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A3476

Sigma-Aldrich

Anti-ADAM-19, Propeptide Domain antibody produced in rabbit

~1 mg/mL, affinity isolated antibody, buffered aqueous glycerol solution

Synonym(s):

Anti-A Disintegrin And Metalloproteinase-19, Anti-Meltrin-β

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About This Item

MDL number:
UNSPSC Code:
12352203

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous glycerol solution

species reactivity

human

concentration

~1 mg/mL

technique(s)

western blot: 1:1,000

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... ADAM19(8728)

General description

ADAM19 or Meltrin-beta belongs to the ADAM (a disintegrin and metalloprotease-like domain) family. ADAM19 is found in muscle, bone, muscle, lung, heart, brain, kidney, and several other cells. This protein shares homology with the fertilins (ADAMs 1 and 2). Studies have reported that ADAM19 is involved in myoblast fusion, similar to sperm-egg fusion aided by ADAMs 1 and 2. Furthermore, ADAM19 has been implicated in osteoblast and dendritic cell differentiation, as well as in the intracellular processing of neuregulin.
Rabbit anti-ADAM-19, propeptide domain antibody localizes human ADAM19. By immunoblotting against the reduced protein, the antibody recognizes bands at 95kDa, 84kDa (major band), and breakdown products at 50kDa and 34kDa from cell lysates. A strong band at 30kDa is often seen, which is probably the propeptide domain cleaved after furin activation of ADAM19.

Immunogen

synthetic peptide corresponding to the propeptide domain of human ADAM-19.

Application

Rabbit anti-ADAM-19, propeptide domain antibody can be used for western blotting assays at 1:1000.

Physical form

Solution in 0.01 M phosphate buffered saline containing 50% glycerol and 0.05% 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

10 - Combustible liquids


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K Kurohara et al.
Biochemical and biophysical research communications, 270(2), 522-527 (2001-02-07)
Meltrin beta (ADAM19) is a member of the metalloprotease-disintegrin family. We report here chromosomal mapping of the mouse and rat meltrin beta genes and cloning and analysis of the mouse upstream regulatory regions. The meltrin beta transcript shows a spatially
J Fritsche et al.
Blood, 96(2), 732-739 (2000-07-11)
The 1alpha,25-dihydroxyvitamin D(3) (1,25- [OH](2)VD(3)) modulates the differentiation of monocytic cell lines and monocytes (MOs) in vitro. Up to now several target genes of 1,25(OH)(2)VD(3) have been described in monocytic cell lines; however, little is known about target genes in
K Shirakabe et al.
The Journal of biological chemistry, 276(12), 9352-9358 (2000-12-26)
Meltrin beta/ADAM19 is a member of ADAMs (a disintegrin and metalloproteases), which are a family of membrane-anchored glycoproteins that play important roles in fertilization, myoblast fusion, neurogenesis, and proteolytic processing of several membrane-anchored proteins. The expression pattern of meltrin beta
D Inoue et al.
The Journal of biological chemistry, 273(7), 4180-4187 (1998-03-28)
Here we report the cloning and initial biochemical characterization of the mouse metalloprotease/disintegrin/cysteine-rich (MDC) protein meltrin beta and the analysis of the mRNA expression of four MDC genes (meltrin alpha, meltrin beta, mdc9, and mdc15) in bone cells, including osteoclasts
P Wei et al.
Biochemical and biophysical research communications, 280(3), 744-755 (2001-02-13)
The adamalysins are involved in proteolysis, adhesion, fusion, and intracellular signaling. Human ADAM19/adamalysin-19 (A disintegrin and metalloproteinase 19) was identified from primary dendritic cell cDNA libraries. It has a signal sequence, a pro-domain with a "cysteine-switch" residue, a metalloproteinase domain

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