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

Name: Recombinant Mouse Amelogenin, X Isoform (AMELX) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-06366P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Amelogenin, X Isoform (AMELX) 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	P63277
Target Symbol	AMELX
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MPLPPHPGSPGYINLSYEKSHSQAINTDRTALVLTPLKWYQSMIRQPYPSYGYEPMGGWLHHQIIPVLSQQHPPSHTLQPHHHLPVVPAQQPVAPQQPMMPVPGHHSMTPTQHHQPNIPPSAQQPFQQPFQPQAIPPQSHQPMQPQSPLHPMQPLAPQPPLPPLFSMQPLSPILPELPLEAWPATDKTKREEVD
Expression Range	17-210aa
Protein Length	Full Length of Mature Protein
Mol. Weight	29.3 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	Plays a role in the biomineralization of teeth. 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	KEGG: mmu:11704 UniGene: PMID: 29337060 Results provide evidence that all three regions of amelogenin (N-terminus, C-terminus, central core) are required for enamel formation and structure. PMID: 26607574 an involvement of LRAP in lipid-raft-dependent signaling pathways are mediated by flotillin-1. PMID: 27277399 transcriptional activation of Amelx was associated with enhanced osteogenic differentiation, especially in the early stage of biomineralization PMID: 26709694 LRAP is primarily monomeric in solution, suggesting that the monomeric species may be an important functional form of some amelogenins. PMID: 25449314 AMELX may function as a growth factor-like molecules solubilized in the aqueous microenvironment. In jaws, it might play some role in bone physiology through autocrine/paracrine pathways, particularly during development and stress-induced remodeling. PMID: 24933156 temporal/spatial localization of amelogenins with exon4 peptide and functional differences in HAP binding suggests unique properties of amelogenins containing exon4 cause specific enhancement of biomineralization of early-formed HAP at maturation stage PMID: 25792521 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 Leucine rich amelogenin peptide alters ameloblast differentiation in vivo. PMID: 23747796 the interaction of amelogenin with Grp78/Bip contributed to cell proliferation, rather than correlate with the osteogenic differentiation PMID: 24167599 among amelogenins, M180 alone is sufficient for normal enamel mechanical properties and prism patterns, but that additional amelogenin splice products are required to restore enamel thickness. PMID: 24072097 ERP expression follows defined developmental profiles; affects osteoblast differentiation, mineralization, calvarial bone development. with role in developing enamel matrix, ERPs retain conserved function related to bone biomineralization. PMID: 23625374 The study investigates the structure, orientation, and dynamics of three regions in the N-terminus of the protein: L(15) to V(19), V(19) to L(23), and K(24) to S(28). Phosphorylation and ionic strength alter the LRAP-hydroxyapatite interface. PMID: 23477367 Analyses of these data suggest that MMP-9 may be involved in controlling amelogenin processing and enamel formation. PMID: 22648084 Amelogenin affected mandible morphology and incisor enamel formation, while enamelin only affected incisors, supporting the multifunctional role of amelogenin. PMID: 22759786 analysis of daily rhythms of clock genes and Amelx in murine ameloblast cells PMID: 22653892 Amelogenin molecules form complex 3D-structures with N-terminal alpha-helix-like segments and C-terminal PPII-helices. PMID: 21984897 Alterations in the assembly (i.e. premature aggregation) of mutant amelogenins may have a profound effect on intra- and extracellular processes. PMID: 21540557 Amelogenin assembly is a multistep hierarchical process and provides new insight into the control of enamel mineralization. PMID: 21597263 Amelogenin promotes odontoblast-like MDPC-23 cell differentiation PMID: 21547453 Amelogenin undergoes stepwise hierarchical self-assembly. PMID: 21825148 Dlx2 and FoxJ1 physically interact and synergistically regulate the Dlx2, FoxJ1, and amelogenin promoters PMID: 21504905 elevated levels of Notch 1 in developing molars. cells within masses express transgenic amelogenins; development of abnormal proliferations suggests communication between amelogenin producing cells and proliferating cells PMID: 20923441 The presence of LRAP leads to changes in enamel appearance compared to enamel from knockout mice.