MABS487
Anti-Modified Citrulline Antibody, clone C4
clone C4, from human(Recombinant)
Sinónimos:
citrulline, modified citrulline
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Productos recomendados
biological source
human (Recombinant)
Quality Level
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
C4, monoclonal
species reactivity (predicted by homology)
all
technique(s)
ELISA: suitable
western blot: suitable
isotype
IgG1λ
shipped in
wet ice
target post-translational modification
unmodified
General description
Citrulline is thought to be an unincorporated amino acid that plays a part in intermediary metabolism. It is produced in the small intestine by enterocytes. Citrulline concentration in plasma and serum is thought to be a reliable and noninvasive biomarker of small intestine function and mass during disease. Citrulline has also been shown to play an important role in protein homeostasis. Modified citrulline is a chemically modified form of citrulline that is more immunogenic.
Immunogen
Citrulline-containing peptide modified with 2,3-butanedione monoxime and antipyrine.
Application
Research Category
Signaling
Signaling
Research Sub Category
Signaling Neuroscience
Signaling Neuroscience
This Anti-Modified Citrulline Antibody is validated for use in Western blotting and ELISA for the detection of Modified Citrulline.
Western Blotting Analysis: A 1:1,000 dilution from a representative lot detected Modified Citrulline in 10 µg of treated HL-60 cell lysate, using Anti-Human secondary antibody.
ELISA Analysis: A representative lot detected Modified Citrulline in ELISA.
ELISA Analysis: A representative lot detected Modified Citrulline in ELISA.
Quality
Evaluated by Western Blotting in treated cornified human cell lysate.
Western Blotting Analysis: A 1:1,000 dilution of this antibody detected Modified Citrulline in 10 µg of treated cornified human cell lysate, using Anti-Human secondary antibody.
Western Blotting Analysis: A 1:1,000 dilution of this antibody detected Modified Citrulline in 10 µg of treated cornified human cell lysate, using Anti-Human secondary antibody.
Physical form
Format: Purified
Human recombinant monoclonal IgG1λ in buffer containing PBS with 0.05% sodium azide.
Protein A purified
Storage and Stability
Stable for 1 year at 2-8°C from date of receipt.
Other Notes
Concentration: Please refer to lot specific datasheet.
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
10 - Combustible liquids
wgk_germany
WGK 2
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Issa O Yusuf et al.
Neurobiology of disease, 192, 106414-106414 (2024-01-23)
Alteration in protein citrullination (PC), a common posttranslational modification (PTM), contributes to pathogenesis in various inflammatory disorders. We previously reported that PC and protein arginine deiminase 2 (PAD2), the predominant enzyme isoform that catalyzes this PTM in the central nervous
Association of citrullination with the progression of aortic stenosis.
Kim, et al.
Scientific Reports, 13, 8919-8919 (2023)
Katerina D Samara et al.
Respiratory research, 18(1), 218-218 (2017-12-31)
Increased protein citrullination and peptidylarginine deiminases (PADIs), which catalyze the citrullination process, are central in Rheumatoid arthritis pathogenesis and probably involved in the initial steps towards autoimmunity. Approximately, 10% of RA patients develop clinically significantly ILD. A possible shared role
Seema Qamar et al.
Cell, 173(3), 720-734 (2018-04-21)
Reversible phase separation underpins the role of FUS in ribonucleoprotein granules and other membrane-free organelles and is, in part, driven by the intrinsically disordered low-complexity (LC) domain of FUS. Here, we report that cooperative cation-π interactions between tyrosines in the
Melissa M Ledet et al.
BMC cancer, 18(1), 412-412 (2018-04-14)
Mammary cancer is highly prevalent in dogs and cats and results in a poor prognosis due to critically lacking viable treatment options. Recent human and mouse studies have suggested that inhibiting peptidyl arginine deiminase enzymes (PAD) may be a novel
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