Recombinant Human Amelogenin, X Isoform (AMELX) Protein (His&Myc)

Name: Recombinant Human Amelogenin, X Isoform (AMELX) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-01388P
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 Human Amelogenin, X Isoform (AMELX) Protein (His&Myc) is produced by our Baculovirus expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q99217
Target Symbol	AMELX
Species	Homo sapiens (Human)
Expression System	Baculovirus
Tag	N-10His&C-Myc
Target Protein Sequence	MPLPPHPGHPGYINFSYEVLTPLKWYQSIRPPYPSYGYEPMGGWLHHQIIPVLSQQHPPTHTLQPHHHIPVVPAQQPVIPQQPMMPVPGQHSMTPIQHHQPNLPPPAQQPYQPQPVQPQPHQPMQPQPPVHPMQPLPPQPPLPPMFPMQPLPPMLPDLTLEAWPSTDKTKREEVD
Expression Range	17-191aa
Protein Length	Full Length of Mature Protein
Mol. Weight	23.8 kDa
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	Plays a role in biomineralization. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel.
Subcellular Location	Secreted, extracellular space, extracellular matrix.
Protein Families	Amelogenin family
Database References	HGNC: 461 OMIM: 300391 KEGG: hsa:265 UniGene: PMID: 29802703 To the best of our knowledge, this is the first report of expression of human amelogenin in plants, offering the possibility to use this plant-made protein for nanotechnological applications. PMID: 28801830 a single-nucleotide polymorphism in the amelogenin gene using amplified product-length polymorphisms in combination with sex-determining region Y analysis, is reported. PMID: 28052096 Full-length amelogenin may have a negative mitogenic impact on human dental pulp stem cells. PMID: 26762641 suggestive overrepresentation of TT genotype of amelogenin marker in cases w/severe erosion when compared to no dentine erosion. Amelogenin also associated with severe erosion in recessive model; TT genotype significantly more frequent in affected group PMID: 25791822 Studies indicate that a single point mutation (41Pro-->Thr) in the amelogenin gene causes severe dental enamel malformation known as amelogenesis imperfect. PMID: 26545753 sequencing data showed presence of mutation. Samples showing mutation (43.3%) showed high correlation with caries (80.7%) experience which was statistically significant. PMID: 26551370 silent mutation in exon 4 of AMELX gene. generating and characterizing transgenic animal model, alteration of the ratio and quantity of the developmentally conserved alternative splicing repertoire of AMELX caused defects in enamel matrix mineralization. PMID: 25117480 Conversion to amelogenin expressing dental epithelial cells involved an up-regulation of the stem cell marker Sox2 and proliferation genes and decreased expression of mesenchymal markers PMID: 25122764 the interaction of amelogenin with Grp78/Bip contributed to cell proliferation, rather than correlate with the osteogenic differentiation PMID: 24167599 demonstrate the presence of copy number variations in regions containing 9 of the 13 CODIS(Combined DNA Index System) short tandem repeat(STR) and AMELX/Y loci PMID: 23948316 Associations between TFIP11 (p=0.02), ENAM (p=0.00001), and AMELX (p=0.01) could be seen with caries independent of having MIH or genomic DNA copies of Streptococcus mutans detected by real time PCR in the Brazilian sample. PMID: 23790503 The 21 non-CODIS STR loci of the Russian ethnic minority group were characterized by high genetic diversity and therefore may be useful for elucidating the population's genetic background, for individual identification. PMID: 23733431 Deletion of AMELX results in males with a characteristic snow-capped enamel phenotype. PMID: 23251683 Evolutionary and statistical analyses showed that none of the SNPs identified in this study were associated with caries susceptibility, suggesting that AMELX is not a gene candidate in our studied population. PMID: 23525533 These results suggest that SNPs of AMELX might be associated with dental caries susceptibility in Korean population. PMID: 21114591 A single Pro-70 to Thr (p.P70T) mutation of amelogenin affected the self-assembly and adsorption behaviour of amelogenin, resulting in increased binding to apatite and inhibited crystal growth. PMID: 21081224 These results suggest that hAm may be a key element in regulating hBMSCs osteogenic differentiation. PMID: 21514271 Perturbed amelogenin secondary structure leads to uncontrolled aggregation in amelogenesis imperfecta mutant proteins. PMID: 20929860 amelogenin may stimulate wound healing by providing connective tissue cells with a temporary extracellular matrix PMID: 20012165 frameshift mutation encoding a truncated amelogenin leads to X-linked amelogenesis imperfecta PMID: 11839357 self-assembly and apatite binding properties of amelogenin proteins lacking the hydrophilic C-terminal. PMID: 11852235 Altered amelogenin self-assembly based on mutations observed in human X-linked amelogenesis imperfecta (AIH1). PMID: 11877393 C-terminus of the normal amelogenin protein is important for controlling enamel thickness. PMID: 11922869 2 mutations within coding region for amelogenin signal peptide predicted to interfere with secretion of amelogenin; could help clinicians in making diagnosis of X-linked AI. PMID: 15111628 Two synonymous single-nucleotide polymorphisms were found in databases. Alignment of the primate exon 6 sequences revealed that AMELX is highly constrained. PMID: 17645864 Amelogenin locus in chimerism monitoring of stem cell patients transplanted. PMID: 17688372 Having at least one copy of the rare amelogenin marker allele was associated with increased age-adjusted caries experience. PMID: 18042988 Binding of the P41T mutant amelogenin for matrix metalloproteinase 20 was significantly lower than that of wild-type amelogenin. PMID: 18434575 Prolines at the amelogenin C terminus are essential for the initial processing of amelogenin and amelogenin-mineral interactions. PMID: 18701806 A total of 463 individuals from 54 families were evaluated and mutations in the AMEL, ENAM and KLK4 genes were identified. PMID: 18714142 Overrepresentation of C allele of amelogenin marker was seen in dmft scores higher than 8 when compared to controls. Overrepresentation of T allele of ameloblastin marker was seen in dmfs scores higher than 10 when compared to controls. PMID: 18781068 Amelogenin can adsorb onto surfaces as small structures that "shed" or disassemble from the nanospheres that are present in solution. PMID: 19025992 Forensic genetic genotyping system using amelogenin using single nucleotide polymorphism. PMID: 19083859 In a family with a hypomaturation-type enamel defect, mutational and haplotype analyses revealed no mutations in the AMELX gene. PMID: 19966041

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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.