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MAB3369

Sigma-Aldrich

Anti-MMP-3 Antibody, clone SL-1 IID4

clone SL-1 IID4, Chemicon®, from mouse

Synonym(s):

Stromelysin-1, Transin, Proteoglycanase

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

100

antibody form

purified antibody

antibody product type

primary antibodies

clone

SL-1 IID4, monoclonal

species reactivity

human

manufacturer/tradename

Chemicon®

technique(s)

ELISA: suitable
immunohistochemistry: suitable (paraffin)
immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgG2b

NCBI accession no.

NM_002422.3

UniProt accession no.

P08254

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... MMP3(4314)

General description

MMPs are frequently expressed in malignant neoplastic cells and play crucial roles in tumor invasion and metastasis. Tissue inhibitors of matrix metalloproteinases (TIMPs) control the activitiy of MMPS. The tissue distribution of three major MMPs has been defined in human mammary pathology: 1) collagenase (MMP-1) which degrades fibrillar interstitial collagens; 2) a 72-k/Da gelatinase (MMP-2) which mainly degrades type IV collagen and denatured collagens; and 3) stromelysin (MMP-3) which has a wider range of action, degrading several matrix components including the core proteins of proteoglycans, laminin and non-helical regions of collagens.

Specificity

MAB3369 recognizes one doublet of 54kDa/59kDa and another doublet of 44kDa/49kDa, which are identified as unglycosylated and glycosylated species of pro (latent) and active forms of matrix metalloproteinase-3 (MMP-3; also known as Stromelysin-1 of Transin). MAB3369 shows no cross-reaction with the pro and active forms of other MMPs.

CELLULAR LOCALIZATION:

Cytoplasmic

Immunogen

APMA (4-Aminophenylmercuric acetate) activated Human stromelysin-1

Application

Anti-MMP-3 Antibody, clone SL-1 IID4 is an antibody against MMP-3 for use in ELISA, IP, WB, IH(P).
Immunofluorescence

Immunoprecipitation (Use Protein A): 2μg/ml protein lysate.

Western blotting: 0.5-1.0 μg/ml for 2hrs at RT

Immunohistology (frozen & formalin-fixed): 10-20 μg/ml for 60 minute at room temperature. No special pretreatment is required for staining of formalin-fixed, paraffin-embedded tissue sections.

Optimal working dilutions and protocols must be determined by end user.
Research Category
Cell Structure
Research Sub Category
MMPs & TIMPs

Physical form

Format: Purified
Purified from ascites fluid by Protein A chromatography. 10mM PBS, pH 7.4, with 0.2% BSA and 0.09% sodium azide.

Storage and Stability

Antibody with sodium azide is stable for 12 months when stored at 2-8°C.

Analysis Note

Control
POSTIVE CONTROL:

Human endometrium cells, placenta, bladder, breast, ovarian carcinomas.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Adel Ghoul et al.
Folia histochemica et cytobiologica, 55(2), 62-73 (2017-06-22)
Elevated plasma homocysteine (Hcy) levels have been associated with several tissue injuries including heart and liver fibrosis. In these diseases, hyperhomocysteinemia (Hhcy) plays a major role in modulating the alteration of the balance between matrix metalloproteinases (MMP) and tissue inhibitors
Asha Shahed et al.
Molecular reproduction and development, 75(9), 1433-1440 (2008-01-24)
Siberian hamsters adapt to seasonal changes by reducing their reproductive function during short days (SD). SD exposure reduces uterine mass and reproductive capacity, but underlying cellular mechanisms remain unknown. Because matrix metalloproteinases (MMPs) and their tissue inhibitors (TIMPs) are important
Yuehua Ma et al.
Journal of cellular physiology, 234(12), 22260-22271 (2019-05-14)
To better understand the molecular mechanisms of anaplastic thyroid carcinoma (ATC), we aimed to identify the hub genes specifically involved in ATC by integrated bioinformatics analysis. In this study, using three Gene Expression Omnibus data sets with the same platform
Ioanna S Sougleri et al.
The FEBS journal, 283(2), 206-220 (2016-02-26)
As a result of Helicobacter pylori adhesion to gastric epithelial cells, the bacterial effector cytotoxin-associated gene A (CagA) is translocated intracellularly, and after hierarchical tyrosine phosphorylation on multiple EPIYA motifs, de-regulates cellular polarity and contributes to induction of an elongation
Yuan Jiang et al.
The Journal of biological chemistry, 293(50), 19317-19329 (2018-10-20)
Human pluripotent stem cells hold great promise for improving regenerative medicine. However, a risk for tumor formation and difficulties in generating large amounts of subtype derivatives remain the major obstacles for clinical applications of stem cells. Here, we discovered that

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