Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | P30566 |
express system | E.coli |
product tag | N-His |
purity | > 95% as determined by Tris-Bis PAGE |
background | Adenylosuccinate lyase (ADSL) is an essential enzyme for de novo purine biosynthesis, ADSL functions in de novo purine synthesis (DNPS) and the purine nucleotide cycle. Adenylosuccinate lyase ADSL) deficiency is a defect of purine metabolism affecting purinosome assembly and reducing metabolite fluxes through purine de novo synthesis and purine nucleotide recycling pathways. |
molecular weight | The protein has a predicted MW of 56.28 kDa same as Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Human Adenylosuccinate Lyase Protein 2466
$300.00 – $1,000.00
Summary
- Expression: E.coli
- Pure: Yes (SDS-PAGE)
- Amino Acid Range: Ala2-Leu484
Human Adenylosuccinate Lyase Protein 2466
protein |
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Size and concentration 100, 500µg and lyophilized |
Form Lyophilized |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped at ambient temperature. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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Adenylosuccinate lyase (ADSL) is an essential enzyme for de novo purine biosynthesis, ADSL functions in de novo purine synthesis (DNPS) and the purine nucleotide cycle. Adenylosuccinate lyase ADSL) deficiency is a defect of purine metabolism affecting purinosome assembly and reducing metabolite fluxes through purine de novo synthesis and purine nucleotide recycling pathways. |
Protein names Adenylosuccinate lyase (ADSL) (ASL) (EC 4.3.2.2) (Adenylosuccinase) (ASase) |
Gene names ADSL,ADSL AMPS |
Protein family Lyase 1 family, Adenylosuccinate lyase subfamily |
Mass 9606Da |
Function Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate. |
Catalytic activity #N/A |
Pathway PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2.; PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole |
Tissues Ubiquitously expressed. Both isoforms are produced by all tissues. Isoform 2 is 10-fold less abundant than isoform 1. |
Structure Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site. |
Target Relevance information above includes information from UniProt accession: P30566 |
The UniProt Consortium |
Data
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Human Adenylosuccinate Lyase on Tris-Bis PAGE under reduced condition. The purity is greater than 95%. |
Publications
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