Product Details

Purity

Greater than 85% as determined by SDS-PAGE.

Target Names

Alas2

Uniprot No.

P08680

Research Area

Cancer

Alternative Names

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)

Source

E.coli

Expression Region

50-587aa

Target Protein Sequence

QIHLKATKAGGDSPSWAKSHCPFMLSELQDRKSKIVQRAAPEVQEDVKTFKTDLLSTMDSTTRSHSFPSFQEPEQTEGAVPHLIQNNMTGSQAFGYDQFFRDKIMEKKQDHTYRVFKTVNRWANAYPFAQHFSEASMASKDVSVWCSNDYLGISRHPRVLQAIEETLKNHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKLLPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPGHLKKLLEKSDPKTPKIVAFETVHSMDGAICPLEELCDVAHQYGALTFVDEVHAVGLYGARGAGIGERDGIMHKLDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGFPVIPCPSHIIPIRVGNAALNSKICDLLLSKHSIYVQAINYPTVPRGEELLRLAPSPHHSPQMMENFVEKLLLAWTEVGLPLQDVSVAACNFCHRPVHFELMSEWERSYFGNMGPQYVTTYA
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.

Mol. Weight

65.6 kDa

Protein Length

Full Length of Mature Protein

Tag Info

N-terminal 6xHis-tagged

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer

Tris-based buffer，50% glycerol

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Target Background

Gene References into Functions

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

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Subcellular Location

Mitochondrion matrix.

Protein Families

Class-II pyridoxal-phosphate-dependent aminotransferase family

Tissue Specificity

Erythroid specific.

Database Links

KEGG: mmu:11656

STRING: 10090.ENSMUSP00000066040

UniGene: Mm.302724

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Code	CSB-EP001560MO
MSDS	MSDS
Size	US$388
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Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Recombinant Mouse 5-aminolevulinate synthase, erythroid-specific, mitochondrial (Alas2)

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