Recombinant Mouse Decorin Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-1052NP
BL-1052NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-1052NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Mouse Decorin Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-1052NP
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description Recombinant Mouse Decorin is produced by our Mammalian expression system and the target gene encoding Gly17-Lys354 is expressed with a 6His tag at the C-terminus.
Accession P28654
Synonym Decorin; Bone proteoglycan II; PG-S2; PG40; Dcn
Gene Background Decorin, also known as PG40 and DCN, is a member of the class I family of small leucine-rich proteoglycans (SLRPs) that is expressed in the stroma of various forms of cancer and has been recently proposed to act as a guardian from the matrix. Mature human Decorin contains 12 tandem LRR and shares 80% and 78% aa sequence identity with mouse and rat Decorin, respectively. Decorin embraces numerous functions including: regulation of collagen fibrillogenesis, hepatic carcinogenesis, fetal membrane and calcium homeostasis, keratinocyte function, and suppression of angiogenesis. Most recently, soluble decorin has been shown to induce autophagy in endothelial cells and mitophagy in breast carcinoma cells.
Molecular Mass 39 KDa
Apmol Mass 41-50 KDa, reducing conditions
Formulation Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

Target Details

Target Function May affect the rate of fibrils formation.
Subcellular Location Secreted, extracellular space, extracellular matrix.
Protein Families Small leucine-rich proteoglycan (SLRP) family, SLRP class I subfamily
Database References

