Recombinant Human Decorin Protein (C-6His,Baculovirus)

Beta LifeScience SKU/CAT #: BL-1150NP
BL-1150NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-1150NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human Decorin Protein (C-6His,Baculovirus)

Beta LifeScience SKU/CAT #: BL-1150NP
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Product Overview

Description Recombinant Human Decorin is produced by our Baculovirus expression system and the target gene encoding Gly17-Lys359 is expressed with a 6His tag at the C-terminus.
Accession P07585
Synonym Decorin; Bone proteoglycan II; PG-S2; PG40; DCN; SLRR1B
Gene Background Decorin is a secreted chondroitin/dermatan sulfate proteoglycan in the family of small leucine-rich proteoglycans (SLRPs). SLRP family members are characterized by N-terminal and C-terminal cysteine-rich regions which flank the central region containing 10-12 tandem leucine-rich repeats (LRR). The human Decorin cDNA encodes a 359 amino acid (aa) precursor that includes a 16 aa signal sequence and a 14 aa propeptide. Alternate splicing of human Decorin generates five isoforms with variable length deletions. Decorin is an N-glycosylated protein that also carries a variablysized hybrid chondroitin/dermatan sulfate chain at Ser34. Decorin regulates assembly of the extracellular collagen matrix and the bioactivity of the matrix associated growth factors FGF2,GDF8/Myostatin, TGFβ,and WISP1. It also binds and activates EGF R, ErbB4, and IGFI-R. In vivo, Decorin promotes myoblast differentiation, supports angiogenesis, and inhibits tumor progression.
Molecular Mass 38.8 KDa
Apmol Mass 40-45 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
Associated Diseases Corneal dystrophy, congenital stromal (CSCD)

