Recombinant Human Dermcidin (DCD) Protein (GST)

Name: Recombinant Human Dermcidin (DCD) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-03686P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Dermcidin (DCD) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P81605
Target Symbol	DCD
Synonyms	AIDD ; DCD 1; dcd; DCD-1; DCD_HUMAN; Dermcidin; DSEP; HCAP; PIF; Preproteolysin
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	YDPEAASAPGSGNPCHEASAAQKENAGEDPGLARQAPKPRKQRSSLLEKGLDGAKKAVGGLGKLGKDAVEDLESVGKGAVHDVKDVLDSVL
Expression Range	20-110aa
Protein Length	Full Length of Mature Protein
Mol. Weight	36.3kDa
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	DCD-1 displays antimicrobial activity thereby limiting skin infection by potential pathogens in the first few hours after bacterial colonization. Highly effective against E.coli, E.faecalis, S.aureus and C.albicans. Optimal pH and salt concentration resemble the conditions in sweat. Also exhibits proteolytic activity, cleaving on the C-terminal side of Arg and, to a lesser extent, Lys residues.; Survival-promoting peptide promotes survival of neurons and displays phosphatase activity. It may bind IgG.
Subcellular Location	Secreted.
Database References	HGNC: 14669 OMIM: 606634 KEGG: hsa:117159 UniGene: PMID: 30226544 The results of this study suggest that these biomarker DCD can serve as a potential non-invasive early diagnosis platform reflecting PiB-PET imaging for Mild Cognitive Impairment and Alzheimer's Disease. PMID: 27392853 this study shows that PIF regulates systemic immunity and targets protective regulatory and cytoskeleton proteins PMID: 26944449 This is the first report of the presence of DCD in nasal mucosa and demonstration of DCD in clinical samples of human nasal secretions at clinically relevant concentrations, which may represent a novel arm of sinonasal airway innate defense. PMID: 27650261 Identification of dermcidin in human sebaceous gland cells supports the concept that sebocytes play an important role in the innate immunity of the skin through the expression of antimicrobial peptides and specific lipids. PMID: 26718508 Reduced DCD concentration in sweat in patients with inflammatory acne may permit proliferation of P. acnes in pilosebaceous units, resulting in progression of inflammatory acne. PMID: 25673161 These findings imply that DCD promotes breast tumorigenesis via modulation of ERBB signaling pathways PMID: 25879571 Dermcidin binds platelets and may inhibit the therapeutic action of aspirin following acute myocardial infarction. PMID: 25055737 Data indicate that Y-P30/dermcidin expressed in placentas of first trimester pregnancies. PMID: 24969620 Increased Dermcidin was also detected with immunoblotting. PMID: 24562771 Crystal structure and functional mechanism of a human antimicrobial membrane channel PMID: 23426625 major binding partners of LEKTI were found to be the antimicrobial peptide dermcidin and the serine protease cathepsin G and no kallikreins. PMID: 22588119 Structure-activity analysis of the dermcidin-derived peptide DCD-1L, an anionic antimicrobial peptide present in human sweat. PMID: 22262861 revealed that Nck1 SH2 domain binds to the phosphotyrosine residue at position 20 (Y20) of the DCD PMID: 21397687 dermcidin was a novel platelet aggregating agent, and potentiated the ADP induced thrombosis in the animal model as well as acutely inhibited glucose induced insulin synthesis. PMID: 20809104 There was a significant correlation between weight loss and survival in the PIF-positive non-small-cell lung cancer patients. PMID: 20837461 Data show that dermcidin adopts a flexible amphipathic alpha-helical structure with a helix-hinge-helix motif, which is a common molecular fold among antimicrobial peptides. PMID: 20510021 identified as antibiotic peptide secreted by sweat glands PMID: 11694882 Our results confirmed previous findings indicating that dermcidin-1L could have promising therapeutic potentials and shed new light on the structure-function relationship of dermcidin-1L. PMID: 15670776 Reduced expression of dermcidin in sweat of patients with atopic dermatitis may contribute to the high susceptibility of these patients to skin infections and altered skin colonization with Staphylococcus aureus. PMID: 15944307 NF-kappaB and STAT3 are activated by proteolysis inducing factor in human Kupffer cells and monocytes PMID: 16142329 Functional analysis indicated that proteolytic processing of DCD-1L by Cathepsin D in human sweat modulates the innate immune defense of human skin. PMID: 16354654 Dermcidin may function as an oncogene in hepatic as well as breast cells; Glycosylation is not required, but the importance of asparagine residues suggests a role for the proteolysis-inducing factor core peptide domain. PMID: 16685272 This work suggests that DCD might participate in the regulation of placental function by means of modulating the proteolytic cascades on the trophoblastic cell surface. PMID: 17448443 Dermcidin is a proliferation and survival factor in prostate cancer cells subjected to stressors found in the prostate cancer microenvironment. PMID: 17626247 These data suggest that the disorder and order transition may be relevant for some biological functions of PIF/DCD. PMID: 18058718 There is a growing body of evidence illustrating dermcidin as an oncogene and its Y-P30 subunite as a survival factor (Review) PMID: 18403914 Expression of dermcidin in human primary tumours appears highly variable and is not induced substantially by hypoxia/oxidative stress in cell line model systems PMID: 18594538 pleiotrophin (PTN) and syndecan-2 and -3 as direct binding partners of Y-P30. PMID: 18599487 IRAK-4, which is essential for virtually all TLR signalling, was suppressed, whereas the precursor for the antibiotic peptide Dermcidin was up-regulated in HIV-infected cells. PMID: 19703016

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.