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The protein encoded by BGN is a small cellular or pericellular matrix proteoglycan that is closely related in structure to two other small proteoglycans, decorin and fibromodulin. Additionally we are shipping Biglycan Antibodies (116) and Biglycan Kits (27) and many more products for this protein.
Showing 10 out of 27 products:
Human Biglycan Protein expressed in Wheat germ - ABIN1346652
Yamada, Ozawa, Tomoeda, Matoba, Matsubara, Murakami: Regulation of PLAP-1 expression in periodontal ligament cells. in Journal of dental research 2006
Human Biglycan Protein expressed in Escherichia coli (E. coli) - ABIN1098780
Babelova, Moreth, Tsalastra-Greul, Zeng-Brouwers, Eickelberg, Young, Bruckner, Pfeilschifter, Schaefer, Gröne, Schaefer: Biglycan, a danger signal that activates the NLRP3 inflammasome via toll-like and P2X receptors. in The Journal of biological chemistry 2009
biglycan exerts an important role in cell proliferation, migration, invasion and apoptosis in colon cancer.
BGN might play an important role on metastasis in human endometrial cancer and it might be a target marker for the molecular therapy of advanced and recurrence endometrial cancer.
This study demonstrated that the small leucine-rich proteoglycan (show Vcan Proteins) BGN accumulates in CADASIL (show NOTCH3 Proteins) and binds to NOTCH3 (show NOTCH3 Proteins).
Biglycan may have a role in development of vascular damage in smokers
BGN is a factor secreted by peritubular cells to modulate FGFR3c signaling and thus contributes to the regulation of spermatogonial maintenance
The results suggest that regions within BGN is associated with ACL (show ACLY Proteins) injury susceptibility and that genetic sequence variability within genes encoding proteoglycans may potentially modulate the ligament fibril properties.
immunolocalization of decorin (show DCN Proteins) and biglycan in samples of first-trimester and term placentas, placenta accreta, invasive mole, and choriocarcinoma
Biglycan modulates angiogenesis and bone formation during fracture healing.
Data indicate that the biglycan (BGN) CC genotype was significantly over-represented in the control group versus the carpal tunnel syndrome (CTS (show TTR Proteins)) group.
High expression of BGN in esophageal squamous cell carcinoma indicated aggressive tumor behaviors and predicted a worse clinical outcome.
Importance of biglycan and decorin (show DCN Proteins) as targets for the manipulation of fetal membrane extracellular matrix stability in the context of inflammation.
Biglycan deficiency leads to loosely packed aortic collagen fibers, increased susceptibility of aortic elastin (show ELN Proteins) fibers to angII-induced stress, and up-regulation of vascular perlecan (show HSPG2 Proteins) content.
Biglycan signaling supported fetal membrane remodeling during early gestation in the absence of concomitant changes in TGFbeta (show TGFB1 Proteins) levels.
Lumican (show LUM Proteins) and biglycan influence corneal keratocyte lamellipodia organization and are critical in the regulation of stromal collagen fibrillogenesis.
Biglycan-triggered TLR-2- and TLR-4 (show TLR4 Proteins)-signaling exacerbates the pathophysiology of ischemic acute kidney injury.
De novo expression of circulating biglycan evokes an innate inflammatory tissue response via MyD88 (show MYD88 Proteins)/TRIF (show RNF138 Proteins) pathways.
Early stage patellar tendon healing was inferior in biglycan-null and decorin (show DCN Proteins)-null mice as compared to wild type.
This suggests that biglycan and decorin (show DCN Proteins) may have sequential roles in the tendon response to injury.
Mast cell chymase (show CMA1 Proteins) degrades the alarmins heat shock protein 70 (show HSP70 Proteins), biglycan, HMGB1 (show HMGB1 Proteins), and interleukin-33 (IL-33 (show IL33 Proteins)) and limits danger-induced inflammation.
extracellular matrix biglycan mediates breast cancer normalization induced by embryonic mesenchyme
Bgn regulates BMP4 (show BMP4 Proteins) signaling through modulation of Chordin (show CHRD Proteins) anti-BMP4 (show BMP4 Proteins) activity.
LDL electrostatic interactions with decorin (show DCN Proteins) and biglycan in the aortic valve leaflets and vascular wall is a major source of LDL retention.
Data show that biglycan, collagen type I, collagen type II, decorin (show DCN Proteins), and versican (show Vcan Proteins) were significantly affected by vibration duration, frequency, and amplitude.
biglycan showed a unique ability to organize collagen VI into extensive hexagonal-like networks over a time period of only a few minutes
biglycan-induced fibroblast cytoskeletal and signalling changes result in an increased cell migration; potential role in the remodelling process
The results indicate that CTGF (show CTGF Proteins) suppresses the synthesis of biglycan but newly induced that of decorin (show DCN Proteins) in the cells when the cell density is low.
The protein encoded by this gene is a small cellular or pericellular matrix proteoglycan that is closely related in structure to two other small proteoglycans, decorin and fibromodulin. The encoded protein and decorin are thought to be the result of a gene duplication. Decorin contains one attached glycosaminoglycan chain, while this protein probably contains two chains. For this reason, this protein is called biglycan. This protein plays a role in assembly of collagen fibrils and muscle regeneration. It interacts with several proteins involved in muscular dystrophy, including alpha-dystroglycan, alpha- and gamma-sarcoglycan and collagen VI, and it is critical for the assembly of the dystrophin-associated protein complex.
, biglycan proteoglycan
, bone/cartilage proteoglycan I
, bone/cartilage proteoglycan-I
, dermatan sulphate proteoglycan I
, small leucine-rich protein 1A
, Small proteoglycan I (biglycan), bone (BSPG1) (bone/cartilage proteclycan 1 precursor)
, bone/cartilage proteclycan 1
, leucine-rich PG I