[LRAP] PMID: 18701811 data indicate that specific levels of Amelx and Dspp gene expression define whether mouse cytomegalovirus induces enamel agenesis or hypoplasia PMID: 20484882 interactions between collagen and amelogenin might play an important role in the formation of the DEB providing structural continuity between dentin and enamel PMID: 20404336 We hypothesize that intracellular protein-protein interactions mediated via the amelogenin tri-tyrosyl motif are a key mechanistic factor underpinning the molecular pathogenesis in this example of AI. PMID: 20067920 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 Polypeptides translated from alternatively spliced transcripts of the amelogenin gene, devoid of the exon 6a, b, c region, have effects on tooth germ development in culture. PMID: 12489164 interaction with cytokeratin-5 in ameloblasts during enamel growth PMID: 12657653 developmental regulated expression pattern is enhanced under vitamin-D-deficiency status and in a broader context may play an important role during ameloblast and odontoblast differentiation and function. PMID: 12667550 a critical signaling molecule required for appropriate development of the periodontium PMID: 14653387 specific amelogenin isoforms have effects on embryonic tooth development in vitro; DMP2 may play a role in the terminal differentiation of both ameloblasts and odontoblasts PMID: 15647828 data supports the hypothesis that: (1) AMELX contains 2 additional exons; (2) ameloblasts and odontoblasts synthesize amelogenin 8/9; and (3) amelogenin splice variants may have unique functions during tooth formation. PMID: 15972588 Conformational analyses of a recombinant mouse tooth enamel amelogenin using circular dichroism (CD), fluorescence, differential scanning calorimetry, and sedimentation equilibrium studies. PMID: 16284958 during differentiation, dental epithelial cells utilize a unique mechanism for increasing the production of amelogenin, the reuptake of secreted amelogenin PMID: 16293627 activated by synergism between C/EPBalpha and NF-Y PMID: 16595692 mutations within conserved amelogenin domains could account for enamel variations preserved in the fossil record PMID: 16707492 Analyses of amelogenin mRNA between control and Mmp20(-/-)mice revealed no differences in the splicing pattern. 3 previously unidentified amelogenin alternatively spliced transcripts are characterized. Exon-8-encoded isoforms are processed by MMP-20 PMID: 16998127 Co-immunoprecipitation analyses identified that the carboxyl-terminal domain (residues 218-359) of C/EBPalpha is required for the C/EBPalpha-Msx2 protein-protein interactions. PMID: 17210130 Female Amelx+/- animals showed significant reduction in optical retardation values when compared with the Amelx+/+ subgroup (p=0.0029). The secretory-stage enamel organic extracellular matrix of the Amelx-/- subgroup did not exhibit birefringence. PMID: 17364666 C/EBPdelta activates the mouse amelogenin promoter and synergistically cooperates with nuclear factor Y, suggesting that C/EBPdelta can functionally substitute for C/EBPalpha to produce an enamel matrix competent to direct biomineralization PMID: 17704518 demonstrate the protein region defined by amino acid residues 103-205 for CD63 interacts not only with amelogenin, but also with other enamel matrix proteins PMID: 17708745 the ameloblastin 37-kDa isoform interacts with amelogenin during early tooth development. PMID: 17921454 a single amelogenin protein was able to significantly rescue the KO phenotype and that one amino acid change abrogated this function during development. PMID: 18390542 Results describe the functional activity of the [A-4] amelogenin gene splice product in newborn mouse ameloblasts. PMID: 18394981 These findings suggest that the BMP2/4 contaminated during the purification process of enamel matrix derivative because of the avidity of amelogenin plays an important role in signaling pathway of calcification. PMID: 18515207 The presence of LRAP leads to changes in enamel appearance compared to enamel from KO mice. PMID: 18701811 Mice lacking expression of the AmelX, Enam and Mmp20 genes have been generated. PMID: 18714142

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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.