Recombinant Human Decorin (DCN) Protein (His)

Beta LifeScience SKU/CAT #: BLC-05284P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Decorin (DCN) Protein (His)

Beta LifeScience SKU/CAT #: BLC-05284P
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Product Overview

Description Recombinant Human Decorin (DCN) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P07585
Target Symbol DCN
Synonyms Bone proteoglycan II; CSCD; DCN; DCN protein; Decorin; Decorin proteoglycan; Dermatan sulphate proteoglycans II ; DKFZp686J19238; DSPG 2; DSPG2; PG 40; PG II; PG S2; PG-S2; PG40; PGII ; PGS 2; PGS2; PGS2_HUMAN; Proteoglycan core protein ; SLRR1B; Small leucine rich protein 1B
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His
Target Protein Sequence QQRGLFDFMLEDEASGIGPEVPDDRDFEPSLGPVCPFRCQCHLRVVQCSDLGLDKVPKDLPPDTTLLDLQNNKITEIKDGDFKNLKNLHALILVNNKISKVSPGAFTPLVKLERLYLSKNQLKELPEKMPKTLQELRAHENEITKVRKVTFNGLNQMIVIELGTNPLKSSGIENGAFQGMKKLSYIRIADTNITSIPQGLPPSLTELHLDGNKISRVDAASLKGLNNLAKLGLSFNSISAVDNGSLANTPHLRELHLDNNKLTRVPGGLAEHKYIQVVYLHNNNISVVGSSDFCPPGHNTKKASYSGVSLFSNPVQYWEIQPSTFRCVYVRSAIQLGNYK
Expression Range 20-359aa
Protein Length Partial
Mol. Weight 41.7kDa
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 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

HGNC: 2705

OMIM: 125255

KEGG: hsa:1634

STRING: 9606.ENSP00000052754

UniGene: PMID: 28631095

  • 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
  • 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
  • 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
  • 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
  • Decorin exhibits promiscuity in its ability to alter tumorigenesis via regulation of angiogenesis, autophagy, and inflammation. (Review) PMID: 27860287
  • 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
  • decorin can alter the bioactivity of TGF-beta2 on human myoblast migration PMID: 27644884
  • 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
  • analysis of decorin and lumican expression in fibroblasts correlated with palmoplantar collagen bundle size PMID: 26663310
  • 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
  • A synthetic peptide corresponding to this decorin region dose-dependently inhibited the response to myostatin in cardiomyocytes PMID: 27559042
  • increased blood DCN levels could be a candidate biomarker for PE. PMID: 26554635
  • 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
  • Decorin plays a key role in the maintenance of the order in the normal corneal extracellular matrix. PMID: 26828927
  • 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
  • Defective Proteolytic Processing of Fibrillar Procollagens and Prodecorin Due to Biallelic BMP1 Mutations Results in a Severe, Progressive Form of Osteogenesis Imperfecta. PMID: 25656619
  • 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
  • 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
  • decorin expression and immunoreactivity in normal and malignant human colorectal tissue PMID: 26001829
  • 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
  • A role for decorin and p-Smad-2 in the pathophysiology of fetal membranes and adverse pregnancy outcomes. PMID: 25232019
  • decorin plays crucial roles in non-small-cell lung cancer against carcinogenesis and progression. PMID: 25524578
  • 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
  • immunolocalization of decorin and biglycan in samples of first-trimester and term placentas, placenta accreta, invasive mole, and choriocarcinoma PMID: 24117774
  • 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
  • DCN is a key regulator for chemoresistant mechanisms. PMID: 25550184
  • Results demonstrate that DCN, a small leucine-rich proteoglycan, localizes to subregions of pathologically thickened arteries affected by CADASIL PMID: 25026535
  • Lumican, decorin and dermatopontin are differentially expressed and may serve as biomarkers for metastatic and recurrent Giant cell tumor of bone PMID: 25304290
  • Decorin differentially modulates the activity of insulin receptor isoform A ligands. PMID: 24389353
  • AMPK is downstream of VEGFR2 and inhibition of AMPK signaling abrogated decorin-evoked autophagy. PMID: 24472739
  • 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
  • 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
  • Periductal myxoid stroma and reduced periductal decorin expression seem to be prognostic for overall ipsilateral locoregional recurrence in ductal carcinoma in situ PMID: 23889174
  • 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
  • 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
  • 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
  • human bladder cancer cells in vitro were negative for decorin expression. PMID: 24146840
  • 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
  • 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
  • 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
  • Polymorphonuclear cell proteases, especially neutrophil elastase, degrade decorin, and this degradation renders collagen fibrils more susceptible to MMP-1 cleavage. PMID: 24023624
  • 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
  • Both lumican and decorin are involved in collagen fibrillogenesis and stability. PMID: 23747391
  • This age-dependent alteration of decorin GAG may contribute to skin fragility of elderly people. PMID: 23939413
  • 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
  • decorin induced VEGFR2-dependent mitochondrial fragmentation and loss of mitochondrial membrane potential PMID: 23798385
  • 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
  • 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
  • The concentration of aggrecan, biglycan, and decorin was determined in six regions of the human supraspinatus tendon. PMID: 22329809

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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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