Recombinant Mouse 5-Aminolevulinate Synthase, Erythroid-Specific, Mitochondrial (ALAS2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-11122P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Mouse 5-Aminolevulinate Synthase, Erythroid-Specific, Mitochondrial (ALAS2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-11122P
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 Mouse 5-Aminolevulinate Synthase, Erythroid-Specific, Mitochondrial (ALAS2) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P08680
Target Symbol ALAS2
Synonyms Alas2; 5-aminolevulinate synthase; erythroid-specific; mitochondrial; ALAS-E; EC 2.3.1.37; 5-aminolevulinic acid synthase 2; Delta-ALA synthase 2; Delta-aminolevulinate synthase 2
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-6His
Target Protein Sequence QIHLKATKAGGDSPSWAKSHCPFMLSELQDRKSKIVQRAAPEVQEDVKTFKTDLLSTMDSTTRSHSFPSFQEPEQTEGAVPHLIQNNMTGSQAFGYDQFFRDKIMEKKQDHTYRVFKTVNRWANAYPFAQHFSEASMASKDVSVWCSNDYLGISRHPRVLQAIEETLKNHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKLLPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPGHLKKLLEKSDPKTPKIVAFETVHSMDGAICPLEELCDVAHQYGALTFVDEVHAVGLYGARGAGIGERDGIMHKLDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGFPVIPCPSHIIPIRVGNAALNSKICDLLLSKHSIYVQAINYPTVPRGEELLRLAPSPHHSPQMMENFVEKLLLAWTEVGLPLQDVSVAACNFCHRPVHFELMSEWERSYFGNMGPQYVTTYA
Expression Range 50-587aa
Protein Length Full Length of Mature Protein
Mol. Weight 65.6 kDa
Research Area Cancer
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.
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

Subcellular Location Mitochondrion matrix.
Protein Families Class-II pyridoxal-phosphate-dependent aminotransferase family
Database References
Tissue Specificity Erythroid specific.

Gene Functions References

  1. we used bioinformatics and computational biology tools to evaluate the role(s) of the C-terminal tail dynamics in the structure and conformational dynamics of the murine ALAS2 homodimer active site loop. PMID: 29958424
  2. Data indicate that the 5-aminolevulinate synthase (mALAS2) active site loop harboring the simultaneous seven amino acid mutations was less flexible than the wild type loop. PMID: 27928941
  3. We propose that the N-terminal truncation offers a cell-specific ALAS2 regulatory mechanism without hindering heme synthesis PMID: 26854603
  4. N150F ALAS variant catalyzes the forward reaction at a mere 1.2-fold faster rate than that of the reverse reaction. PMID: 26511319
  5. Light treatments revealed that ALAS2 expression results in an increase in cell death in comparison to aminolevulinic acid (ALA) treatment producing a similar amount of protoprophyrin IX. PMID: 24718052
  6. The rate of ALA release is also controlled by a hysteretic kinetic mechanism (observed as a lag in the ALA external aldimine formation progress curve), consistent with conformational changes governing the dissociation of ALA from ALAS. PMID: 24920668
  7. impaired mitochondrial [Fe-S] cluster biogenesis in Mfrn1(gt/gt) cells results in elevated IRP1 RNA-binding that attenuates ALAS2 mRNA translation and protoporphyrin accumulation PMID: 24509859
  8. Data suggest the reaction of glycine with ALAS follows a three-step kinetic process, and the substrate 5-aminolevulinate induces a conformational change in ALAS which may modulate product release. PMID: 12191993
  9. Aberrant iron accumulation and peroxidized state of (ALAS2)-deficient definitive erythroblasts PMID: 12393610
  10. mechanism of up-regulation in erythroleukemia cells exposed to hypoxia PMID: 12393745
  11. These findings thus suggest that heme may regulate a wide variety of hitherto unrecognized genes, and further analysis of these genes may clarify their role in erythroid cell differentiation. PMID: 16356476
  12. Gene expression and enzymatic assays indicate that erythroid 5-aminolevulinic acid synthase (Alas2) is decreased in hem6 animals, suggesting a mechanism that could account for the anemia. PMID: 18780836

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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