Recombinant Human Biglycan protein is a Human Full Length protein, in the 20 to 368 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
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| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application HPLC | Reactivity Reacts | Dilution info - | Notes - |
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SLRR1A, BGN, Biglycan, Bone/cartilage proteoglycan I, PG-S1
Recombinant Human Biglycan protein is a Human Full Length protein, in the 20 to 368 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
pH: 7.2
Constituents: 99% Phosphate Buffer, 0.88% Sodium chloride
Greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE.
May be involved in collagen fiber assembly.
Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class I subfamily.
The two attached glycosaminoglycan chains can be either chondroitin sulfate or dermatan sulfate.
Biglycan also known as BGN is a small leucine-rich proteoglycan with a molecular weight of roughly 38 kDa. Researchers frequently observe Biglycan in tissues such as bone cartilage and vasculature. The protein interacts with several other molecules in the extracellular matrix (ECM) including collagen and elastin to maintain the structural integrity of tissues. Through these interactions Biglycan plays an important role in supporting cell attachment and matrix organization.
The protein Biglycan influences cellular processes such as growth and differentiation. It is part of a complex network within the ECM that modulates cell signaling. Biglycan interacts with growth factors like transforming growth factor-beta (TGF-beta) and binds to Toll-like receptors (TLRs) affecting immune responses. These capabilities reveal Biglycan’s involvement in tissue development and repair.
Extracellular matrix modulation shows a significant role for Biglycan. It is involved in the TGF-beta signaling pathway and the inflammatory pathway mediated by TLRs. Through these pathways Biglycan interacts with proteins such as decorin and fibromodulin contributing to the regulation of collagen fibrillogenesis and inflammatory responses. Its role in these pathways highlights Biglycan’s influence in cellular communication and matrix regulation.
Biglycan has associations with osteoarthritis and muscular dystrophy. In osteoarthritis researchers observe altered expression levels of Biglycan which affects cartilage integrity. In muscular dystrophy the protein’s connection to dystrophin an important structural protein is noted. These associations illustrate Biglycan's impact on disease progression and its potential as a therapeutic target.
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