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Mouse Anti-BGN Recombinant Antibody (4E1-1G7) (CBMAB-P0101-YC)


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Published Data
Mouse Anti-BGN Recombinant Antibody (4E1-1G7) (CBMAB-P0101-YC) in IHC
Mouse Anti-BGN Recombinant Antibody (4E1-1G7) (CBMAB-P0101-YC) in IHC
Photomicrographs of BGN protein expression in (A) invasive ductal carcinoma, and in (B) normal breast tissue. Lung tissue was used as an external negative (C) and positive (D) control. Bars represent 50 μm. Scatter dot plot (E) demonstrates a significant reduction of BGN protein expression in breast cancer tissue, compared to benign breast tissue. ...View More
Thiesen, A. P., Mielczarski, B., & Savaris, R. F. (2023). Deep learning neural network image analysis of immunohistochemical protein expression reveals a significantly reduced expression of biglycan in breast cancer. PloS one, 18(3), e0282176.
Mouse Anti-BGN Recombinant Antibody (4E1-1G7) (CBMAB-P0101-YC) in IHC
Mouse Anti-BGN Recombinant Antibody (4E1-1G7) (CBMAB-P0101-YC) in IHC
Example of BGN expression in DAB only in photomicrographs, after color deconvolution in normal breast tissue (A) and with cancer (B), bars represent 50 μm. ...View More
Thiesen, A. P., Mielczarski, B., & Savaris, R. F. (2023). Deep learning neural network image analysis of immunohistochemical protein expression reveals a significantly reduced expression of biglycan in breast cancer. PloS one, 18(3), e0282176.
Mouse Anti-BGN Recombinant Antibody (4E1-1G7) (CBMAB-P0101-YC) in IHC and Immunoblot
Mouse Anti-BGN Recombinant Antibody (4E1-1G7) (CBMAB-P0101-YC) in IHC and Immunoblot
BGN protein in CADASIL and control brain. Immunohistochemical analysis of geneticallydefined CADASIL brains (A and B) and matched controls (C) was performed on frontal cortex sections with antibody 4E1-1G7. Penetrating arteries (A, C) and leptomeningeal (B) vessels are shown. Magnification is at 400x. (D) Brain lysates were analyzed by immunoblotting with 4E1-1G7 and the core BGN protein band was quantified for
CADASIL and control frontal cortex, normalized to tubulin levels. Protein was not treated with glycosidases. Difference were significant (p<0.05) for CADASIL samples versus controls. ...View More
Zhang, X., Lee, S. J., Young, M. F., & Wang, M. M. (2015). The small leucine-rich proteoglycan BGN accumulates in CADASIL and binds to NOTCH3. Translational stroke research, 6, 148-155.

Summary

Host Animal
Mouse
Specificity
Human
Clone
4E1-1G7
Antibody Isotype
IgG2a, κ
Application
WB, IF, IP, ELISA

Basic Information

Immunogen
Recombinant protein corresponding to aa 1-369 of human Proteoglycan 1.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
IHC3 μg/ml

