Recombinant Human Dermcidin (DCD) Protein (His-B2M)

Beta LifeScience SKU/CAT #: BLC-02179P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Dermcidin (DCD) Protein (His-B2M)

Beta LifeScience SKU/CAT #: BLC-02179P
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Product Overview

Description Recombinant Human Dermcidin (DCD) Protein (His-B2M) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% 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-6His-B2M
Target Protein Sequence YDPEAASAPGSGNPCHEASAAQKENAGEDPGLARQAPKPRKQRSSLLEKGLDGAKKAVGGLGKLG kDaVEDLESVGKGAVHDVKDVLDSVL
Expression Range 20-110aa
Protein Length Full Length of Mature Protein
Mol. Weight 23.3 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 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
Tissue Specificity Specifically and constitutively expressed in eccrine sweat gland cells. Secreted into the sweat at a concentration of 1-10 micrograms/ml.

Gene Functions References

  1. the present study suggests that dermcidin is a novel binding protein of lncRNA STCAT3, which serves an important role in the progress and clinical outcome of gastric cancer PMID: 30226544
  2. 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
  3. this study shows that PIF regulates systemic immunity and targets protective regulatory and cytoskeleton proteins PMID: 26944449
  4. 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
  5. 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
  6. 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
  7. These findings imply that DCD promotes breast tumorigenesis via modulation of ERBB signaling pathways PMID: 25879571
  8. Dermcidin binds platelets and may inhibit the therapeutic action of aspirin following acute myocardial infarction. PMID: 25055737
  9. Data indicate that Y-P30/dermcidin expressed in placentas of first trimester pregnancies. PMID: 24969620
  10. Increased Dermcidin was also detected with immunoblotting. PMID: 24562771
  11. Crystal structure and functional mechanism of a human antimicrobial membrane channel PMID: 23426625
  12. major binding partners of LEKTI were found to be the antimicrobial peptide dermcidin and the serine protease cathepsin G and no kallikreins. PMID: 22588119
  13. Structure-activity analysis of the dermcidin-derived peptide DCD-1L, an anionic antimicrobial peptide present in human sweat. PMID: 22262861
  14. revealed that Nck1 SH2 domain binds to the phosphotyrosine residue at position 20 (Y20) of the DCD PMID: 21397687
  15. 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
  16. There was a significant correlation between weight loss and survival in the PIF-positive non-small-cell lung cancer patients. PMID: 20837461
  17. 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
  18. identified as antibiotic peptide secreted by sweat glands PMID: 11694882
  19. 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
  20. 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
  21. NF-kappaB and STAT3 are activated by proteolysis inducing factor in human Kupffer cells and monocytes PMID: 16142329
  22. 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
  23. 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
  24. 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
  25. Dermcidin is a proliferation and survival factor in prostate cancer cells subjected to stressors found in the prostate cancer microenvironment. PMID: 17626247
  26. These data suggest that the disorder and order transition may be relevant for some biological functions of PIF/DCD. PMID: 18058718
  27. There is a growing body of evidence illustrating dermcidin as an oncogene and its Y-P30 subunite as a survival factor (Review) PMID: 18403914
  28. 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
  29. pleiotrophin (PTN) and syndecan-2 and -3 as direct binding partners of Y-P30. PMID: 18599487
  30. 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.

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