AV53616
Anti-PDXK (AB2) antibody produced in rabbit
affinity isolated antibody
Synonym(s):
Anti-C21orf124, Anti-C21orf97, Anti-DKFZp566A071, Anti-FLJ31940, Anti-FLJ37311, Anti-MGC15873, Anti-MGC31754, Anti-Pyridoxal (pyridoxine, vitamin B6) kinase
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About This Item
NACRES:
NA.41
UNSPSC Code:
12352203
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
34 kDa
species reactivity
human
concentration
0.5 mg - 1 mg/mL
technique(s)
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Gene Information
human ... PDXK(8566)
Immunogen
Synthetic peptide directed towards the middle region of human PDXK
Application
Anti-PDXK (AB2) antibody produced in rabbit is suitable for western blotting at a concentration of 1μg/mL.
Biochem/physiol Actions
PDXK phosphorylates vitamin B6, a step required for the conversion of vitamin B6 to pyridoxal-5-phosphate, an important cofactor in intermediary metabolism. PDXK is cytoplasmic and probably acts as a homodimer. The protein encoded by this gene phosphorylates vitamin B6, a step required for the conversion of vitamin B6 to pyridoxal-5-phosphate, an important cofactor in intermediary metabolism. The encoded protein is cytoplasmic and probably acts as a homodimer. Alternatively spliced transcript variants have been described, but their biological validity has not been determined. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
Other Notes
Synthetic peptide located within the following region: RKIHSQEEALRVMDMLHSMGPDTVVITSSDLPSPQGSNYLIVLGSQRRRN
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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Storage Class
12 - Non Combustible Liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Elizabeth E Rueschhoff et al.
Plant physiology and biochemistry : PPB, 63, 281-291 (2013-01-17)
Vitamin B(6) (pyridoxal 5'-phosphate and its vitamers) is an important cofactor in numerous enzymatic reactions. In spite of its importance, the consequences of altering vitamin B(6) content on plant growth and development are not well understood. This study compares two
Deuan C Jones et al.
Molecular microbiology, 86(1), 51-64 (2012-08-04)
Pyridoxal-5'-phosphate (vitamin B(6) ) is an essential cofactor for many important enzymatic reactions such as transamination and decarboxylation. African trypanosomes are unable to synthesise vitamin B(6) de novo and rely on uptake of B(6) vitamers such as pyridoxal and pyridoxamine
Amit K Gandhi et al.
PloS one, 7(7), e40954-e40954 (2012-08-11)
Several drugs and natural compounds are known to be highly neurotoxic, triggering epileptic convulsions or seizures, and causing headaches, agitations, as well as other neuronal symptoms. The neurotoxic effects of some of these compounds, including theophylline and ginkgotoxin, have been
Freddy Navarro et al.
Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 26(5), 805-812 (2013-07-19)
Pyridoxal 5'-phosphate is the active form of vitamin B6 and its deficiency is directly related with several human disorders, which make human pyridoxal kinase (hPLK) an important pharmacologic target. In spite of this, a carefully kinetic characterization of hPLK including
Faik N Musayev et al.
Protein science : a publication of the Protein Society, 16(10), 2184-2194 (2007-09-04)
Pyridoxal kinase catalyzes the transfer of a phosphate group from ATP to the 5' alcohol of pyridoxine, pyridoxamine, and pyridoxal. In this work, kinetic studies were conducted to examine monovalent cation dependence of human pyridoxal kinase kinetic parameters. The results
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