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.
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
- 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
- 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
- We propose that the N-terminal truncation offers a cell-specific ALAS2 regulatory mechanism without hindering heme synthesis PMID: 26854603
- N150F ALAS variant catalyzes the forward reaction at a mere 1.2-fold faster rate than that of the reverse reaction. PMID: 26511319
- 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
- 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
- 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
- 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
- Aberrant iron accumulation and peroxidized state of (ALAS2)-deficient definitive erythroblasts PMID: 12393610
- mechanism of up-regulation in erythroleukemia cells exposed to hypoxia PMID: 12393745
- 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
- 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