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

Format
Liquid
Buffer
PBS
Preservative
None
Concentration
Batch dependent
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
biglycan
Introduction
BGN is a member of the small leucine-rich proteoglycan (SLRP) family of proteins. The encoded preproprotein is proteolytically processed to generate the mature protein, which plays a role in bone growth, muscle development and regeneration, and collagen fibril assembly in multiple tissues. This protein may also regulate inflammation and innate immunity. Additionally, the encoded protein may contribute to atherosclerosis and aortic valve stenosis in human patients. This gene and the related gene decorin are thought to be the result of a gene duplication.
Entrez Gene ID
633
UniProt ID
P21810
Alternative Names
SLRR1A; MRLS; PGI; SEMDX; DSPG1; PG-S1
Function
May be involved in collagen fiber assembly.
Biological Process
Articular cartilage development Source: Ensembl
Blood vessel remodeling Source: Ensembl
Bone development Source: Ensembl
Chondroitin sulfate biosynthetic process Source: Reactome
Chondroitin sulfate catabolic process Source: Reactome
Dermatan sulfate biosynthetic process Source: Reactome
Extracellular matrix organization Source: Reactome
Peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan Source: Ensembl
Cellular Location
Extracellular matrix
Involvement in disease
Meester-Loeys syndrome (MRLS): An X-linked, thoracic aortic aneurysm syndrome characterized by early-onset, severe aortic aneurysm and dissection. Other recurrent findings include hypertelorism, pectus deformity, joint hypermobility, contractures, and mild skeletal dysplasia.
Spondyloepimetaphyseal dysplasia, X-linked (SEMDX): An X-linked recessive bone disease characterized by severe short-trunk dwarfism, brachydactyly, metaphyseal flaring of lower extremities, short and broad long bone diaphyses, moderate platyspondyly, normal facies, and normal intelligence.
PTM
The two attached glycosaminoglycan chains can be either chondroitin sulfate or dermatan sulfate.
More Infomation

Shao, C., Cheng, C., Shao, Q., & Chen, B. (2021). Identification and Validation of Biglycan as Prognosis and Therapy Markers for Patients with Stomach Adenocarcinoma. International Journal of General Medicine, 14, 3497.

Salimi, H., Suzuki, A., Habibi, H., Orita, K., Hori, Y., Yabu, A., ... & Nakamura, H. (2021). Biglycan expression and its function in human ligamentum flavum. Scientific reports, 11(1), 1-13.

Hua, R., Ni, Q., Eliason, T. D., Han, Y., Gu, S., Nicolella, D. P., ... & Jiang, J. X. (2020). Biglycan and chondroitin sulfate play pivotal roles in bone toughness via retaining bound water in bone mineral matrix. Matrix Biology, 94, 95-109.

Scuruchi, M., Potì, F., Rodríguez-Carrio, J., Campo, G. M., & Mandraffino, G. (2020). Biglycan and atherosclerosis: Lessons from high cardiovascular risk conditions. Biochimica et Biophysica Acta (BBA)-Molecular and Cell Biology of Lipids, 1865(2), 158545.

Zhao, S. F., Yin, X. J., Zhao, W. J., Liu, L. C., & Wang, Z. P. (2020). Biglycan as a potential diagnostic and prognostic biomarker in multiple human cancers. Oncology letters, 19(3), 1673-1682.

Schulz, G. B., Grimm, T., Sers, C., Riemer, P., Elmasry, M., Kirchner, T., ... & Horst, D. (2019, August). Prognostic value and association with epithelial-mesenchymal transition and molecular subtypes of the proteoglycan biglycan in advanced bladder cancer. In Urologic Oncology: Seminars and Original Investigations (Vol. 37, No. 8, pp. 530-e9). Elsevier.

Zhang, Y. J., Qing, Q., Zhang, Y. J., Ning, L. J., Cui, J., Yao, X., ... & Qin, T. W. (2019). Enhancement of tenogenic differentiation of rat tendon‐derived stem cells by biglycan. Journal of cellular physiology, 234(9), 15898-15910.

Guo, D., Zhang, W., Yang, H., Bi, J., Xie, Y., Cheng, B., ... & Chen, S. (2019). Celastrol induces necroptosis and ameliorates inflammation via targeting biglycan in human gastric carcinoma. International journal of molecular sciences, 20(22), 5716.

Liu, B., Xu, T., Xu, X., Cui, Y., & Xing, X. (2018). Biglycan promotes the chemotherapy resistance of colon cancer by activating NF-κB signal transduction. Molecular and cellular biochemistry, 449(1), 285-294.

Jacobsen, F., Kraft, J., Schroeder, C., Hube-Magg, C., Kluth, M., Lang, D. S., ... & Melling, N. (2017). Up-regulation of biglycan is associated with poor prognosis and PTEN deletion in patients with prostate cancer. Neoplasia, 19(9), 707-715.

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

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