Gene Functions References

  1. Systemic rAAV-DCN in neuroblastoma-grafted nude mice inhibited stabilin-1. PMID: 28631095
  2. Our data suggests that the endometrium of patients with polycystic ovary syndrome (PCOS) exhibits higher expressions of decorin and lumican than that of healthy control women in the proliferative phase of the menstrual cycle. It is then possible that this proteoglycan excess may interfere with normal endometrial hemostasis in PCOS. PMID: 28789706
  3. The negative correlation between miR-200c and DCN (Decorin) was calculated in colorectal carcinoma, indicating that DCN could be a potential target of miR-200c. PMID: 28567416
  4. Genetic screening showed a deletion of chromosome 12q21.33-q22 containing the identified four small leucine-rich proteoglycans (SLRP's) associated with this particular dystrophy. PMID: 27096414
  5. Data suggest that PEG3 is required for TFEB induction and nuclear translocation in a VEGFR2- and AMPK-dependent manner for decorin/decorin receptor-evoked autophagy. (PEG3 = paternally expressed 3 protein; TFEB = transcription factor EB; VEGFR2 = vascular endothelial growth factor receptor-2; AMPK = AMP-activated protein kinase) PMID: 28798237
  6. Decorin exhibits promiscuity in its ability to alter tumorigenesis via regulation of angiogenesis, autophagy, and inflammation. (Review) PMID: 27860287
  7. Quantitative polymerase chain reaction for messenger RNA expression from tissue specimens revealed significantly higher expression of Biglycan (p = 0.0008) and Lumican (p = 0.01) and lower expression of Decorin (p < 0.0001) in urothelial carcinoma of bladder PMID: 28459201
  8. decorin can alter the bioactivity of TGF-beta2 on human myoblast migration PMID: 27644884
  9. A Finnish cohort of 336 subjects with diagnosed hypertension and 444 controls was analyzed. Samples were genotyped for decorin rs7308752 and rs516115 polymorphisms. The GG genotype of the decorin polymorphism rs7308752 (A>G) and the CC genotype of the rs516115 (T>C) are associated with decreased plasma resistin levels. These two decorin polymorphisms appear to have biological relevance in human vascular pathophysiology. PMID: 27315044
  10. analysis of decorin and lumican expression in fibroblasts correlated with palmoplantar collagen bundle size PMID: 26663310
  11. via gain-of-function analyses, DCN overexpression could inhibit renal cell carcinoma (RCC) cell proliferation and metastasis in vitro and vivo. At the mechanism level, we found that an ectopic expression of DCN significantly upregulated P21 and E-cadherin expression. Altogether, these results revealed that DCN is a tumor suppressor in RCC, and it could serve as a potential therapeutic target in patients with RCC. PMID: 26547587
  12. A synthetic peptide corresponding to this decorin region dose-dependently inhibited the response to myostatin in cardiomyocytes PMID: 27559042
  13. increased blood DCN levels could be a candidate biomarker for PE. PMID: 26554635
  14. An emerging concept that multiple proteases, especially those produced by inflammatory cells, are capable of cleaving DCN suggests that native DCN could be inactivated in a number of pathological inflammatory conditions PMID: 26697491
  15. Decorin plays a key role in the maintenance of the order in the normal corneal extracellular matrix. PMID: 26828927
  16. Compared with bone graft and marrow cavity contents, sticking scars had the highest expression of BMP-2 while bone grafts had the highest expression of DCN. PMID: 26400336
  17. Defective Proteolytic Processing of Fibrillar Procollagens and Prodecorin Due to Biallelic BMP1 Mutations Results in a Severe, Progressive Form of Osteogenesis Imperfecta. PMID: 25656619
  18. Data show that decorin is not only associated with angiogenesis, but it plays a causal role in this process. Also, depending on the molecular microenvironment where angiogenesis is induced, decorin can either promote or inhibit angiogenesis. [review] PMID: 25661523
  19. findings indicate that decorin may indirectly act as an antagonist to MM cell survival and that the interplay between MM and decorin may be an important target to explore in manipulating the tumor niche to inhibit tumorigenesis PMID: 25407518
  20. decorin expression and immunoreactivity in normal and malignant human colorectal tissue PMID: 26001829
  21. Our results reveal the molecular details of the periostin-decorin complex in both phyllodes tumor tissues and breast cancer cells; this interaction may represent a novel target for anti-cancer therapy PMID: 25400079
  22. A role for decorin and p-Smad-2 in the pathophysiology of fetal membranes and adverse pregnancy outcomes. PMID: 25232019
  23. decorin plays crucial roles in non-small-cell lung cancer against carcinogenesis and progression. PMID: 25524578
  24. The results suggest that regions within decorin is associated with ACL injury susceptibility and that genetic sequence variability within genes encoding proteoglycans may potentially modulate the ligament fibril properties. PMID: 24552666
  25. immunolocalization of decorin and biglycan in samples of first-trimester and term placentas, placenta accreta, invasive mole, and choriocarcinoma PMID: 24117774
  26. The targets of DCN include genes that play important roles in angiogenesis and cellular growth and may contribute to the pathogenesis of fetal growth restriction. PMID: 24947404
  27. DCN is a key regulator for chemoresistant mechanisms. PMID: 25550184
  28. Results demonstrate that DCN, a small leucine-rich proteoglycan, localizes to subregions of pathologically thickened arteries affected by CADASIL PMID: 25026535
  29. Lumican, decorin and dermatopontin are differentially expressed and may serve as biomarkers for metastatic and recurrent Giant cell tumor of bone PMID: 25304290
  30. Decorin differentially modulates the activity of insulin receptor isoform A ligands. PMID: 24389353
  31. AMPK is downstream of VEGFR2 and inhibition of AMPK signaling abrogated decorin-evoked autophagy. PMID: 24472739
  32. Decorin induced by dienogest appears to play a crucial role in suppressing endometriosis by exerting anti-proliferative effects and inducing cell cycle arrest. PMID: 25244916
  33. 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
  34. Periductal myxoid stroma and reduced periductal decorin expression seem to be prognostic for overall ipsilateral locoregional recurrence in ductal carcinoma in situ PMID: 23889174
  35. The results of our study showed that the presence of increased DCN levels in women with fetal growth restriction could contribute to pathogenesis of the disease. PMID: 24256371
  36. we identified the methylated +58CpG in DCN 5'-UTR associated with reduced expression of DCN mRNA, thereby downregulating E-cadherin in NSCLC cells with high metastatic potential. PMID: 24424784
  37. We present the clinical, histopathological, and molecular genetic assessment of a Chinese family with congenital stromal corneal dystrophy in which a novel DCN mutation was identified. PMID: 24413633
  38. human bladder cancer cells in vitro were negative for decorin expression. PMID: 24146840
  39. findings have shown that MMP-8 is able to modify the metastatic potential of breast cancer cells because of its ability to proteolytically cleave decorin and regulate miR-21 levels PMID: 23851508
  40. Overexpress decorin together with angiogenesis- and adhesion/migration-related genes, and that decorin overexpression in the human bladder carcinoma cell line TCCSUP is required for efficient invasiveness in vitro. PMID: 24142880
  41. decorin-mediated inhibition of cholangiocarcinoma cell growth, migration, and invasion and promotion of cell apoptosis might be through regulation of the expression of E-cadherin in vitro. PMID: 24272200
  42. Polymorphonuclear cell proteases, especially neutrophil elastase, degrade decorin, and this degradation renders collagen fibrils more susceptible to MMP-1 cleavage. PMID: 24023624
  43. Micro vessel density and VEGF-A expression were significantly associated with reduced decorin expression in tumor stroma suggesting, decorin as angiogenic modulator in oral squamous cell carcinomas. PMID: 24152495
  44. Both lumican and decorin are involved in collagen fibrillogenesis and stability. PMID: 23747391
  45. This age-dependent alteration of decorin GAG may contribute to skin fragility of elderly people. PMID: 23939413
  46. 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
  47. decorin induced VEGFR2-dependent mitochondrial fragmentation and loss of mitochondrial membrane potential PMID: 23798385
  48. The expression of collagen type IalphaI, collagen type III and decorin could be detected in tenocyte-like cell cultures using both enzymatic digestion and cell migration methodology. PMID: 22871215
  49. immunohistochemistry. Gene expression from mRNA extracted from cartilage showed high levels of decorin expression, likely associated with the large, complex tubular structures running through this cartilage type. PMID: 22490077
  50. The concentration of aggrecan, biglycan, and decorin was determined in six regions of the human supraspinatus tendon. PMID: 22329809

FAQs

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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