Recombinant Human Desmoglein-2 (DSG2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-07439P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Desmoglein-2 (DSG2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-07439P
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Product Overview

Description Recombinant Human Desmoglein-2 (DSG2) 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 Q14126
Target Symbol DSG2
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His
Target Protein Sequence AWITAPVALREGEDLSKKNPIAKIHSDLAEERGLKITYKYTGKGITEPPFGIFVFNKDTGELNVTSILDREETPFFLLTGYALDARGNNVEKPLELRIKVLDINDNEPVFTQDVFVGSVEELSAAHTLVMKINATDADEPNTLNSKISYRIVSLEPAYPPVFYLNKDTGEIYTTSVTLDREEHSSYTLTVEARDGNGEVTDKPVKQAQVQIRILDVNDNIPVVENKVLEGMVEENQVNVEVTRIKVFDADEIGSDNWLANFTFASGNEGGYFHIETDAQTNEGIVTLIKEVDYEEMKNLDFSVIVANKAAFHKSIRSKYKPTPIPIKVKVKNVKEGIHFKSSVISIYVSESMDRSSKGQIIGNFQAFDEDTGLPAHARYVKLEDRDNWISVDSVTSEIKLAKLPDFESRYVQNGTYTVKIVAISEDYPRKTITGTVLINVEDINDNCPTLIEPVQTICHDAEYVNVTAEDLDGHPNSGPFSFSVIDKPPGMAEKWKIARQESTSVLLQQSEKKLGRSEIQFLISDNQGFSCPEKQVLTLTVCECLHGSGCREAQHDSYVG
Expression Range 50-609aa
Protein Length partial
Mol. Weight 68.4 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 Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.
Subcellular Location Cell membrane; Single-pass type I membrane protein. Cell junction, desmosome.
Database References
Associated Diseases Arrhythmogenic right ventricular dysplasia, familial, 10 (ARVD10); Cardiomyopathy, dilated 1BB (CMD1BB)
Tissue Specificity All of the tissues tested and carcinomas.

