Recombinant Human Enamelin (ENAM) Protein (His)

Name: Recombinant Human Enamelin (ENAM) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06728P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Human Enamelin (ENAM) Protein (His) is produced by our Baculovirus expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9NRM1
Target Symbol	ENAM
Species	Homo sapiens (Human)
Expression System	Baculovirus
Tag	C-6His
Target Protein Sequence	ERQQQRPSNILHLPCFGSKLAKHHSSTTGTPSSDGRQSPFDGDSITPTENPNTLVELATEEQFKSINVDPLDADEHSPFEFLQRGTNVQDQVQDCLLLQA
Expression Range	1043-1142aa
Protein Length	Partial
Mol. Weight	12.4 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	Involved in the mineralization and structural organization of enamel. Involved in the extension of enamel during the secretory stage of dental enamel formation.
Subcellular Location	Secreted, extracellular space, extracellular matrix.
Database References	HGNC: 3344 OMIM: 104500 KEGG: hsa:10117 STRING: 9606.ENSP00000379383 UniGene: Hs.667018
Associated Diseases	Amelogenesis imperfecta 1B (AI1B); Amelogenesis imperfecta 1C (AI1C)
Tissue Specificity	Expressed in tooth particularly in odontoblast, ameloblast and cementoblast.

Gene Functions References

Lack of association between the ENAM polymorphism (rs12640848) and dental caries in Czech children was detected. PMID: 29185146
The ENAM and TNF-alpha genes were likely associated with caries occurrence in Chinese children. The ENAM rs3796703 CT and TNF-alpha rs1800629 AG genotypes might be involved in caries susceptibility and protection, respectively. PMID: 28395167
study investigated the phenotypic effect of SNP C14625T (rs7671281) on the thickness of human dental enamel, exploring the effects of positive selection on a dental gene PMID: 27357321
Among the variants shared with modern humans, two are ancestral (common with apes) and one is the derived enamelin major variant, T648I (rs7671281), associated with a thinner enamel and specific to the Homo lineage. PMID: 28902892
The study revealed the strong association between rs12640848 marker of ENAM gene and caries susceptibility in primary teeth in children from Poland. PMID: 26910531
Overrepresentation of the G allele of the enamelin marker was seen in the erosion group compared to the unaffected group. PMID: 25791822
Screening of ENAM and LAMB3 genes was performed by direct sequencing of genomic DNA from blood samples. PMID: 25769099
findings provide useful information for the implication of ENAM gene polymorphism in autosomal-dominant/-recessive amelogenesis imperfecta. PMID: 25427323
Whole-exome sequencing identified 2 novel heterozygous nonsense mutations in the ENAM gene (c.454G>T p.Glu152* in family 1, c.358C>T p.Gln120* in family 2) in the probands. Affected individuals were heterozygous for the mutation in each family. PMID: 25143514
2 exonic SNPs, both changing an amino acid in protein region encoded by exon 10 (p.I648T and p.R763Q), increased caries susceptibility 2.66-fold. findings support ENAM as gene candidate for caries susceptibility. PMID: 24487377
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
Mutations in FAM83H and ENAM and related phenotypes were observed in Chinese families with amelogenesis imperfecta. PMID: 22414746
hypocalcified amelogenesis imperfecta, Witkop type III, was unrelated to previously described mutations in the ENAM or MMP-20 genes PMID: 21504268
The structure and composition of deciduous enamel affected by local hypoplastic autosomal dominant amelogenesis imperfecta resulting from an ENAM mutation PMID: 19923784
A nonsense mutation in the enamelin gene causes local hypoplastic autosomal dominant amelogenesis imperfecta PMID: 11978766
heterogeneous mutations are responsible for an autosomal-dominant hypoplastic form of amelogenesis imperfecta PMID: 12407086
critical for proper dental enamel formation PMID: 14656895
Demonstration of a ENAM mutation responsible for autosomal recessive amelogenesis imperfecta and localised enamel pitting. PMID: 14684688
Ultrastructural enamel changes in the patient with the autosomal dominant ENAM g.13185-13186insAG mutation, were less pronounced compared to ultrastructural changes in patients with the autosomal dominant ENAM mutation 8344delG. PMID: 17125728
A mutation was found in exon 9 where guanine was substituted by thymine in one of the alleles in position 817, generating a change of arginine to methionine in codon 179 of the protein. PMID: 17316551
This work shows that bursts of adaptive enamelin evolution occur on primate lineages with inferred dietary changes. PMID: 18245370
a single base difference g359A --> G located in exon 1 was identified and ruled out the possible mutation in exon 2, exon 3, exon 4, exon 5, exon 6, exon 7, exon 8, exon 9, exon 10, g2382, g6395 and g8344 of ENAM gene in the AI patient. PMID: 18466877
A total of 463 individuals from 54 families were evaluated and mutations in the AMEL, ENAM and KLK4 genes were identified. PMID: 18714142
Analysis revealed 2 ENAM mutations (autosomal-dominant g.14917delT and autosomal-recessive g.13185-13186insAG mutations). Single T deletion in exon 10 is a novel deletion mutation(g.14917delT, c.2991delT)predicted to result in premature termination codon. PMID: 19329462

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.