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Key Documents

SAB3500181

Sigma-Aldrich

Anti-ADAM10 antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

Anti-KUZ

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

predicted mol wt 85 kDa

species reactivity

human

technique(s)

immunocytochemistry: suitable
immunofluorescence: suitable
indirect ELISA: suitable
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... ADAM10(102)

General description

ADAM metallopeptidase domain 10 or A disintegrin and metalloprotease 10 (ADAM10) is a transmembrane protein which is widely distributed. It consists of an amino-terminal signal sequence, a prodomain, a metalloprotease domain, a disintegrin domain, a cysteine-rich region, a transmembrane region and a cytoplasmic tail. The gene encoding this protein is localized on human chromosome 15q21.3.

Immunogen

ADAM10 antibody was raised against a peptide corresponding to amino acids 732 to 748 of human ADAM10. This sequence is identical to those of bovine and rat origins and differs from that of mouse ADAM10 by one amino acid (2,4).

Biochem/physiol Actions

ADAM metallopeptidase domain 10 (ADAM10) activates Notch proteins and has a role in embryonic development. It functions as a molecular scissor and cleaves the extracellular domains of proteins. The protein is a therapeutic target for a variety of diseases and malignancies.

Features and Benefits

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Linkage

The action of this antibody can be blocked using blocking peptide SBP3500181.

Physical form

Supplied in PBS with 0.02% sodium azide.

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 Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Elizabeth Spangenberg et al.
Nature communications, 10(1), 3758-3758 (2019-08-23)
Many risk genes for the development of Alzheimer's disease (AD) are exclusively or highly expressed in myeloid cells. Microglia are dependent on colony-stimulating factor 1 receptor (CSF1R) signaling for their survival. We designed and synthesized a highly selective brain-penetrant CSF1R
Johannes Steffen et al.
Acta neuropathologica communications, 5(1), 49-49 (2017-06-24)
Amyloid-β (Aβ) deposition is one of the hallmarks of the amyloid hypothesis in Alzheimer's disease (AD). Mouse models using APP-transgene overexpression to generate amyloid plaques have shown to model only certain parts of the disease. The extent to which the
Yasumori Sobue et al.
Scientific reports, 9(1), 14901-14901 (2019-10-19)
CD44 fragmentation is enhanced in chondrocytes of osteoarthritis (OA) patients. We hypothesized that mechanical stress-induced enhancement of CD44-intracellular domain (CD44-ICD) production plays an important role in the de-differentiation of chondrocytes and OA. This study aimed to assess the relationship between
Zichen Li et al.
Cancer science, 108(3), 347-353 (2016-12-18)
An artificial receptor for proMMP-9 was created by fusing tissue inhibitor of MMP-1 (TIMP-1) with type II transmembrane mosaic serine protease (MSP-T1). Expression of MSP-T1 in 293T cells induced binding of proMMP-9, which was processed by MMP-2 activated by membrane
Tomonori Kobayakawa et al.
Biochemical and biophysical research communications, 478(3), 1230-1235 (2016-08-23)
Although excessive mechanical stress loading is known to induce articular cartilage degradation, the mechanism underlying this process is unclear. The interaction between hyaluronan (HA) and its primary receptor CD44 maintains the homeostasis of articular chondrocytes. CD44 cleavage and the generation

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