BGN Human

Biglycan Human Recombinant
Cat. No.
BT27007
Source
E.coli.
Synonyms
DSPG1, PG-S1, PGI, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, BGN.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85% 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 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (38-368a.a) and having a molecular mass of 39.5kDa. BGN is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Biglycan (BGN) is a small leucine-rich repeat proteoglycan present in various connective tissues. It plays a crucial role in collagen fibrillogenesis, cell signaling, and tissue repair.
Description
Recombinant human BGN, expressed in E. coli, is a single, non-glycosylated polypeptide chain encompassing amino acids 38 to 368. It includes a 21 amino acid His-tag at the N-terminus and has a molecular weight of 39.5 kDa. Purification is achieved through proprietary chromatographic methods.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The BGN protein is supplied in a solution at a concentration of 1 mg/ml. The solution is buffered with 20mM Tris-HCl at pH 8.0 and contains 10% glycerol and 0.4M Urea.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 85% using SDS-PAGE analysis.
Synonyms
DSPG1, PG-S1, PGI, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, BGN.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDEEASGADT SGVLDPDSVT PTYSAMCPFG CHCHLRVVQC SDLGLKSVPK EISPDTTLLD LQNNDISELR KDDFKGLQHL YALVLVNNKI SKIHEKAFSP LRKLQKLYIS KNHLVEIPPN LPSSLVELRI HDNRIRKVPK GVFSGLRNMN CIEMGGNPLE NSGFEPGAFD GLKLNYLRIS EAKLTGIPKD LPETLNELHL DHNKIQAIEL EDLLRYSKLY RLGLGHNQIR MIENGSLSFL PTLRELHLDN NKLARVPSGL PDLKLLQVVY LHSNNITKVG VNDFCPMGFG VKRAYYNGIS LFNNPVPYWE VQPATFRCVT DRLAIQFGNY KK.

Product Science Overview

Introduction

Biglycan is a small leucine-rich proteoglycan (SLRP) that plays a crucial role in the extracellular matrix (ECM) of various tissues, including bone, cartilage, and tendon . It is encoded by the BGN gene located on the X chromosome in humans . Recombinant human biglycan is a laboratory-produced version of this protein, designed to mimic its natural form and function.

Structure and Function

Biglycan belongs to the class I SLRP family, characterized by a core protein with leucine-rich repeats (LRRs) and N-terminal and C-terminal cysteine-rich domains . These structural features enable biglycan to interact with other ECM components, such as collagen fibrils, and mediate cell signaling .

Role in the Extracellular Matrix

As a key component of the ECM, biglycan contributes to the structural organization of tissues and the delivery of external cues to cells . It participates in scaffolding collagen fibrils, which is essential for maintaining the integrity and function of connective tissues . Additionally, biglycan interacts with toll-like receptors (TLR)-2 and TLR-4 on immune cells, initiating inflammation and aggravating inflammatory disorders .

Clinical Significance

Dysregulation of biglycan expression is associated with various clinical conditions, including metabolic disorders, inflammatory disorders, musculoskeletal defects, and malignancies . For instance, high biglycan expression is linked to tumor growth, invasion, and metastasis, which are associated with poor clinical outcomes in cancer patients . In the musculoskeletal system, biglycan strengthens tissues, and its absence can lead to defects .

Recombinant Human Biglycan

Recombinant human biglycan is produced using advanced biotechnological methods to ensure high purity and functionality . It is often used in research to study its effects on cell growth, signaling pathways, and interactions with other proteins . For example, recombinant human biglycan has been shown to enhance utrophin expression and increase its bioavailability in developing myocytes, which is beneficial in models of muscular dystrophy .

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