Gene Functions References

  1. A homozygous mutation of DSG2 p.F531C was identified as the pathogenic mutation in patients with arrhythmogenic right ventricular cardiomyopathy/dysplasia (ARVC/D) involving both ventricles, as a result of widened and impaired intercalated discs, interrupted myocardial fibers, and abnormally hyperplastic interstitial fibers, collagen fibers, and adipocytes. PMID: 28578331
  2. DSG2 as a key regulator of vasculogenic mimicry (VM) activity in human melanoma and suggest this molecule might be therapeutically targeted to reduce tumor blood supply and metastatic spread. PMID: 27340778
  3. Data suggest that Dsg2 stimulates cell growth and migration by positively regulating EGFR level and signaling through a c-Src and Cav1-dependent mechanism using lipid rafts as signal modulatory platforms. PMID: 26918609
  4. identified DSG2 expression in distinct progenitor cell subpopulations and show that, independent from its classical function as a component of desmosomes, this cadherin also plays a critical role in the vasculature PMID: 27338829
  5. Expression of the desmosomal protein Desmoglein-2 was reduced in pediatric dilated cardiomyopathy pediatric patients. PMID: 28764973
  6. This study defines a mechanism by which Dsg2 expression in cancer cells can modulate the tumor microenvironment, a step critical for tumor progression. PMID: 28438789
  7. Silencing of Dsg2 but not Dsc2 resulted in loss of cell cohesion and enhanced migration, and invasion of pancreatic adenocarcinoma cells. PMID: 28277619
  8. The homozygous desmoglein 2 variant c.1003A;G co-segregated with Arrhythmogenic right ventricular cardiomyopathy, indicating autosomal recessive inheritance and complete penetrance. PMID: 28818065
  9. these data suggest that palmitoylation of Dsg2 regulates protein transport to the plasma membrane. Modulation of the palmitoylation status of desmosomal cadherins can affect desmosome dynamics. PMID: 27703000
  10. Both Dsg2 mRNA and protein were highly expressed in non-small cell lung cancer (NSCLC) tissues and associated with NSCLC size, but not with overall survival of patients. PMID: 27629878
  11. Currently, 13 genes have been associated with the disease but nearly 40 % of clinically diagnosed cases remain without a genetic diagnosis. PMID: 25398255
  12. DSG2 and DSG3 might be potential diagnostic markers for squamous cell carcinoma of the lung. PMID: 25468811
  13. In endometrial luminal epithelium, cadherin 6, desmoglein 2 and plexin b2 were surprisingly found in the apical as well as the lateral membrane domain; their knock-down compromised epithelial integrity. PMID: 25237006
  14. a low DSG2 expression phenotype is a useful prognostic biomarker of tumor aggressiveness and may serve as an aid in identifying patients with clinically significant prostate cancer. PMID: 24896103
  15. Six variants of uncertain clinical significance in the PKP2, JUP, and DSG2 genes showed a deleterious effect on mRNA splicing, indicating these are ARVD/C-related pathogenic splice site mutations. PMID: 25087486
  16. This structure reveals that the ectodomain of Dsg2 is flexible even in the calcium-bound state and, on average, is shorter than the type 1 cadherin crystal structures. PMID: 25855637
  17. Desmoglein 2 expression attenuates migration of melanoma cells, mediated by downregulation of secretogranin II. PMID: 24558503
  18. Gal3 has a role in stabilizing desmoglein-2, a desmosomal cadherin, and intercellular adhesion in intestinal epithelial cells PMID: 24567334
  19. Desmoglein-2 co-localizes with integrin-beta8 in N-MVECs. PMID: 23874518
  20. Authors found a number of mutations within or near the EF loop of the Ad3 fiber knob that resulted in affinities to DSG2 that were several orders of magnitude higher than those to the wild-type Ad3 knob. PMID: 23946456
  21. findings were consistent with the results obtained by immunohistochemistry of endomyocardial biopsies and epidermal tissue of mutation carriers, which indicated a normal cellular distribution of DSG2 PMID: 23381804
  22. Snail regulates levels of E-cadherin and desmoglein 2 in oral squamous cell carcinoma cells both transcriptionally and post-translationally. PMID: 23261431
  23. CD133 interacts with plakoglobin and knockdown of CD133 by RNA interference (RNAi) results in the downregulation of desmoglein-2. PMID: 23326490
  24. Specific desmosomal cadherins contribute differently to keratinocyte cohesion and that Dsg2 compared to Dsg3 is less important in this context. PMID: 23326495
  25. an impaired prodomain cleavage and an influence on the DSG2-properties could be demonstrated for the R46Q-variant leading to the classification of the variant as a potential gain-of-function mutant in arrhythmogenic right ventricular cardiomyopathy PMID: 23071725
  26. The Dsg unique region(DUR) of Dsg2 stabilized Dsg2 at the cell surface by inhibiting its internalization and promoted strong intercellular adhesion. PMID: 23128240
  27. Gastroesophageal reflux disease was specifically associated with elevated transcript levels of desmoglein 2 and plakoglobin PMID: 22521077
  28. Dsg-2 with a mutation at the predicted cleavage site is resistant to cleavage by matriptase. Thus Dsg-2 seems to be a functionally relevant physiological substrate of matriptase. PMID: 22783993
  29. Desmoglein 2, expressed earliest among the four isoforms in development, was found to be mutated in arrythmogenic right ventricular cardiomyopathy and is a receptor for a subset of adenoviruses that cause respiratory and urinary tract infections. PMID: 22189787
  30. The Dsg2 exhibit microtubule-dependent transport in epithelial cells but use distinct motors to traffic to the plasma membrane. PMID: 22184201
  31. We detected a novel mutation: DSG2 3059_3062delAGAG and it may induce disintegrationofthe desmosomal structure PMID: 21397041
  32. Dsg2 extracellular and intracellular domains are cleaved by proteolytic enzymes, and multiple cleavage fragments of Dsg2 are generated in colonic epithelial cells. PMID: 21715983
  33. Study demonstrated a molecular switching in gene expression within the desmoglein subfamily between DSG3 and DSG2 during oral cancer progression. PMID: 20923451
  34. Co-segregation of the G812S mutation with disease expression was established in a large Caucasian family.No differences in targeting or stability of the mutant proteins, suggesting that they act via a dominant negative mechanism PMID: 20708101
  35. Dsg2-mediated adhesion affects tight junction integrity and is required to maintain intestinal epithelial barrier properties PMID: 20224006
  36. Desmoglein 2 was highly expressed by the least differentiated cells of the cutaneous epithelium, including the hair follicle bulge of the fetus and adult, bulb matrix cells, and basal layer of the outer root sheath. PMID: 12787134
  37. Nine heterozygous DSG2 mutations (5 missense, 2 insertion-deletions, 1 nonsense, and 1 splice site mutation) were detected in subjects with ARVC. PMID: 16505173
  38. mutations in DSG2 contribute to the development ofarrhythmogenic right ventricular dysplasia/cardiomyopathy PMID: 16773573
  39. Data demonstrate that UV-induced desmoglein-2 down-regulation is mediated via reactive oxygen species which are generated through EGF receptor activation and Rac2/NADPH oxidase activation. PMID: 16820949
  40. Mutations in DSG2 display a high degree of penetrance. Disease expression was of variable severity with left ventricular involvement a prominent feature. PMID: 17105751
  41. long term treatment with epidermal growth factor (EGF) leads to a marked increase in the levels of ADAM17, which also increases the shedding of several substrates of ADAM17, including the desmosomal cadherin Dsg-2 PMID: 17227756
  42. desmoglein 2 is a novel solitary surface glycoprotein in malignant melanoma cells PMID: 17495963
  43. Dsg2 was targeted by caspases in cell lines undergoing staurosporine-induced apoptosis. The proteolytic processing of full-length Dsg2 released a 70-kDa fragment into the cytosol. PMID: 17559062
  44. Dsg2 regulates intestinal epithelial cell apoptosis driven by cysteine proteases during physiological differentiation and inflammation PMID: 17804817
  45. DSG2-V55M polymorphism is identified as a novel risk variant for dilated cardiomyopathy. PMID: 18678517
  46. Monoclonal antibodies against the proregion of the desmosomal cadherin, human desmoglein-2. PMID: 18707543
  47. Desmoglein 2 has been demonstrated in a sizable subset of nevi and primary melanomas. PMID: 18975006
  48. Results show that epidermal growth factor receptor inhibition stabilizes desmoglein 2 at intercellular junctions by interfering with its accumulation in an internalized cytoplasmic pool. PMID: 18987342
  49. levels of Dsg1 & Dsg2 are reduced in pancreatic tumors; expression of kallikrein 7 in BxPC-3 cells resulted in increase in shedding of soluble Dsg2 PMID: 19091121
  50. While Dsg2 expression was consistently strong in BCC, it varied in SCC with a minor correlation between a decrease of Dsg2 expression and tumor differentiation PMID: 19458482

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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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