M8683
Anti-Matrix Metalloproteinase-7, N-Terminal of Catalytic Zinc Site antibody produced in rabbit
~1 mg/mL, affinity isolated antibody, buffered aqueous glycerol solution
别名:
Anti-MMP-7
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关于此项目
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ELISA (i), IHC, IP, WB
Citations:
7
biological source
rabbit
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
Quality Level
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.
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.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)
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.
Reacts with reduced and non-reduced MMP-7.
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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存储类别
10 - Combustible liquids
法规信息
新产品
此项目有
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
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
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
Takayuki Shiomi et al.
Laboratory investigation; a journal of technical methods and pathology, 85(12), 1489-1506 (2005-10-04)
Matrix metalloproteinase-7 (MMP-7) (also known as matrilysin-1) is secreted as a proenzyme (proMMP-7) and plays a key role in the degradation of various extracellular matrix (ECM) and non-ECM molecules after activation. To identify the binding proteins related to proMMP-7 activation
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
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