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Merck
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07-377

Sigma-Aldrich

Anti-Citrulline Antibody

Upstate®, from rabbit

Sinónimos:

Anti-Citrulline

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

purified by

affinity chromatography

species reactivity

human, vertebrates, mouse

manufacturer/tradename

Upstate®

technique(s)

immunohistochemistry: suitable
western blot: suitable

isotype

IgG

shipped in

wet ice

target post-translational modification

unmodified

General description

The amino acid Citrulline is required to detoxify the liver from ammonia, which is a waste product of the body from oxidation. Citrulline promotes energy and assists with the immune system. This unusual amino acid is formed in the urea cycle by the addition of carbon dioxide and ammonia to ornithine. It is then combined with aspartic acid to form arginosuccinic acid, which later is metabolized into the amino acid arginine.

Specificity

Multiple deiminated keratins in human cornified skin. Thought to react preferentially with citrulline residues in glycine rich contexts.

Immunogen

Linear peptide containing Citrulline.

Application

Detect Citrulline with Anti-Citrulline Antibody (Rabbit Polyclonal Antibody), that has been shown to work in WB & IHC.
Research Category
Inflammation & Immunology
Research Sub Category
General Post-translation Modification

Quality

routinely evaluated by immunoblot in whole cell lysates from tape-stripped human outer cornified layers

Target description

43-65 kDa

Physical form

25mM Tris/Tris-HCl, pH 7.4, 137mM NaCl,2.7mM KCl, 0.02% sodium azide before the addition of glycerol to 30%
ImmunoAffinity Purified

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Analysis Note

Control
Human outer cornified layer whole cell lysate

Legal Information

UPSTATE 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.

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Storage Class

10 - Combustible liquids

wgk_germany

WGK 1


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Hans-Georg Kopp et al.
The Journal of clinical investigation, 116(12), 3277-3291 (2006-12-05)
Thrombopoietic cells may differentially promote or inhibit tissue vascularization by releasing both pro- and antiangiogenic factors. However, the molecular determinants controlling the angiogenic phenotype of thrombopoietic cells remain unknown. Here, we show that expression and release of thrombospondins (TSPs) by
Yi-Fang Yang et al.
Cellular & molecular biology letters, 27(1), 19-19 (2022-03-04)
Peptididylarginine deiminase type 2 (PADI2) catalyzes the conversion of arginine residues to citrulline residues on proteins. We demonstrate that PADI2 induces T cell activation and investigate how PADI2 promotes activated T cell autonomous death (ACAD). In activated Jurkat T cells
A Ishida-Yamamoto et al.
The Journal of investigative dermatology, 114(4), 701-705 (2000-03-25)
Citrulline-containing proteins, mainly originating from keratin K1 and formed by enzymatic deimination of arginine residues, have been identified in the cornified layers of human epidermis. We analyzed the localization and nature of the deiminated proteins in psoriatic epidermis. Immunostaining based
T Senshu et al.
Journal of dermatological science, 21(2), 113-126 (1999-10-08)
Citrulline residues are detected in keratins and filaggrin in the cornified layers of mammalian epidermis. Such citrulline residues are formed by the enzymatic deimination of arginine residues by peptidylarginine deiminases (EC 3.5.3.15). Major deiminated keratins are derived from keratin K1.
T Senshu et al.
Biochemical and biophysical research communications, 225(3), 712-719 (1996-08-23)
The upper layers of mammalian epidermis contain citrulline-containing proteins formed by enzymatic deimination of arginine residues. To study the role of protein deimination in epidermal differentiation, we identified deiminated proteins extracted from human epidermis. Major deiminated proteins were identified as

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