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AV53618

Sigma-Aldrich

Anti-ADAM7 antibody produced in rabbit

affinity isolated antibody

Synonym(s):

Anti-ADAM metallopeptidase domain 7, Anti-EAPI, Anti-GP-83

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100 μL
$541.00

About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

$541.00


Usually ships in 5 business days. (Orders outside of US, please allow an additional 1-2 weeks for delivery)

Notify Me

Get notified when this item is ready to ship via email.

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

83 kDa

species reactivity

human

concentration

0.5 mg - 1 mg/mL

technique(s)

western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... ADAM7(8756)

General description

ADAM7 (ADAM metallopeptidase domain 7) gene encodes a single-pass type I membrane protein that belongs to ADAMs family of zinc proteases and is expressed in melanoma cells. It has a role in epididymosomes and is an integral plasma membrane protein in sperm that has unique secretory feature and interactive relationship during epididymis-to-sperm transfer process. Mutation in ADAM7 gene results in melanoma progression.

Immunogen

Synthetic peptide directed towards the C terminal region of human ADAM7

Application

Anti-ADAM7 antibody produced in rabbit is suitable for western blotting at a concentration of 1μg/mL.

Biochem/physiol Actions

Adam7 resides in an intracellular compartment of epididymal cells and is transferred to sperm membranes, where its levels are dependent on the expression of Adam2 and Adam3, which play critical roles in fertilization. It functions in fertilization through the formation of a chaperone complex and enhances association with integral membrane protein 2B (Itm2b) during capacitation in sperm. It also helps in the maturation of sperm cells in mammals and also plays a unique secretory feature and interactive relationship with sperm.

Sequence

Synthetic peptide located within the following region: PTETLGVENKGYFGDEQQIRTEPILPEIHFLNKPASKDSRGIADPNQSAK

Physical form

Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

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 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Jungsu Oh et al.
Biochemical and biophysical research communications, 331(4), 1374-1383 (2005-05-11)
The mammalian epididymis is critical for sperm to acquire motility and fertilizing capacity. This maturation process involves the interaction of epididymal secretory proteins with sperm. We analyzed mouse a disintegrin and metalloprotease (ADAMs) 7 and 28 expressed specifically or predominantly
Jeong Su Oh et al.
Molecules and cells, 28(5), 441-446 (2009-10-27)
During epididymal transit, mammalian sperm acquire selected proteins secreted by the epididymis. We previously showed that a disintegrin and metalloprotease (ADAM) 7 is expressed specifically in the epididymis and transferred to the sperm surface during epididymal transit. Here, we show
Cecil Han et al.
Journal of cellular physiology, 226(5), 1186-1195 (2010-10-15)
In mammals, sperm acquire their motility and ability to fertilize eggs in the epididymis. This maturation process involves the acquisition of particular proteins from the epididymis. One such secretory protein specifically expressed in the epididymis is Adam7 (a disintegrin and
Xiaomu Wei et al.
Human mutation, 32(6), E2148-E2175 (2011-05-28)
We performed a mutational analysis of the 19 disintegrin-metalloproteinases (ADAMs) genes in human cutaneous metastatic melanoma and identified eight to be somatically mutated in 79 samples, affecting 34% of the melanoma tumors analyzed. Functional analysis of the two frequently mutated

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