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anti-Human Biglycan Antibodies:
anti-Mouse (Murine) Biglycan Antibodies:
anti-Rat (Rattus) Biglycan Antibodies:
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Human Polyclonal Biglycan Primary Antibody for IHC, ELISA - ABIN188683
Antipova, Orgel: Non-enzymatic decomposition of collagen fibers by a biglycan antibody and a plausible mechanism for rheumatoid arthritis. in PLoS ONE 2012
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Human Polyclonal Biglycan Primary Antibody for IHC, IHC (p) - ABIN4284625
Van Bockstal, Lambein, Van Gele, De Vlieghere, Limame, Braems, Van den Broecke, Cocquyt, Denys, Bracke, Libbrecht, De Wever: Differential regulation of extracellular matrix protein expression in carcinoma-associated fibroblasts by TGF-β1 regulates cancer cell spreading but not adhesion. in Oncoscience 2015
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Human Polyclonal Biglycan Primary Antibody for IF (p), IHC (p) - ABIN872817
Huang, Zou, Shi, Zhang, Pen, Zhang, Gao, Wang: The effect of electroacupuncture on the extracellular matrix synthesis and degradation in a rabbit model of disc degeneration. in Evidence-based complementary and alternative medicine : eCAM 2014
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Human Polyclonal Biglycan Primary Antibody for WB - ABIN513714
Gasimli, Stansfield, Nairn, Liu, Paluh, Yang, Dordick, Moremen, Linhardt: Structural remodeling of proteoglycans upon retinoic acid-induced differentiation of NCCIT cells. in Glycoconjugate journal 2013
Rat (Rattus) Polyclonal Biglycan Primary Antibody for ELISA, WB - ABIN334359
Chen, Lenschow, Tiede, Fischer, Kalthoff, Ungefroren: Smad4/DPC4-dependent regulation of biglycan gene expression by transforming growth factor-beta in pancreatic tumor cells. in The Journal of biological chemistry 2002
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Human Monoclonal Biglycan Primary Antibody for IHC (p), IP - ABIN560056
Zhang, Lee, Young, Wang: The Small Leucine-Rich Proteoglycan BGN Accumulates in CADASIL and Binds to NOTCH3. in Translational stroke research 2015
BGN contributed to the formation of chemotherapy resistance in colon cancer cells by activating NF-kappaB signaling.
Study identified biglycan as a novel trigger of Th1 and Th17 cell recruitment into the kidney and chemoattractants production.
The differential immunoexpression of perlecan and biglycan in these types of ameloblastomas suggests their participation in the developmental process of these tumors.
TLR2 and BGN contribute to sterile inflammation and infertility in man.
Results show that Biglycan expression was upregulated by DNA demethylation in tumour endothelial cells from myeloma.
Elevated biglycan mRNA expression in adipose tissues of obese women
sex-specific allele combinations of BGN, COL5A1, and DCN, as well as eight miRNA recognition sequences, were associated with altered susceptibility to anterior cruciate ligament ruptures
high Bgn expression levels promote a more dense collagen architecture, leading to increased tissue stiffness. This increased tissue stiffness leads to higher integrin-beta1 expression on melanoma cells, which promotes their invasiveness.
The expression of hBGN in the skeletal muscle of the treated mice was 1.34-fold higher than that of the native mouse Bgn (mBgn). The low transduction efficiency and improved motor functions suggest that biglycan expressed in a small number of muscle fibers was likely to have been secreted and anchored to the cell surface throughout the whole muscular fibers
Results identified loss-of-function mutation in BGN gene in patients with an X-linked syndromic form of severe thoracic aortic aneurysms and dissections (TAAD) confirming BGN as causative gene in severe form of TAAD.
After the first year of smoking abstinence the levels of BGN expression and carotid-femoral pulse wave velocity are significantly improved as compared to baseline.
study reports a temporal relationship between altered placental biglycan expression and subsequent development of fetal growth restriction/small for gestational age.
