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ABT94

Sigma-Aldrich

Anti-Adam17 Antibody

serum, from rabbit

Synonym(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

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

biological source

rabbit

Quality Level

antibody form

serum

antibody product type

primary antibodies

clone

polyclonal

species reactivity

human

technique(s)

immunocytochemistry: suitable
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... ADAM17(6868)

General description

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.

Specificity

This antibody recognizes the cytoplasmic domain of Adam17.

Immunogen

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.).

Quality

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.

Target description

~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.).

Physical form

Rabbit polyclonal serum with 0.05% sodium azide.
Unpurified

Storage and Stability

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.

Analysis Note

Control
A431 cell lysate

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


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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