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Recombinant Human ADSL, His-tagged

Cat.No. : ADSL-26897TH
Product Overview : Recombinant full length protein, (amino acids 1-484) of Human Adenylosuccinate Lyase with N terminal His tag; 520 amino acids, 59 kDa inclusive of tag.
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Description : Adenylsuccinate lyase is involved in both de novo synthesis of purines and formation of adenosine monophosphate from inosine monophosphate. It catalyzes two reactions in AMP biosynthesis: the removal of a fumarate from succinylaminoimidazole carboxamide (SAICA) ribotide to give aminoimidazole carboxamide ribotide (AICA) and removal of fumarate from adenylosuccinate to give AMP. Adenylosuccinase deficiency results in succinylpurinemic autism, psychomotor retardation, and , in some cases, growth retardation associated with muscle wasting and epilepsy. Two transcript variants encoding different isoforms have been found for this gene.
Protein length : 484 amino acids
Conjugation : HIS
Molecular Weight : 59.000kDa inclusive of tags
Source : E. coli
Tissue specificity : Ubiquitously expressed. Both isoforms are produced by all tissues. Isoform 2 is 10-fold less abundant than isoform 1.
Form : Liquid
Purity : >95% by SDS-PAGE
Storage buffer : pH: 8.00Constituents:0.32% Tris HCl, 0.02% DTT, 40% Glycerol, 0.58% Sodium chloride
Storage : Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze / thaw cycles.
Sequences of amino acids : MRGSHHHHHHGMASMTGGQQMGRDL YDDDDKDRWGSMAAGGDHGSPDSYR SPLASRYASPEMCFVFSDRYKFRTW RQLWLWLAEAEQTLGLPITDEQIQE MKSNLENIDFKMAAEEEKRLRHDVM AHVHTFGHCCPKAAGIIHLGATSCY VGDNTDLIILRNALDLLLPKLARVI SRLADFAKERASLPTLGFTHFQPAQ LTTVGKRCCLWIQDLCMDLQNLKRV RDDLRFRGVKGTTGTQASFLQLFEG DDHKVEQLDKMVTEKAGFKRAFIIT GQTYTRKVDIEVLSVLASLGASVHK ICTDIRLLANLKEMEEPFEKQQIGS SAMPYKRNPMRSERCCSLARHLMTL VMDPLQTASVQWFERTLDDSANRRI CLAEAFLTADTILNTLQNISEGLVV YPKVIERRIRQELPFMATENIIMAM VKAGGSRQDCHEKIRVLSQQAASVV KQEGGDNDLIERIQVDAYFSPIHSQ LDHLLDPSSFTGRASQQVQRFLEEE VYPLLKPYESVMKVKAELCL
Sequence Similarities : Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
Gene Name : ADSL adenylosuccinate lyase [ Homo sapiens ]
Official Symbol : ADSL
Synonyms : ADSL; adenylosuccinate lyase;
Gene ID : 158
mRNA Refseq : NM_000026
Protein Refseq : NP_000017
MIM : 608222
Uniprot ID : P30566
Chromosome Location : 22q13.1
Pathway : Alanine, aspartate and glutamate metabolism, organism-specific biosystem; Alanine, aspartate and glutamate metabolism, conserved biosystem; Inosine monophosphate biosynthesis, PRPP + glutamine => IMP, organism-specific biosystem; Inosine monophosphate biosynthesis, PRPP + glutamine =>
Function : (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity; N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; NOT N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; N6-(1,2-;

For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.

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Q&As (10)

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Are there any known genetic variations or mutations in the Adsl gene that affect protein function or stability? 10/08/2022

Genetic variations or mutations in the Adsl gene can affect the stability or function of Adsl protein, leading to metabolic disorders like Adenylosuccinate Lyase Deficiency.

Can Adsl protein interact with other proteins or form protein complexes, and if so, what are their functional implications? 02/15/2021

Adsl protein can interact with other proteins and form complexes, including the formation of multiprotein complexes involved in purine metabolism.

What are the structural features of Adsl protein that contribute to its enzymatic activity and substrate specificity? 09/09/2020

The enzymatic activity and substrate specificity of Adsl protein are attributed to its unique structural features, including conserved domains and active sites.

What experimental techniques have been used to characterize the enzymatic activity of Adsl protein? 05/10/2020

Experimental techniques such as enzymatic assays and substrate analysis have been used to characterize the enzymatic activity of Adsl protein.

Are there any pharmacological agents or small molecules that can modulate the activity or expression of Adsl protein, and could they have therapeutic potential for related conditions? 08/31/2019

Currently, there are no specific pharmacological agents targeting Adsl protein. However, understanding its regulation and functional implications may lead to the development of potential therapeutic approaches for related conditions.

What are the specific metabolic pathways or cellular processes in which Adsl protein is involved? 02/03/2018

Adsl protein is primarily involved in the de novo synthesis of purine nucleotides and participates in the purine salvage pathway.

Can the cellular localization of Adsl protein change in response to specific signals or cellular conditions? 01/15/2018

The cellular localization of Adsl protein is primarily in the cytoplasm, but it can also be found in the nucleus under specific conditions.

How does dysregulation or dysfunction of Adsl protein impact cellular metabolism and contribute to human diseases or disorders? 08/03/2017

Dysregulation or dysfunction of Adsl protein can disrupt purine metabolism, leading to metabolic disorders such as Adenylosuccinate Lyase Deficiency, which affects neurological and developmental processes.

How is the expression of Adsl protein regulated at the transcriptional and post-transcriptional levels? 04/07/2017

The expression of Adsl protein is regulated at both the transcriptional and post-transcriptional levels by various factors, such as transcription factors and microRNAs.

Are there any known cellular factors or cofactors that modulate the activity of Adsl protein? 09/23/2016

Adsl protein activity can be modulated by cellular factors and cofactors, including magnesium ions and ATP.

Customer Reviews (3)

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07/31/2021

    Exploring protein-protein interactions involved in apoptosis signaling.

    03/27/2018

      Characterizing protein-protein interactions involved in cancer progression.

      01/17/2017

        Determining protein-protein interaction interfaces using X-ray crystallography.

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