Quantitative polymerase chain reaction for messenger RNA expression from tissue specimens revealed significantly higher expression of Biglycan (p = 0.0008) and Lumican (p = 0.01) and lower expression of Decorin (p < 0.0001) in urothelial carcinoma of bladder
Mutation in BGN gene is associated with X-Linked Spondyloepimetaphyseal Dysplasia.
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 BGN accumulates in CADASIL and binds to NOTCH3.
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 injury susceptibility and that genetic sequence variability within genes encoding proteoglycans may potentially modulate the ligament fibril properties.
biglycan is a novel high-affinity ligand for CD14, a well-known GPI-anchored co-receptor for TLRs.
Transcriptomic profiling of hypothalamus, hippocampus, and liver supported the regulatory action of Bgn on key molecular pathways involved in metabolism, immune response, and neuronal plasticity. Overall results underscore the tissue-specific role of the extracellular matrix in the regulation of metabolism and brain function, and support Bgn as a key modulator for the impact of fructose across body and brain.
our data indicates that Bgn and Fmod expressed by the bone forming cells, are novel coupling ECM components that control bone mass through sequestration of TNFalpha and/or RANKL, thereby adjusting their bioavailability in order to regulate osteoclastogenesis.
Bgn deficiency led to abrogation of contact hypersensitivity responses.
The increased atherosclerosis in biglycan deficient mice does not appear to be due to elevations in TGF-beta.
Knockout results provide evidence that decorin and biglycan are necessary for maintaining collagen fibril structure, fiber realignment, and mechanical properties of mature tendons.
A novel biological pathway has been discovered of soluble biglycan inducing HIF-2alpha protein stabilization and Epo production presumably in an oxygen-independent manner, ultimately giving rise to secondary polycythemia.
Results show that Bgn plays a role in the process of angiogenesis during fracture healing, and that effect appears to be partially mediated through endostatin suppression.
Asporin deficiency changes skin glycosaminoglycan composition, and decorin and biglycan content, which may explain the changes in skin mechanical properties.
Biglycan plays a protective role during the progression of atherosclerosis in ApoE-deficient mice by inhibiting thrombin generation.
These genes were concordantly induced by TAC in WT but not in biglycan KO mice. CONCLUSIONS: Left ventricular pressure overload induces biglycan expression in cardiac fibroblasts. Ablation of biglycan improves cardiac function and attenuates left ventricular hypertrophy and fibrosis after long-term pressure overload.
Importance of biglycan and decorin 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 fibers to angII-induced stress, and up-regulation of vascular perlecan content.
Biglycan signaling supported fetal membrane remodeling during early gestation in the absence of concomitant changes in TGFbeta levels.
Lumican and biglycan influence corneal keratocyte lamellipodia organization and are critical in the regulation of stromal collagen fibrillogenesis.
Biglycan-triggered TLR-2- and TLR-4-signaling exacerbates the pathophysiology of ischemic acute kidney injury.
De novo expression of circulating biglycan evokes an innate inflammatory tissue response via MyD88/TRIF pathways.
Early stage patellar tendon healing was inferior in biglycan-null and decorin-null mice as compared to wild type.
This suggests that biglycan and decorin may have sequential roles in the tendon response to injury.
Mast cell chymase degrades the alarmins heat shock protein 70, biglycan, HMGB1, and interleukin-33 (IL-33) and limits danger-induced inflammation.
Data show that biglycan, collagen type I, collagen type II, decorin, and versican 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 suppresses the synthesis of biglycan but newly induced that of decorin in the cells when the cell density is low.
LDL electrostatic interactions with decorin and biglycan in the aortic valve leaflets and vascular wall is a major source of LDL retention.
Bgn regulates BMP4 signaling through modulation of Chordin anti-BMP4 activity.
These differentially expressed proteins associated with key mechanisms involved in atherosclerosis and signaling mechanisms related with vitamin E.
Data rule out BGN as a candidate gene for a simple X-linked inheritance for bilateral corneal stromal loss in Friesian horses.
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.
, 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