Recombinant Human Matrix Metalloproteinase-20 (MMP20) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-05269P
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) MMP20.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) MMP20.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) MMP20.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) MMP20.

Recombinant Human Matrix Metalloproteinase-20 (MMP20) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-05269P
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Product Overview

Description Recombinant Human Matrix Metalloproteinase-20 (MMP20) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb O60882
Target Symbol MMP20
Synonyms AI2A2; Enamel metalloproteinase; Enamelysin; Matrix metalloproteinase 20; Matrix metalloproteinase-20; MMP 20; MMP-20; MMP20; MMP20_HUMAN
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His&C-Myc
Target Protein Sequence YRLFPGEPKWKKNTLTYRISKYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRINSGEADIMISFENGDHGDSYPFDGPRGTLAHAFAPGEGLGGDTHFDNAEKWTMGTNGFNLFTVAAHEFGHALGLAHSTDPSALMYPTYKYKNPYGFHLPKDDVKGIQALYGPRKVFLGKPTLPHAPHHKPSIPDLCDSSSSFDAVTMLGKELLLFKDRIFWRRQVHLRTGIRPSTITSSFPQLMSNVDAAYEVAERGTAYFFKGPHYWITRGFQMQGPPRTIYDFGFPRHVQQIDAAVYLREPQKTLFFVGDEYYSYDERKRKMEKDYPKNTEEEFSGVNGQIDAAVELNGYIYFFSGPKTYKYDTEKEDVVSVVKSSSWIGC
Expression Range 108-483aa
Protein Length Full Length of Mature Protein
Mol. Weight 47.6 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 Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation. Cleaves aggrecan at the '360-Asn-|-Phe-361' site.
Subcellular Location Secreted, extracellular space, extracellular matrix.
Protein Families Peptidase M10A family
Database References
Associated Diseases Amelogenesis imperfecta, hypomaturation type, 2A2 (AI2A2)
Tissue Specificity Expressed specifically in the enamel organ.

Gene Functions References

  1. The levels of MMP20 silencing-induced downregulation differed amongst CSC markers, with ABCG2 and CD44 showing more pronounced downregulations. PMID: 30002682
  2. common variants at 11q22.2 within MMP20 associate with neuroblastoma cases harboring 11q deletion (rs10895322) PMID: 28924153
  3. The article data showed that MMP20 rs1784418 C>T (Matrix metalloproteinase 20) appears to protect against dental caries, but its effects are likely to be more marked in certain populations. PMID: 27992873
  4. DSPP-MMP20 pair may play a role in the normal turnover of cell surface proteins and/or repair of pericellular matrix proteins of the basement membranes in the metabolically active duct epithelial system of the nephrons. PMID: 27666430
  5. Levels of matrix metalloproteinases MMP-19 and MMP-20 expression are significantly increased in pancreatic ductal adenocarcinoma (PDAC). PMID: 26692439
  6. The expression of MMP20 was lower in calcifying cystic odontogenic tumor when compared to all tumors and cysts. PMID: 26558991
  7. The growth of choroidal neovascularization in AMD would be affected by 2 genes: MMP20, a newly confirmed gene expressed in the retina, and ARMS2/HTRA1, a well-known susceptibility gene for AMD. PMID: 26337002
  8. Novel homozygous mutation MMP20 (c.1054G>A, p.Glu352Lys) genes were identified in amelogenesis imperfect consanguinity. Mutant MMP20 was expressed at a normal level but secreted only minimally with proteolytic function. PMID: 26124219
  9. expression of MMP-20 and co-expression and potential interaction with DSPP in human major salivary gland tissues PMID: 25805840
  10. The results identify MMP-20 as a broad activator of pro-KLKs, suggesting the potential for intersection of the KLK and MMP axes under pathological dysregulation of MMP-20 expression. PMID: 23241590
  11. Polymorphisms of MMP7 and MMP20 genes may be surrogate markers to predict long-term outcomes after kidney transplantation. PMID: 23953525
  12. mineralized content slightly decreased; magnesium substituting for calcium in crystal. anomalies affected enamel with minimal interrod enamel; apatite crystals perpendicular to enamel prisms, suggesting possible new role for MMP20 in enamel formation. PMID: 23625376
  13. amelogenesis imperfecta-causing mutations were identified in three of the probands: 2)a novel missense transition mutation in both MMP20 alleles (g.15390A>G; c.611A>G; p.His204Arg) that substituted arginine for histidine. PMID: 23355523
  14. Variation in MMP20 may be associated with caries experience mainly in Caucasian subjects with poor oral health habits. PMID: 22330321
  15. hypocalcified amelogenesis imperfecta, Witkop type III, was unrelated to previously described mutations in the ENAM or MMP-20 genes PMID: 21504268
  16. MMP-20 is overexpresssed in LSCC compared with the adjacent normal laryngeal epithelium. PMID: 21466263
  17. Associations between tooth agenesis and MMP1 (p=0.007), and MMP20 (p=0.03) were found in Brazilian families. MMP20 continued to be associated with tooth agenesis (p=0.01). Mmp20 was not expressed during the initial stages of tooth development. PMID: 21144496
  18. Enamelysin and collagen XVIII were co-localized in the developing enamel matrix and stratum intermedium and in the enamel-like tumor matrix of odontogenic tumors. PMID: 15296943
  19. A mutation in the MMP-20 gene has been identified and associated with amelogenesis imperfecta. PMID: 15744043
  20. c-Jun is a key regulatory element for MMP-20 expression PMID: 17611094
  21. Binding of the P41T mutant amelogenin for matrix metalloproteinase 20 was significantly lower than that of wild-type amelogenin. PMID: 18434575
  22. A total of 463 individuals from 54 families were evaluated and mutations in the AMEL, ENAM and KLK4 genes were identified. PMID: 18714142
  23. were able to find SNPs in the matrix metallopeptidase gene MMP20(GeneID 9313) that are significantly associated with kidney aging. PMID: 19834535
  24. In a family with a hypomaturation-type enamel defect, mutational and haplotype analyses revealed an amelogenesis imperfecta-causing point mutation in exon 6 of MMP20 that results in a single amino acid substitution in the hemopexin domain. PMID: 19966041

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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