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Mouse Anti-BMPER Recombinant Antibody (C1097) (CBMAB-C1097-CN)

This product is a Rabbit antibody that recognizes BMPER. The antibody 7H123 can be used for immunoassay techniques such as: ELISA, WB.
See all BMPER antibodies
Published Data
CBMAB-C1097-CN-1
CBMAB-C1097-CN in IHC
Spatial expression of SOX8/ELN (a-f), TBX2/ELN (g-l), BMPER/ELN (m-r), and ACTC1/ELN (s-x) in the alveolar compartment in control and mutant lungs at postnatal day 14 as detected by immunostaining. Scale bar: 25 um for all images. ...View More
Gao, F., Li, C., Smith, S. M., Peinado, N., Kohbodi, G., Tran, E., ... & Minoo, P. (2022). Decoding the IGF1 signaling gene regulatory network behind alveologenesis from a mouse model of bronchopulmonary dysplasia. Elife, 11, e77522.

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
C1097
Antibody Isotype
IgG2a
Application
WB, IP, IF, E

Basic Information

Immunogen
Amino acids 497-685 mapping at the C-terminus of Crossveinless-2 of human origin.
Host Species
Mouse
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG2a
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)1:50-1:500
ELISA1:100-1:1,000

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

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
0.09% sodium azide
Concentration
0.2 mg/ml

Target

Full Name
BMP Binding Endothelial Regulator
Introduction
This gene encodes a secreted protein that interacts with, and inhibits bone morphogenetic protein (BMP) function. It has been shown to inhibit BMP2- and BMP4-dependent osteoblast differentiation and BMP-dependent differentiation of the chondrogenic cells. Mutations in this gene are associated with a lethal skeletal disorder, diaphanospondylodysostosis. [provided by RefSeq, Dec 2011]
Entrez Gene ID
168667
UniProt ID
Q8N8U9
Alternative Names
BMP Binding Endothelial Regulator; Bone Morphogenetic Protein-Binding Endothelial Cell Precursor-Derived Regulator; HCV2; BMP-Binding Endothelial Regulator Precursor Protein; BMP-Binding Endothelial Regulator Protein; Protein Crossveinless-2; Crossveinless-2;
Function
Inhibitor of bone morphogenetic protein (BMP) function, it may regulate BMP responsiveness of osteoblasts and chondrocytes.
Biological Process
Blood vessel development Source: GO_Central
Blood vessel endothelial cell proliferation involved in sprouting angiogenesis Source: BHF-UCL
Endothelial cell activation Source: BHF-UCL
Inner ear development Source: Ensembl
Negative regulation of BMP signaling pathway Source: BHF-UCL
Positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
Positive regulation of sprouting angiogenesis Source: BHF-UCL
Regulation of angiogenesis Source: GO_Central
Regulation of endothelial cell migration Source: BHF-UCL
Regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
Ureteric bud development Source: Ensembl
Cellular Location
Secreted
Involvement in disease
Diaphanospondylodysostosis (DSD): A rare, recessively inherited, perinatal lethal skeletal disorder. The primary skeletal characteristics of the phenotype include a small chest, abnormal vertebral segmentation, and posterior rib gaps containing incompletely differentiated mesenchymal tissue. Consistent craniofacial features include ocular hypertelorism, epicanthal folds, a depressed nasal bridge with a short nose, and low-set ears. The most commonly described extraskeletal finding is nephroblastomatosis with cystic kidneys, but other visceral findings have been described in some cases.

Mao, H., Li, L., Fan, Q., Angelini, A., Saha, P. K., Wu, H., ... & Pi, X. (2021). Loss of bone morphogenetic protein-binding endothelial regulator causes insulin resistance. Nature communications, 12(1), 1-10.

Lockhart-Cairns, M. P., Lim, K. T. W., Zuk, A., Godwin, A. R., Cain, S. A., Sengle, G., & Baldock, C. (2019). Internal cleavage and synergy with twisted gastrulation enhance BMP inhibition by BMPER. Matrix Biology, 77, 73-86.

Osmanagic‐Myers, S., & Rezniczek, G. A. (2018). Arteriovenous specification: BMPER and TWSG 1 determine endothelial cell fate via activation of synergistic BMP and Notch signaling. The FEBS journal, 285(8), 1399-1402.

Xiao, F., Wang, C., Wang, C., Gao, Y., Zhang, X., & Chen, X. (2018). BMPER enhances bone formation by promoting the osteogenesis-angiogenesis coupling process in mesenchymal stem cells. Cellular Physiology and Biochemistry, 45(5), 1927-1939.

Lockyer, P., Mao, H., Fan, Q., Li, L., Yu-Lee, L. Y., Eissa, N. T., ... & Pi, X. (2017). LRP1-dependent BMPER signaling regulates lipopolysaccharide-induced vascular inflammation. Arteriosclerosis, thrombosis, and vascular biology, 37(8), 1524-1535.

Hasebe, T., Tanaka, H., Sawada, K., Nakajima, S., Ohtake, T., Fujiya, M., & Kohgo, Y. (2017). Bone morphogenetic protein-binding endothelial regulator of liver sinusoidal endothelial cells induces iron overload in a fatty liver mouse model. Journal of gastroenterology, 52(3), 341-351.

Helbing, T., Wiltgen, G., Hornstein, A., Brauers, E. Z., Arnold, L., Bauer, A., ... & Moser, M. (2017). Bone morphogenetic protein-modulator BMPER regulates endothelial barrier function. Inflammation, 40(2), 442-453.

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

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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