Sf9, Insect cells.
BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.
Sterile filtered colorless solution.
Greater than 90.0% as determined by SDS-PAGE.
BGN produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 340 amino acids (38-368 a.a.) and having a molecular mass of 38.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).
BGN is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.
Sf9, Insect cells.
ADPDEEASGA DTSGVLDPDS VTPTYSAMCP FGCHCHLRVV QCSDLGLKSV PKEISPDTTL LDLQNNDISE LRKDDFKGLQ HLYALVLVNN KISKIHEKAF SPLRKLQKLY ISKNHLVEIP PNLPSSLVEL RIHDNRIRKV PKGVFSGLRN MNCIEMGGNP LENSGFEPGA FDGLKLNYLR ISEAKLTGIP KDLPETLNEL HLDHNKIQAI ELEDLLRYSK LYRLGLGHNQ IRMIENGSLS FLPTLRELHL DNNKLARVPS GLPDLKLLQV VYLHSNNITK VGVNDFCPMG FGVKRAYYNG ISLFNNPVPY WEVQPATFRC VTDRLAIQFG NYKKHHHHHH.
Biglycan is a small leucine-rich proteoglycan (SLRP) that plays a crucial role in the extracellular matrix (ECM). It is involved in various biological processes, including collagen fibril organization, cell signaling, and tissue repair. The recombinant form of human biglycan, produced in Sf9 insect cells, is used in research to study its functions and potential therapeutic applications.
Biglycan is characterized by its core protein, which contains leucine-rich repeats (LRR) and is bound to glycosaminoglycan (GAG) chains. This structure allows biglycan to interact with collagen and other ECM components, contributing to the structural integrity of tissues . Additionally, biglycan can bind to cell surface receptors, such as toll-like receptors (TLR)-2 and TLR-4, initiating signaling pathways that regulate inflammation and immune responses .
Biglycan is essential for maintaining the structural organization of the ECM and mediating cell signaling. Dysregulation of biglycan expression has been linked to various clinical conditions, including metabolic disorders, inflammatory diseases, musculoskeletal defects, and cancer . In cancer, high levels of biglycan expression are associated with tumor growth, invasion, and metastasis, making it a potential marker for poor clinical outcomes .
The recombinant production of human biglycan in Sf9 insect cells involves the use of baculovirus expression systems. This method allows for the efficient production of large quantities of recombinant protein with post-translational modifications similar to those found in humans. The recombinant biglycan produced in Sf9 cells is used in various research applications, including studies on its biological functions and potential therapeutic uses.
Research on recombinant biglycan has provided insights into its role in various diseases and its potential as a therapeutic target. For example, studies have shown that inhibiting biglycan can normalize the tumor microenvironment and enhance the efficacy of chemotherapy in breast cancer . Additionally, biglycan’s role in inflammation and immune responses makes it a potential target for treating inflammatory and metabolic disorders .