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Rabbit Anti-EFEMP2 Recombinant Antibody (EPR684) (CBMAB-E0821-FY)

This product is rabbit antibody that recognizes EFEMP2. The antibody EPR684 can be used for immunoassay techniques such as: WB, IHC-P.
See all EFEMP2 antibodies

Summary

Host Animal
Rabbit
Specificity
Human
Clone
EPR684
Antibody Isotype
IgG
Application
WB, IHC-P

Basic Information

Immunogen
A synthetic peptide corresponding to residues in human Fibulin-4 was used as an immunogen
Specificity
Human
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Format
Liquid
Buffer
49% PBS, 50% glycerol, 0.05% BSA
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
EGF-containing fibulin-like extracellular matrix protein 2
Introduction
A large number of extracellular matrix proteins have been found to contain variations of the epidermal growth factor (EGF) domain and have been implicated in functions as diverse as blood coagulation, activation of complement and determination of cell fate during development. The protein encoded by this gene contains four EGF2 domains and six calcium-binding EGF2 domains. This gene is necessary for elastic fiber formation and connective tissue development. Defects in this gene are cause of an autosomal recessive cutis laxa syndrome. Alternatively spliced transcript variants have been identified for this gene.
Entrez Gene ID
30008
UniProt ID
O95967
Alternative Names
EGF Containing Fibulin Extracellular Matrix Protein 2; EGF Containing Fibulin Like Extracellular Matrix Protein 2; EGF-Containing Fibulin-Like Extracellular Matrix Protein 2; Fibulin 4; FIBL-4; FBLN4; Mutant P53 Binding Protein 1
Research Area
Plays a crucial role in elastic fiber formation in tissue, and in the formation of ultrastructural connections between elastic laminae and smooth muscle cells in the aorta, therefore participates in terminal differentiation and maturation of smooth muscle cell (SMC) and in the mechanical properties and wall integrity maintenance of the aorta (PubMed:27339457).

In addition, is involved in the control of collagen fibril assembly in tissue throught proteolytic activation of LOX leading to cross- linking of collagen and elastin (By similarity).

Also promotes ELN coacervation and participates in the deposition of ELN coacervates on to microfibrils but also regulates ELN cross- linking through LOX interaction (PubMed:18973305, PubMed:19570982).

Moreover adheres to the cells through heparin binding in a calcium-dependent manner and regulates vascularlar smooth muscle cells proliferation through angiotensin signaling (PubMed:23782690).
Biological Process
Aorta development Source: UniProtKB
Aorta smooth muscle tissue morphogenesis Source: UniProtKB
Elastic fiber assembly Source: UniProtKB
Negative regulation of vascular associated smooth muscle cell proliferation Source: UniProtKB
Positive regulation of aortic smooth muscle cell differentiation Source: UniProtKB
Positive regulation of collagen fibril organization Source: UniProtKB
Positive regulation of smooth muscle cell-matrix adhesion Source: UniProtKB
Regulation of collagen fibril organization Source: UniProtKB
Vascular associated smooth muscle cell development Source: UniProtKB
Cellular Location
Extracellular matrix; Basement membrane. Localizes on the microfibrils surrounding ELN cores.
Involvement in disease
Cutis laxa, autosomal recessive, 1B (ARCL1B):
A connective tissue disorder characterized by loose, hyperextensible skin with decreased resilience and elasticity leading to a premature aged appearance. Face, hands, feet, joints, and torso may be differentially affected. The clinical spectrum of autosomal recessive cutis laxa is highly heterogeneous with respect to organ involvement and severity. ARCL1B features include emphysema, lethal pulmonary artery occlusion, aortic aneurysm, cardiopulmonary insufficiency, birth fractures, arachnodactyly, and fragility of blood vessels.
PTM
N-glycosylated; contains mostly complex-type glycans (PubMed:27339457, PubMed:23782690). Not O-glycosylated (PubMed:27339457).
Cleaved by ELANE; produces a 50-55 kDa fragment (PubMed:27339457). Cleaved by MMP2 and MMP9; produces several fragments (PubMed:27339457).

Li, N., Ji, G. X., & Yang, Z. Y. (2022). EFEMP2 increases the invasion ability of cervical cancer cells by promoting EMT via the Raf/MEK/ERK signaling pathway. Neoplasma, 220117N74-220117N74.

Zhou, Q., Chen, S., Lu, M., Luo, Y., Wang, G., Xiao, Y., ... & Wang, X. (2022). Erratum: EFEMP2 suppresses epithelial-mesenchymal transition via Wnt/β-catenin signaling pathway in human bladder cancer: Erratum. International Journal of Biological Sciences, 18(9), 3798-3799.

Shen, Y., Zhou, T., Liu, X., Liu, Y., Li, Y., Zeng, D., ... & Zhang, M. (2021). Sevoflurane-induced miR-211-5p promotes neuronal apoptosis by inhibiting Efemp2. ASN neuro, 13, 17590914211035036.

Loeys, B., De Paepe, A., & Urban, Z. (2020). EFEMP2-related cutis laxa.

Song, L., Li, X. X., Liu, X. Y., Wang, Z., Yu, Y., Shi, M., ... & He, X. P. (2020). EFEMP2 suppresses the invasion of lung cancer cells by inhibiting epithelial-mesenchymal transition (EMT) and down-regulating MMPs. OncoTargets and therapy, 13, 1375.

Huang, L., Wang, Z., Chang, Y., Wang, K., Kang, X., Huang, R., ... & Hu, H. (2020). EFEMP2 indicates assembly of M0 macrophage and more malignant phenotypes of glioma. Aging (Albany NY), 12(9), 8397.

Zhou, Q., Chen, S., Lu, M., Luo, Y., Wang, G., Xiao, Y., ... & Wang, X. (2019). EFEMP2 suppresses epithelial-mesenchymal transition via Wnt/β-catenin signaling pathway in human bladder cancer. International journal of biological sciences, 15(10), 2139.

Kang, N., Zhou, J., Xu, J., Zhou, D., & Shi, W. (2019). EFEMP2 Inhibits Breast Cancer Invasion And Metastasis In Vitro And In Vivo. OncoTargets and therapy, 12, 8915.

Zuo, T., Shan, J., Liu, Y., Xie, R., Yu, X., & Wu, C. (2018). EFEMP2 mediates GALNT14-dependent breast cancer cell invasion. Translational oncology, 11(2), 346-352.

Letard, P., Schepers, D., Albuisson, J., Bruneval, P., Spaggiari, E., Van de Beek, G., ... & Guimiot, F. (2018). Severe phenotype of cutis laxa type 1B with antenatal signs due to a novel homozygous nonsense mutation in EFEMP2. Molecular Syndromology, 9(4), 190-196.

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

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