Sign In to View Organizational & Contract Pricing.
Select a Size
About This Item
NACRES:
NA.41
UNSPSC Code:
12352203
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ELISA (i)
Citations:
2
biological source
rabbit
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
species reactivity
human
technique(s)
indirect ELISA: 1:1000
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... ADPRH(141)
General description
ADP-ribosylarginine hydrolase (ADPRH) is part of the ADP-ribosylhydrolase (ARH) gene family.
Immunogen
ADPRH (NP_001116, 13-48)
This antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected from the N-terminal region of human ADPRH.
This antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected from the N-terminal region of human ADPRH.
Biochem/physiol Actions
ADP-ribosylarginine hydrolase (ADPRH) catalyzes the removal of mono-ADP-ribose from arginine residues of proteins in the ADP-ribosylation cycle. Unlike the rat and mouse enzymes, which require DTT for maximal activity, the human enzyme is DTT-independent.
Physical form
Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide.
Not finding the right product?
Try our Product Selector Tool.
Storage Class
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
常规特殊物品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Cloning, expression, purification and crystallization as well as X-ray fluorescence and preliminary X-ray diffraction analyses of human ADP-ribosylhydrolase 1.
Kernstock S
Acta Crystallographica. Section F, Structural Biology Communications (2009)
The family of toxin-related ecto-ADP-ribosyltransferases in humans and the mouse.
Glowacki G
Protein Science (2002)
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service