y., Zheng, W., Li, L., Huang, G., Liu, Y., Jiang, H., ... & Tang, C. (2019). Loss of BMP-10 is correlated with poor survival in ovarian cancer. Pathology-Research and Practice, 215(1), 121-126.

Jumabay, M., Zhumabai, J., Mansurov, N., Niklason, K. C., Guihard, P. J., Cubberly, M. R., ... & Boström, K. I. (2018). Combined effects of bone morphogenetic protein 10 and crossveinless‐2 on cardiomyocyte differentiation in mouse adipocyte‐derived stem cells. Journal of cellular physiology, 233(3), 1812-1822.

Tillet, E., Ouarné, M., Desroches-Castan, A., Mallet, C., Subileau, M., Didier, R., ... & Bailly, S. (2018). A heterodimer formed by bone morphogenetic protein 9 (BMP9) and BMP10 provides most BMP biological activity in plasma. Journal of Biological Chemistry, 293(28), 10963-10974.

Mitrofan, C. G., Appleby, S. L., Nash, G. B., Mallat, Z., Chilvers, E. R., Upton, P. D., & Morrell, N. W. (2017). Bone morphogenetic protein 9 (BMP9) and BMP10 enhance tumor necrosis factor-α-induced monocyte recruitment to the vascular endothelium mainly via activin receptor-like kinase 2. Journal of Biological Chemistry, 292(33), 13714-13726.

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For research use only. Not intended for any clinical use.

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