Gene Functions References

  1. The absence of a dermatan sulfate chain on decorin does not appear to overtly influence its functional properties in vivo. PMID: 28412940
  2. Fibroblasts differentiated to adipocytes and treated with TIP39 also showed increased decorin and production of chondroitin sulfate. Furthermore, the skin of PTH2R(-/-) mice showed abnormal extracellular matrix structure, decreased decorin expression, and skin hardness. PMID: 28454729
  3. The disruption of decorin-restricted TGFbeta signalling leads to higher stiffness of articular cartilage matrix, rendering joints more resistant to osteoarthritis. PMID: 27377816
  4. We could show that ablation of either candidate enhanced adipogenesis in visceral preadipocytes, while treatment of primary cultures with recombinant Sparcl1 and Dcn blocked adipogenesis in a dose dependent manner. In conclusion, our data suggests that the differences in adipogenesis between depots might be due to paracrine and autocrine feedback mechanisms which could in turn contribute to metabolic homeostasis PMID: 27317982
  5. A synthetic peptide corresponding to this decorin region dose-dependently inhibited the response to myostatin in cardiomyocytes PMID: 27559042
  6. Systemic delivery of an oncolytic adenovirus expressing decorin for the treatment of breast cancer bone metastases reduced tumor burden and inhibited bone destruction. PMID: 26467629
  7. Decorin is an autophagy-inducible proteoglycan and is required for proper in vivo autophagy. PMID: 26344480
  8. The results suggest that decorin plays a dual role in AAA. Adventitial decorin in normal aorta may protect against the development of AAA PMID: 25781946
  9. Development of congenital stromal dystrophy is dependent on export and extracellular deposition of truncated decorin. PMID: 26029887
  10. decorin may modulate follicular cycling and morphogenesis PMID: 24816226
  11. We found that decorin is abundantly secreted and deposited in normal connective tissue but its expression is consistently decreased in the tumor microenvironment. PMID: 24634138
  12. Decorin signaling supported fetal membrane remodeling at early stages of gestation in a TGFbeta-dependent manner, and fetal membrane stabilization at later stages of gestation without changes in TGFbeta levels. PMID: 24373743
  13. A decorin-deficient matrix affects skin chondroitin/dermatan sulfate levels and keratinocyte function. PMID: 24447999
  14. Decorin deficiency promotes hepatic carcinogenesis. PMID: 24361483
  15. decorin secreted from myotubes in response to exercise is involved in the regulation of muscle hypertrophy and hence could play a role in exercise-related restructuring processes of skeletal muscle. PMID: 24996176
  16. the gene encoding the small leucine-rich proteoglycan decorin is repressed by FOXD1 in cortical interstitial cells, compound genetic inactivation of DCN partially rescues the failure of progenitor cell differentiation in the Foxd1 null. PMID: 24284212
  17. Dimerization could be abolished by engineering glycosylation sites into the dimer interface; other interface mutants remained dimeric. The monomeric mutants were as stable as wild-type decorin in thermal unfolding experiments. PMID: 24169694
  18. Decorin lacking c-terminal repeat is retained intracellularly, its accumulation triggering endoplasmic reticulum stress that results in abnormal synthesis and secretion, leading to congenital stromal corneal dystrophy. PMID: 23685109
  19. Alterations in glycosylated decorin core protein might be implicated in myocardial remodeling and reverse remodeling, with a potential important role for CS/DS GAG chain-synthesizing enzymes. PMID: 23412898
  20. decorin induced VEGFR2-dependent mitochondrial fragmentation and loss of mitochondrial membrane potential PMID: 23798385
  21. decorin modulates delayed-type hypersensitivity responses by augmenting the induction of downstream effector cytokines of IFN-gamma and TNF-alpha, thereby influencing the recruitment of CD8(+) lymphocytes into the inflamed tissue. PMID: 23460644
  22. Lack of decorin leads to enhanced tumor formation in the liver. PMID: 23448253
  23. These data show for the first time that decorin has an impact on the biology of alpha2beta1 integrin and the vimentin intermediate filament system. PMID: 23226541
  24. DCN gene can inhibit the growth of nude mice xenograft, which is probably related with the decreased expressions of TGF-beta1 and MMP-9 protein and the inhibition of tumor angiogenesis. PMID: 23046927
  25. Decorin protein core affects the global gene expression profile of the tumor microenvironment in a triple-negative orthotopic breast carcinoma xenograft model. PMID: 23029096
  26. decorin plays a role in tendon viscoelasticity that cannot be completely explained by its role in collagen fibrillogenesis PMID: 22482685
  27. The expression of decorin, a naturally occurring TGF-beta suppressor, was elevated in Mstn-null mice. PMID: 22277753
  28. Decorin regions LRR6 and LRR5 participate in the interaction with LRP-1 and TGF-beta as well as in its dependent signaling. PMID: 22203668
  29. Wild type N-ras appears to mediate its anti-malignant effect by downregulating decorin expression. PMID: 21809347
  30. decorin prevented translational repression of PDCD4 by decreasing the activity of transforming growth factor-beta1 and the abundance of oncogenic miR-21, a translational inhibitor of PDCD4. PMID: 22087031
  31. Cleavage product of decorin serves as a functional receptor of resistin in adipocyte progenitors and may regulate white adipose tissue expansion. PMID: 21683670
  32. gradual increase in muscle regeneration PMID: 21416223
  33. these results implicated a role for decorin in mediating delayed-type hypersensitivity responses by influencing polymorphonuclear leukocyte attachment to the endothelium. PMID: 22043007
  34. Decorin is expressed in placenta/fetal membranes and is developmentally regulated in fetal membranes; data from mutant mouse strains suggest that both decorin and biglycan contribute to gestational success (i.e., prevent premature birth). PMID: 21502335
  35. We show a so far unknown function of decorin and chondroitin-6-sulfate: their ability to inhibit B16V cell migration by intracellular acidification. PMID: 21792923
  36. CTGF specifically induced the synthesis of decorin, suggesting a mechanism of autoregulation. PMID: 21454550
  37. Decorin can modify collagen I-stimulated, but not fibronectin-stimulated myoblast migration in vitro. PMID: 21059388
  38. decorin is a protective agent during the development of diabetic nephropathy PMID: 20083846
  39. Dcn has been identified as an imprinted gene by high-throughput screening using RIKEN cDNA microarray. PMID: 11820791
  40. decorin is dramatically induced in the desmin-null myocardium PMID: 11891192
  41. decorin exerts beneficial effects on tubulointerstitial fibrosis PMID: 11891213
  42. decorin binds fibrinogen in a Zn2+-dependent interaction PMID: 12582160
  43. 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
  44. Inhibition of myoblast migration via decorin expression is critical for normal skeletal muscle differentiation. PMID: 12871697
  45. These alterations in lung tissue mechanical behavior in Dcn-/- mice support a critical role for decorin in the formation of the lung collagen network. PMID: 15447936
  46. in DCN-deficient mice, the growth of corneal vessels was significantly diminished PMID: 15528932
  47. Results describe the effect of bone morphogenetic protein-2 (BMP-2) on the synthesis of proteoglycan during osteogenic conversion of myoblasts and suggest a role for decorin in cell response to BMP-2. PMID: 15920756
  48. decorin is not required for cell survival PMID: 15949467
  49. decorin is required for the proper fibrotic evolution of myocardial infarctions PMID: 15949932
  50. systemic overexpression of decorin reduces inflammation, triglycerides and fibrosis in atherosclerotic plaques of ApoE(-/-) mice resulting in slowing down of disease progression PMID: 16183063

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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.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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