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M8683

Sigma-Aldrich

Anti-Matrix Metalloproteinase-7, N-Terminal of Catalytic Zinc Site antibody produced in rabbit

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

Synonym(s):

Anti-MMP-7

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About This Item

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

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous glycerol solution

mol wt

antigen (active form) 18 kDa (reduced)
antigen (pro-form) 28 kDa

species reactivity

human

concentration

~1 mg/mL

technique(s)

immunohistochemistry: suitable
immunoprecipitation (IP): suitable
indirect ELISA: suitable
western blot: 1:1,000

UniProt accession no.

shipped in

wet ice

Storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... MMP7(4316)

General description

Matrix metallopeptidase 7 (MMP-7) is also known as matrilysin and expressed in tumor cells. It possesses many α-helices and β-sheets, with an active domain. The gene is localized on human chromosome 11q21-q22.

Specificity

Reacts with reduced and non-reduced MMP-7.

Immunogen

synthetic peptide corresponding to the N-terminal end of the catalytic zinc site of human matrix metalloproteinase-7 (matrilysin, PUMP).

Application

Anti-matrix metalloproteinase-7, N-terminal of catalytic zinc site antibody produced in rabbit has been used in immunohistochemistry and Western blotting.[1]
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)

Biochem/physiol Actions

Matrix metallopeptidase 7 (MMP-7) is a proteolytic enzyme which acts on fibronectin, laminin and collagen type IV. It can also activate other metalloproteinases like MMP-2 and MMP-9. MMP-7 plays an important role in the growth of cancerous cells.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 50% glycerol and 15 mM 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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Saeed Soleyman-Jahi et al.
PloS one, 10(4), e0122316-e0122316 (2015-04-29)
The prognostic role of matrix metalloproteinase-7 in gastric cancer survival has been widely evaluated. However, the results are controversial. We aimed to set up a meta-analysis to reach a conclusion on the prognostic significance of metalloproteinase-7 in gastric cancer survival
Hideaki Nagase et al.
Cardiovascular research, 69(3), 562-573 (2006-01-13)
Matrix metalloproteinases (MMPs), also called matrixins, function in the extracellular environment of cells and degrade both matrix and non-matrix proteins. They play central roles in morphogenesis, wound healing, tissue repair and remodelling in response to injury, e.g. after myocardial infarction
Ji-Chang Han et al.
World journal of surgical oncology, 13, 5-5 (2015-01-16)
Matrix metalloproteinase 7 (MMP-7) promotes tumor invasion and metastasis in several cancers. However, its role in lung cancer progression is understudied. In this study, we investigated the correlation between MMP-7 expression and lung cancer pathology. We searched the databases PubMed
Soo Jin Jung et al.
The world journal of men's health, 31(1), 36-46 (2013-05-10)
To investigate the relationships among the Wnt/β-catenin pathway, androgen receptor (AR), and clinicopathological factors in hormone-naïve prostate cancer. This study was conducted with132 cases of hormone-naïve prostate cancer treated by prostatectomy and prostate needle biopsy. An immunohistochemical study using antibodies
Takao Ide et al.
International journal of cancer, 119(12), 2750-2759 (2006-09-26)
The hypoxic environment in tumor is reported to play an important role in pancreatic cancer progression. The interaction between stromal and cancer cells also contributes to the malignant behavior of pancreatic cancer. In the present study, we investigated whether hypoxic

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