"AMPD2" Related Products

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Recombinant Human AMPD2

Cat.No.: AMPD2-27197TH
Product Overview: Recombinant fragment of Human AMPD2, isoform Ex1A-2-3 with N terminal proprietary tag; Predicted MW 36.63 kDa.
Description: Adenosine monophosphate deaminase-2 (EC 3.5.4.6) catalyzes the deamination of AMP to IMP and plays an important role in the purine nucleotide cycle.
Protein length: 100 amino acids
Molecular Weight: 36.630kDa inclusive of tags
Source: Wheat germ
Tissue specificity: Three isoforms are present in mammals: AMP deaminase 1 is the predominant form in skeletal muscle; AMP deaminase 2 predominates in smooth muscle, non-muscle tissue, embryonic muscle and undifferentiated myoblasts; AMP deaminase 3 is found in erythrocytes.
Form: Liquid
Purity: Proprietary Purification
Storage buffer: pH: 8.00Constituents:0.3% Glutathione, 0.79% Tris HCl
Storage: Shipped on dry ice. Upon delivery aliquot and store at -80oC. Avoid freeze / thaw cycles.
Sequences of amino acids: ISQDVKLEPDILLRAKQDFLKTDSDSDLQLYKEQGEGQGDRSLRERDVLEREFQRVTISGEEKCGVPFTDLLDAAKSVVRALFIREKYMALSLQSFCPTT
Sequence Similarities: Belongs to the adenosine and AMP deaminases family.
Gene Name: AMPD2 adenosine monophosphate deaminase 2 [ Homo sapiens ]
Official Symbol: AMPD2
Synonyms: AMPD2; adenosine monophosphate deaminase 2; adenosine monophosphate deaminase 2 (isoform L); AMP deaminase 2; AMPD isoform L;
Gene ID: 271
mRNA Refseq: NM_004037
Protein Refseq: NP_004028
MIM: 102771
Uniprot ID: Q01433
Chromosome Location: 1p13.3
Pathway: Metabolic pathways, organism-specific biosystem; Metabolism, organism-specific biosystem; Metabolism of nucleotides, organism-specific biosystem; Purine metabolism, organism-specific biosystem; Purine metabolism, organism-specific biosystem;
Function: AMP deaminase activity; hydrolase activity; metal ion binding;

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Optional requirements on this protein    +Expand
C-fusion    N-fusion   Non-tagged
His    GST   Fc   Others
<1.0 eu/μg    <0.1 eu/μg   <0.01 eu/μg   Not required
Monomer Isolation    Dimer Isolation    Not required
>80% by SDS-PAGE    >90% by SDS-PAGE   >95% by SDS-PAGE   Others

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