Recombinant Mouse Biglycan (BGN) Protein (His)

Beta LifeScience SKU/CAT #: BLC-05135P
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Bgn.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Bgn.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Bgn.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Bgn.

Recombinant Mouse Biglycan (BGN) Protein (His)

Beta LifeScience SKU/CAT #: BLC-05135P
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Product Overview

Description Recombinant Mouse Biglycan (BGN) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P28653
Target Symbol BGN
Synonyms Bgn; Biglycan; Bone/cartilage proteoglycan I; PG-S1
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-10His
Target Protein Sequence DEEASGSDTTSGVPDLDSVTPTFSAMCPFGCHCHLRVVQCSDLGLKTVPKEISPDTTLLDLQNNDISELRKDDFKGLQHLYALVLVNNKISKIHEKAFSPLRKLQKLYISKNHLVEIPPNLPSSLVELRIHDNRIRKVPKGVFSGLRNMNCIEMGGNPLENSGFEPGAFDGLKLNYLRISEAKLTGIPKDLPETLNELHLDHNKIQAIELEDLLRYSKLYRLGLGHNQIRMIENGSLSFLPTLRELHLDNNKLSRVPAGLPDLKLLQVVYLHSNNITKVGINDFCPMGFGVKRAYYNGISLFNNPVPYWEVQPATFRCVTDRLAIQFGNYKK
Expression Range 38-369aa
Protein Length Full Length of Mature Protein
Mol. Weight 43.4 kDa
Research Area Signal Transduction
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function May be involved in collagen fiber assembly.
Subcellular Location Secreted, extracellular space, extracellular matrix.
Protein Families Small leucine-rich proteoglycan (SLRP) family, SLRP class I subfamily
Database References

