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biological source
human
Quality Level
assay
>95% (SDS-PAGE)
form
liquid
specific activity
864 U/mg
manufacturer/tradename
Chemicon®
concentration
3.28 mg/mL
NCBI accession no.
UniProt accession no.
shipped in
wet ice
Gene Information
human ... ACPP(55)
General description
Product Source: Human seminal fluid. Tested negative for HIV I/II, HIV-1 antigen, and HCV antibodies and Hepatitis B surface antigen.
Purified HUMAN PROSTATIC ACID PHOSPHATASE (PAP) Protien isolated from human seminal Fluid.
NOTE:
This product exhibits phosphatase activity in acid conditions in the presence of chromogenic phosphate substrates.
NOTE:
This product exhibits phosphatase activity in acid conditions in the presence of chromogenic phosphate substrates.
Physical form
Purified protein. Lyophilized from 0.2um filtered solution with 0.02mM Ammonium Bicarbonate.
Storage and Stability
Maintain at -20°C in undiluted aliquots for up to 6 months. Avoid repeated freeze/thaw cycles.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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PloS one, 5(1), e8674-e8674 (2010-01-20)
Thiamine monophosphatase (TMPase, also known as Fluoride-resistant acid phosphatase or FRAP) is a classic histochemical marker of small- to medium-diameter dorsal root ganglia (DRG) neurons and has primarily been studied in the rat. Previously, we found that TMPase was molecularly
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