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>   首页   >   产品   >   一抗   >   神经科学   >   PPT2 Antibody - C-terminal region   

PPT2 Antibody - C-terminal region

Rabbit Polyclonal Antibody

     
  • 1 - PPT2 Antibody - C-terminal region AI16118

    Host: Rabbit
    Target Name: PPT2
    Sample Tissue: Fetal Liver lysates
    Antibody Dilution: 1.0μg/ml
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB
Primary Accession Q9UMR5
Reactivity Human
Host Rabbit
Clonality Polyclonal
Calculated MW 34225 Da
Additional Information
Gene ID 9374
Alias Symbol PPT2,
Other Names Lysosomal thioesterase PPT2, PPT-2, 3.1.2.-, S-thioesterase G14, PPT2
Format Liquid. Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
Reconstitution & Storage Add 50 &mu, l of distilled water. Final Anti-PPT2 antibody concentration is 1 mg/ml in PBS buffer with 2% sucrose. For longer periods of storage, store at -20°C. Avoid repeat freeze-thaw cycles.
PrecautionsPPT2 Antibody - C-terminal region is for research use only and not for use in diagnostic or therapeutic procedures.

For Research Use Only. Not For Use In Diagnostic Procedures.

Protein Information
Name PPT2 (HGNC:9326)
Function Catalyzes the cleavage of thioester bonds from S-palmitoyl- CoA or S-palmitoyl-N-acetylcysteamine (unbranched structures) but does not have activity against palmitoylcysteine or palmitoylated proteins, branched structures or bulky head groups. Conversely, hydrolyzes both long and short chain fatty acyl-CoA substrate.
Cellular Location Lysosome.
Tissue Location Broadly expressed, with highest levels in skeletal muscle.
Research Areas

BACKGROUND

Removes thioester-linked fatty acyl groups from various substrates including S-palmitoyl-CoA. Has the highest S- thioesterase activity for the acyl groups palmitic and myristic acid followed by other short- and long-chain acyl substrates. However, because of structural constraints, is unable to remove palmitate from peptides or proteins.

REFERENCES

Soyombo A.A.,et al.J. Biol. Chem. 272:27456-27463(1997).
Aguado B.,et al.Biochem. J. 341:679-689(1999).
Wiemann S.,et al.Genome Res. 11:422-435(2001).
Ebert L.,et al.Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
Ota T.,et al.Nat. Genet. 36:40-45(2004).

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