Recombinant Mouse Biglycan / BGN Protein (Fc Tag)
Beta LifeScience
SKU/CAT #: BLPSN-0404

Recombinant Mouse Biglycan / BGN Protein (Fc Tag)
Beta LifeScience
SKU/CAT #: BLPSN-0404
Catalog No.: BLPSN-0404
Product Overview
Tag | Fc |
Host Species | Mouse |
Accession | NP_031568.2 |
Synonym | BG, DSPG1, PG-S1, PGI, SLRR1A |
Background | Biglycan, also known as PG-S1 and BGN, is a a small leucine-rich repeat proteoglycan (SLRP). It can be detected in a variety of extracellular matrix tissues, including bone, cartilage and tendon. Biglycan consists of a protein core containing leucine-rich repeat regions and two glycosaminoglycan (GAG) chains consisting of either chondroitin sulfate (CS) or dermatan sulfate (DS). Non-glycanated forms of biglycan (no GAG chains) increase with age in human articular cartilage. Biglycan interacts with collagen, both via the core protein and GAG chains. Biglycan plays a role in the mineralisation of bone. Biglycan core protein binds to the growth factors BMP-4 and influences its bioactivity. |
Description | A DNA sequence encoding the mouse BGN (Met1-Lys369) was expressed with the Fc region of human IgG1 at the C-terminus. |
Source | HEK293 |
Predicted N Terminal | Glu 20 |
AA Sequence | Met1-Lys369 |
Molecular Weight | The recombinant mouse BGN /Fc is a disulfide-linked homodimer. The reduced monomer comprises 591 a.a. and has a predicted molecular mass of 66.5 KDa. The apparent molecular mass of the protein is approximately 67 KDa in SDS-PAGE under reducing conditions due to glycosylation. |
Purity | >85% as determined by SDS-PAGE |
Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method |
Bioactivity | Please contact us for detailed information |
Formulation | Lyophilized from sterile PBS, pH 7.4.. |
Stability | The recombinant proteins are stable for up to 1 year from date of receipt at -70°C. |
Usage | For Research Use Only |
Storage | Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |