MTAP Blocking Peptide for STJ503533 peptide (STJ505071)

SPECIFICATIONS
ImmunogenSynthetic peptide taken within amino acid region 233-283 on human methylthioadenosine phosphorylase protein.
STJ505071-250
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General Information

Short DescriptionMTAP Blocking Peptide for STJ503533 is synthetically produced from the 233-283 sequence and is suitable for use in western blot applications.
ApplicationsImmunodepletion/Immunocompetition
NoteSTRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.

Product Properties

FormulationLiquid form at 2.5mg/ml concentration in PBS. Up to 5% DMSO can be added. Orders with >1mg can be supplied in lyophilized powder form, or in buffer of choice.
Storage InstructionStore at-20°C for long term storage. Avoid freeze-thaw cycles.

Target Information

Gene SymbolMTAP
Gene ID4507
Uniprot IDMTAP_HUMAN
ImmunogenSynthetic peptide taken within amino acid region 233-283 on human methylthioadenosine phosphorylase protein.
Immunogen Region233-283
SpecificityThis blocking peptide is recommended for use in combination with MTAP antibody, STJ503533

Additional Info

Tissue Specificity Ubiquitously expressed.
Function Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.
Peptide Name S-Methyl-5'-Thioadenosine Phosphorylase
5'-Methylthioadenosine Phosphorylase
Mta Phosphorylase
Mtap
Mtapase
Database Links Reactome: R-HSA-1237112
Reactome: R-HSA-8950505
Cellular Localisation Cytoplasm
Nucleus
Alternative Peptide Names S-Methyl-5'-Thioadenosine Phosphorylase protein
5'-Methylthioadenosine Phosphorylase protein
Mta Phosphorylase protein
Mtap protein
Mtapase protein
MTAP protein
MSAP protein

Information sourced from Uniprot.org

Citations

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