A6610
Anti-ASNS (506-520) antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
Synonym(s):
Anti-Asparagine synthetase, Anti-TS11
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
biological source
rabbit
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~64 kDa
species reactivity
human
technique(s)
western blot: 1:500-1:2,000
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... ASNS(440)
General description
ASNS is an enzyme that promotes the production of asparagine from aspartate.
Asparagine synthetase (ASNS) deficiencies have been linked to progressive encephalopathy and congenital microcephaly. Furthermore, ASNS has also been analyzed for its role in drug-resistant childhood acute lymphoblastic leukemia (ALL). Rabbit Anti-ASNS (506-520) binds to human ASNS (506-520).
Immunogen
synthetic peptide corresponding to amino acids 506-520 of human ASNS
Application
Rabbit Anti-ASNS (506-520) antibody has been used for western blot applications at dilutions of 1:500-1:2,000.
Yale Center for High Throughput Cell Biology IF-tested antibodies. Each antibody is tested by immunofluorescence against HUVEC cells using the Yale HTCB IF protocol. To learn more about us and Yale Center for High Throughput Cell Biology partnership, visit sigma.com/htcb-if.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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.
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Nigel G J Richards et al.
Annual review of biochemistry, 75, 629-654 (2006-06-08)
Modern clinical treatments of childhood acute lymphoblastic leukemia (ALL) employ enzyme-based methods for depletion of blood asparagine in combination with standard chemotherapeutic agents. Significant side effects can arise in these protocols and, in many cases, patients develop drug-resistant forms of
Philip L Lorenzi et al.
Drug news & perspectives, 22(1), 61-64 (2009-02-12)
L-Asparaginase (L-ASP) is an enzyme drug that has been an asset to leukemia treatment regimens for four decades. Variability in its clinical efficacy, however, has prompted the search for biomarkers capable of distinguishing responders from non-responders. In that regard, the
Elizabeth K Ruzzo et al.
Neuron, 80(2), 429-441 (2013-10-22)
We analyzed four families that presented with a similar condition characterized by congenital microcephaly, intellectual disability, progressive cerebral atrophy, and intractable seizures. We show that recessive mutations in the ASNS gene are responsible for this syndrome. Two of the identified
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