BGN Human, Sf9

Biglycan Human Recombinant, Sf9
Cat. No.
BT27073
Source

Sf9, Insect cells.

Synonyms

BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.

Appearance

Sterile filtered colorless solution.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

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.

Product Specs

Introduction
Biglycan (BGN) is a small proteoglycan found in the cellular matrix and surrounding cells. It plays a crucial role in the formation of collagen fibrils and the regeneration of muscle tissue. Structurally similar to decorin and fibromodulin, BGN interacts with various proteins implicated in muscular dystrophy, including alpha-dystroglycan, alpha- and gamma-sarcoglycan, and collagen VI. Furthermore, BGN is essential for the assembly of the dystrophin-associated protein complex.
Description
Produced in Sf9 insect cells, BGN is a single, glycosylated polypeptide chain consisting of 340 amino acids (residues 38-368) and possessing a molecular mass of 38.3 kDa. On SDS-PAGE, its molecular size appears to be approximately 40-57 kDa. This BGN protein is engineered with a 9-amino acid His tag at its C-terminus and purified using proprietary chromatographic methods.
Physical Appearance
Clear, sterile solution without any color.
Formulation
The provided BGN solution has a concentration of 0.5 mg/ml and is buffered with Phosphate Buffered Saline (pH 7.4) containing 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep the vial refrigerated at 4°C. For extended periods, store frozen at -20°C. It is advisable to add a carrier protein such as HSA or BSA (0.1%) for long-term storage. Avoid repeated cycles of freezing and thawing.
Purity
SDS-PAGE analysis indicates a purity of greater than 90.0%.
Biological Activity
The half-maximal effective concentration (ED50) for this protein is less than or equal to 20 µg/ml. Biological activity is determined by measuring the inhibition of cell growth in 3T3-L1 mouse embryonic fibroblast adipose-like cells.
Synonyms

BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.

Source

Sf9, Insect cells.

Amino Acid Sequence

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.

Product Science Overview

Introduction

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.

Structure and Function

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 .

Biological Significance

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 .

Recombinant Production in Sf9 Cells

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 and Therapeutic Applications

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 .

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