Recombinant Mouse Decorin (DCN) Protein (His)

Name: Recombinant Mouse Decorin (DCN) Protein (His)
Brand: Beta LifeScience
SKU: BLC-02095P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Decorin (DCN) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P28654
Target Symbol	DCN
Synonyms	Dcn; Decorin; Bone proteoglycan II; PG-S2; PG40
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	GIIPYDPDNPLISMCPYRCQCHLRVVQCSDLGLDKVPWDFPPDTTLLDLQNNKITEIKEGAFKNLKDLHTLILVNNKISKISPEAFKPLVKLERLYLSKNQLKELPEKMPRTLQELRVHENEITKLRKSDFNGLNNVLVIELGGNPLKNSGIENGAFQGLKSLSYIRISDTNITAIPQGLPTSLTEVHLDGNKITKVDAPSLKGLINLSKLGLSFNSITVMENGSLANVPHLRELHLDNNKLLRVPAGLAQHKYIQVVYLHNNNISAVGQNDFCRAGHPSRKASYSAVSLYGNPVRYWEIFPNTFRCVYVRSAIQLGNYK
Expression Range	35-354aa
Protein Length	Partial
Mol. Weight	39.9 kDa
Research Area	Others
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	KEGG: mmu:13179 STRING: 10090.ENSMUSP00000100924 UniGene: PMID: 28412940 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 The disruption of decorin-restricted TGFbeta signalling leads to higher stiffness of articular cartilage matrix, rendering joints more resistant to osteoarthritis. PMID: 27377816 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 A synthetic peptide corresponding to this decorin region dose-dependently inhibited the response to myostatin in cardiomyocytes PMID: 27559042 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 Decorin is an autophagy-inducible proteoglycan and is required for proper in vivo autophagy. PMID: 26344480 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 Development of congenital stromal dystrophy is dependent on export and extracellular deposition of truncated decorin. PMID: 26029887 decorin may modulate follicular cycling and morphogenesis PMID: 24816226 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 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 A decorin-deficient matrix affects skin chondroitin/dermatan sulfate levels and keratinocyte function. PMID: 24447999 Decorin deficiency promotes hepatic carcinogenesis. PMID: 24361483 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 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 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 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 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 decorin induced VEGFR2-dependent mitochondrial fragmentation and loss of mitochondrial membrane potential PMID: 23798385 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 Lack of decorin leads to enhanced tumor formation in the liver. PMID: 23448253 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 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 Decorin protein core affects the global gene expression profile of the tumor microenvironment in a triple-negative orthotopic breast carcinoma xenograft model. PMID: 23029096 decorin plays a role in tendon viscoelasticity that cannot be completely explained by its role in collagen fibrillogenesis PMID: 22482685 The expression of decorin, a naturally occurring TGF-beta suppressor, was elevated in Mstn-null mice. PMID: 22277753 Decorin regions LRR6 and LRR5 participate in the interaction with LRP-1 and TGF-beta as well as in its dependent signaling. PMID: 22203668 Wild type N-ras appears to mediate its anti-malignant effect by downregulating decorin expression. PMID: 21809347 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 Cleavage product of decorin serves as a functional receptor of resistin in adipocyte progenitors and may regulate white adipose tissue expansion. PMID: 21683670 gradual increase in muscle regeneration PMID: 21416223 these results implicated a role for decorin in mediating delayed-type hypersensitivity responses by influencing polymorphonuclear leukocyte attachment to the endothelium. PMID: 22043007 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 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 CTGF specifically induced the synthesis of decorin, suggesting a mechanism of autoregulation. PMID: 21454550 Decorin can modify collagen I-stimulated, but not fibronectin-stimulated myoblast migration in vitro. PMID: 21059388 decorin is a protective agent during the development of diabetic nephropathy PMID: 20083846 Dcn has been identified as an imprinted gene by high-throughput screening using RIKEN cDNA microarray. PMID: 11820791 decorin is dramatically induced in the desmin-null myocardium PMID: 11891192 decorin exerts beneficial effects on tubulointerstitial fibrosis PMID: 11891213 decorin binds fibrinogen in a Zn2+-dependent interaction PMID: 12582160 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 Inhibition of myoblast migration via decorin expression is critical for normal skeletal muscle differentiation. PMID: 12871697 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 in DCN-deficient mice, the growth of corneal vessels was significantly diminished PMID: 15528932 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 decorin is not required for cell survival PMID: 15949467 decorin is required for the proper fibrotic evolution of myocardial infarctions PMID: 15949932 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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