KEGG: mmu:12111

STRING: 10090.ENSMUSP00000033741

UniGene: PMID: 28882761

  • A novel biological pathway has been discovered of soluble biglycan inducing HIF-2alpha protein stabilization and Epo production presumably in an oxygen-independent manner, ultimately giving rise to secondary polycythemia. PMID: 27600268
  • Results show that Bgn plays a role in the process of angiogenesis during fracture healing, and that effect appears to be partially mediated through endostatin suppression. PMID: 27072616
  • Asporin deficiency changes skin glycosaminoglycan composition, and decorin and biglycan content, which may explain the changes in skin mechanical properties. PMID: 28859141
  • Biglycan plays a protective role during the progression of atherosclerosis in ApoE-deficient mice by inhibiting thrombin generation. PMID: 27034473
  • These genes were concordantly induced by TAC in WT but not in biglycan KO mice. CONCLUSIONS: Left ventricular pressure overload induces biglycan expression in cardiac fibroblasts. Ablation of biglycan improves cardiac function and attenuates left ventricular hypertrophy and fibrosis after long-term pressure overload. PMID: 27789290
  • Importance of biglycan and decorin as targets for the manipulation of fetal membrane extracellular matrix stability in the context of inflammation. PMID: 25914258
  • Biglycan deficiency leads to loosely packed aortic collagen fibers, increased susceptibility of aortic elastin fibers to angII-induced stress, and up-regulation of vascular perlecan content. PMID: 25093698
  • Biglycan signaling supported fetal membrane remodeling during early gestation in the absence of concomitant changes in TGFbeta levels. PMID: 24373743
  • Lumican and biglycan influence corneal keratocyte lamellipodia organization and are critical in the regulation of stromal collagen fibrillogenesis. PMID: 24447998
  • Biglycan-triggered TLR-2- and TLR-4-signaling exacerbates the pathophysiology of ischemic acute kidney injury. PMID: 24480070
  • De novo expression of circulating biglycan evokes an innate inflammatory tissue response via MyD88/TRIF pathways. PMID: 24361484
  • Early stage patellar tendon healing was inferior in biglycan-null and decorin-null mice as compared to wild type. PMID: 24157578
  • This suggests that biglycan and decorin may have sequential roles in the tendon response to injury. PMID: 24072490
  • Mast cell chymase degrades the alarmins heat shock protein 70, biglycan, HMGB1, and interleukin-33 (IL-33) and limits danger-induced inflammation. PMID: 24257755
  • extracellular matrix biglycan mediates breast cancer normalization induced by embryonic mesenchyme PMID: 23817524
  • Biglycan plays a role in tendon viscoelasticity that cannot be completely explained by its role in collagen fibrillogenesis. PMID: 23592048
  • Biglycan deletion alters adiponectin expression in murine adipose tissue and 3T3-L1 adipocytes. PMID: 23189205
  • The glycosaminoglycans chains of biglycan (BGN) promote BGN-assisted BMP-4 function. PMID: 22895561
  • Bgn inhibits the major properties of HER-2/neu-transformed cells, which is inversely modulated by the PKC signaling cascade. PMID: 22582394
  • Increased messenger RNA (mRNA) expression of extracellular matrix genes BGN and COL1A1 was observed in the mouse epididymal adipose tissue after high-fat diet. PMID: 21775118
  • Biglycan/decorin mixed double knockout mouse is a model of dystocia and delayed labor onset. PMID: 22253749
  • Extracellular matrix protein biglycan plays a novel role in regulating synapse stability. PMID: 22396407
  • Use of a transplant system and a fracture healing model revealed that expression of Wnt-induced secreted protein 1 was decreased in bone formed by biglycan-deficient cells, further suggesting reduced Wnt signaling in vivo. PMID: 21969569
  • Biglycan is expressed/developmentally regulated in placenta and fetal membranes; data from mutant mouse strains suggest that both biglycan and decorin contribute to gestational success (i.e., prevent premature birth). PMID: 21502335
  • critical for temporomandibular joint subchondral bone integrity PMID: 21917603
  • Biglycan and decorin reduced the proliferation of pre-adipocytes, partly by induction of apoptosis. Furthermore, the anti-proliferative capabilities of decorin and biglycan were nullified with removal of GAG side-chains. PMID: 21702857
  • bgn deficiency promotes myofibroblast differentiation and proliferation in vitro and in vivo likely due to increased responses to TGF-beta and SMAD2 signaling PMID: 21454527
  • Biglycan and fibromodulin are novel key players in regulating chondrogenesis and extracellular matrix turnover during temoporomandibular joint osteoarthritis pathology. PMID: 20035055
  • Biglycan deficiency significantly accelerated disc degeneration in mice. PMID: 19940720
  • Beta1 integrin and htis protein's binding sites are localized to different laminin-G-domain-like (LG) modules within the laminin alpha5 chain G domain. PMID: 12519075
  • decorin and biglycan play distinct roles in palatogenesis, and decorin was more actively involved in the process of secondary palate formation than biglycan. PMID: 12666199
  • biglycan deficient mice have diminished capacity to produce marrow stromal cells, the bone cell precursors, and this deficiency increases with age PMID: 12975603
  • Deficiency protects against increased trabecular bone turnover and bone loss in response to estrogen depletion. PMID: 14672350
  • bgn is required for retaining an appropriate microenvironment for the maturation of osteoblastic stem cells PMID: 15173106
  • In addition to the imbalance between differentiation and proliferation, there was a differential decrease in secretory leukocyte protease inhibitor (slpi) in bgn deficient osteoblasts treated with 1,25-(OH)(2)D(3) PMID: 16364709
  • biglycan is important for the maintenance of muscle cell integrity and plays a direct role in regulating the expression and sarcolemmal localization of the intracellular signaling proteins dystrobrevin-1 and -2, alpha- and beta1-syntrophin and nNOS PMID: 16807372
  • biglycan has a particularly important function during muscle and connective tissue development PMID: 16810681
  • Biglycan is a ligand for two members of the sarcoglycan complex and regulates their expression at discrete developmental ages. PMID: 16883602
  • Biglycan is a positive modulator of BMP-2 induced osteoblast differentiation PMID: 17120779
  • At embryonic day 18.5, alizarin red/alcian blue staining showed that the Bgn/Dcn double deficient mice had hypomineralization of the frontal and parietal craniofacial bones. PMID: 17188951
  • death of biglycan-deficient mice from aortic rupture implicates biglycan as essential for the structural and functional integrity of the aortic wall and implicates biglycan gene defects in the pathogenesis of aortic dissection and rupture PMID: 17502576
  • These preliminary data suggest that WISP-1 and BGN may functionally interact and control each other's activity, thus regulating the differentiation and proliferation of osteogenic cells. PMID: 18701807
  • Biglycan overexpression did not significantly affect the amelogenin expression in incisor and molar teeth in 3-day postnatal transgenic mice. PMID: 18727043
  • decorin has a primary role in regulating fibril assembly, a function that can be fine-tuned by biglycan during early development. PMID: 19136671
  • Findings indicate that normal expression of small leucine rich proteoglycans, such as biglycan and decorin, plays an important role in the highly orchestrated process of dentin mineralization. PMID: 19379665
  • By signaling through TLR2/4, biglycan stimulates the expression of NLRP3 and pro-IL-1beta mRNA. PMID: 19605353
  • Binds to the carboxyl-terminal third of the alpha-dystroglycan core polypeptide. This interaction requires the chondroitin sulfate side chains of biglycan. PMID: 10684260
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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

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