Recombinant Human AMG Protein

Name: Recombinant Human AMG Protein
Brand: Beta LifeScience
SKU: BLA-12123P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Human
Accession	Q99217
Synonym	AI1E AIH1 ALGN Amel Amelogenesis imperfecta 1 Amelogenin Amelogenin (amelogenesis imperfecta 1, X linked) Amelogenin (X chromosome) Amelogenin (X chromosome, amelogenesis imperfecta 1) Amelogenin X isoform Amelogenin, X linked AMELX AMELX_HUMAN Amg AMGL AMGX OTTHUMP00000022906 OTTHUMP00000022907 X isoform
Description	Recombinant Human AMG Protein was expressed in E.coli. It is a Full length protein
Source	E.coli
AA Sequence	MGSSHHHHHH SSGLVPRGSH MGSMPLPPHP GHPGYINFSY EVLTPLKWYQ SIRPPYPSYG YEPMGGWLHH QIIPVLSQQH PPTHTLQPHH HIPVVPAQQP VIPQQPMMPV PGQHSMTPIQ HHQPNLPPPA QQPYQPQPVQ PQPHQPMQPQ PPVHPMQPLP PQPPLPPMFP MQPLPPMLPD LTLEAWPSTD KTKREEVD
Molecular Weight	22 kDa including tags
Purity	Greater than 90% SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Liquid Solution
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

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: Hs.654436
Associated Diseases	Amelogenesis imperfecta 1E (AI1E)

Gene Functions References

High AMEL expression is associated with Aggressiveness in Odontogenic Tumors. 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

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.