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Key Documents

ABT94

Sigma-Aldrich

Anti-Adam17 Antibody

serum, from rabbit

Synonyme(s) :

Disintegrin and metalloproteinase domain-containing protein 17, ADAM 17, TNF-alpha convertase, TNF-alpha-converting enzyme, CD156b

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About This Item

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

Source biologique

rabbit

Niveau de qualité

Forme d'anticorps

serum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Espèces réactives

human

Technique(s)

immunocytochemistry: suitable
western blot: suitable

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... ADAM17(6868)

Description générale

ADAM17, also known as TNF-alpha Convertase, or TACE, was first cloned from human epithelial cells. Tumor-necrosis factor alpha is a proinflammatory cytokine and contributes to a variety of inflammatory disease responses and programmed cell death. TNF-alpha is synthesized as a 26 kDa Type II membrane-bound precursor that is cleaved by a convertase to generate secreted 17K mature TNF-alpha. TNF-alpha converting enzyme (TACE) protein was recently purified and the human and mouse TACE cDNAs were cloned by several groups separately. The ADAM proteins are structurally similar, with a signal sequence, metalloprotease domain (inactive in some ADAMs), disintegrin domain, cystein rich domain, EGF like repeat, type I transmembrane, and a cytoplasmic domain. A member of the metalloproteinase family containing disintegrin like domains (ADAMs), ADAM17 is known to process the TNF alpha trimer from the membrane attached precursor to the soluble form. ADAM17 contains the canonical HExxHxxxxxH zinc metallo-proteinase motif, and has been shown to be proteolytically active, cleaving TNF precursor as well as TNF p75 receptor, myeloid precursor protein, amyloid plaque protein, L selectin and TGF alpha, making ADAM17 a "sheddase". Reports have shown that ADAM17 expression in human breast tumor samples is an indicator of poor prognosis.

Spécificité

This antibody recognizes the cytoplasmic domain of Adam17.

Immunogène

Epitope: Cytoplasmic domain
GST-tagged recombinant protein corresponding to the cytoplasmic domain of mouse Adam17.

Application

Anti-Adam17 Antibody is a highly specific rabbit polyclonal antibody, that targets ADAM 17 & has been tested in western blotting & ICC.
Research Category
Cell Structure
Research Sub Category
ECM Proteins
Western Blotting Analysis: A 1:1,000 dilution of this antibody detected Adam17 in 10 µg of the following cell lysates--C2C12, HEK293, HeLa, HepG2, HUVEC, L6, NIH/3T3, PC12, and PC3.

Western Blotting Analysis: A representative lot detected pro-form and the truncated, mature form of Adam17 in COS cell lysates (Schlondorff, J., et al. (2000) Biochem J. 1(347):131-138.).

Western Blotting Analysis: A representative lot detected Adam17 in COS-7 cell lysates (Zheng, Y., et al. (2002). J Biol Chem. 277(45):42463-42470.).

Western Blotting Analysis: A representative lot detected the Pro-form and the truncated. mature form of Adam17 in COS-7 cell lysates (Le Gall, S. M., et al. (2010). J Cell Sci. 123(22):3913-3922.).

Qualité

Evaluated by Western Blotting in A431 cell lysate.

Western Blotting Analysis: A 1:1,000 dilution of this antibody detected Adam17 in 10 µg of A431 cell lysate.

Description de la cible

~120 kDa and ~100 kDa observed. The pro-form and the truncated, mature form of Adam17 may be observed at 120 kDa and 100 kDa, respectively (Schlondorff, J., et al. (2000) Biochem J. 1(347):131-138.; Le Gall, S. M., et al. (2010). J Cell Sci. 123(22):3913-3922.).

Forme physique

Rabbit polyclonal serum with 0.05% sodium azide.
Unpurified

Stockage et stabilité

Stable for 1 year at -20°C from date of receipt.
Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.

Remarque sur l'analyse

Control
A431 cell lysate

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1


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Consulter la Bibliothèque de documents

Sylvain M Le Gall et al.
Journal of cell science, 123(Pt 22), 3913-3922 (2010-10-29)
Protein ectodomain shedding is crucial for cell-cell interactions because it controls the bioavailability of soluble tumor necrosis factor-α (TNFα) and ligands of the epidermal growth factor (EGF) receptor, and the release of many other membrane proteins. Various stimuli can rapidly
Yufang Zheng et al.
The Journal of biological chemistry, 277(45), 42463-42470 (2002-09-19)
Tumor necrosis factor alpha-convertase (TACE) is a metalloprotease-disintegrin involved in the ectodomain shedding of several proteins and is critical for proper murine development. TACE-mediated ectodomain shedding is regulated, and the cytoplasmic domain of TACE contains several potential signaling motifs, suggesting
J Schlöndorff et al.
The Biochemical journal, 347 Pt 1, 131-138 (2000-03-23)
Tumour necrosis factor alpha convertase (TACE) is a metalloprotease/disintegrin involved in the ectodomain shedding of several proteins, a process thought to be important in inflammation, rheumatoid arthritis and murine development. The characterization of the intracellular maturation and subcellular localization of
Motoko Niida-Kawaguchi et al.
Neuropathology : official journal of the Japanese Society of Neuropathology, 40(2), 152-166 (2019-12-29)
Previous studies on sporadic amyotrophic lateral sclerosis (SALS) demonstrated iron accumulation in the spinal cord and increased glutamate concentration in the cerebrospinal fluid. To clarify the relationship between the two phenomena, we first performed quantitative and morphological analyses of substances

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