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MAB3317

Sigma-Aldrich

Anti-MMP-14 Antibody, hemopexin domain, clone 113-5B7

clone 113-5B7, Chemicon®, from mouse

Synonym(s):

MT1-MMP

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About This Item

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

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

113-5B7, monoclonal

species reactivity

rat, human, bovine, mouse

manufacturer/tradename

Chemicon®

technique(s)

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

isotype

IgG3κ

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... MMP14(4323)

Specificity

Reacts with human MMP-14, also known as MT1-MMP, with a very slight cross-reactivity to hMMP-3. For unknown reasons this antibody does not react on westerns to CC1043.

Immunogen

CDGNFDTVAMLRGEM in the hemopexin-like domain of human MT1-MMP
Epitope: a.a. 319-333

Application

Anti-MMP-14 Antibody, hemopexin domain, clone 113-5B7 is an antibody against MMP-14 for use in ELISA, IH(P) & WB.
Research Category
Cell Structure
Research Sub Category
MMPs & TIMPs
Western Blot: 10 μg/mL, membrane preparations; MD-MB-231 cells pretreated with 1-5 μg/mL ConA for 24-48 hours as positive control. 60-65 kDa proteins are identified.


When tested against recombinant MT1-MMP (lacking the TM domain) expressed in CHO cells the antibody reacts with a band of ~59 kDa.


Immunohistochemistry: Frozen tissue sections; traditional formalin fixation is problematic. Paraffin-embedded tissue sections with PLP fixation required.


Immunoprecipitation


EIA


Optimal working dilutions must be determined by the end user.

Target description

~59-69 kDa

Physical form

Format: Purified
Protein A purified
Purified immunoglobulin. Liquid in 0.1 M sodium phosphate buffer, pH 7.0, containing 2% protease-free bovine Serum albumin.

Storage and Stability

Maintain for 1 year at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Analysis Note

Control
Breast carcinoma tissue

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.

Manufactured by Daiichi Fine Chemical Co., Ltd

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Storage Class

12 - Non Combustible Liquids

wgk_germany

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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Dynamic expression of matrix metalloproteinases (MMP-2, -9 and -14) and the tissue inhibitors of MMPs (TIMP-1, -2 and -3) at the implantation site during tubal pregnancy.
Bai, SX; Wang, YL; Qin, L; Xiao, ZJ; Herva, R; Piao, YS
Reproduction (Cambridge, England) null
Vasculostatin inhibits intracranial glioma growth and negatively regulates in vivo angiogenesis through a CD36-dependent mechanism.
Kaur, B; Cork, SM; Sandberg, EM; Devi, NS; Zhang, Z; Klenotic, PA; Febbraio, M; Shim et al.
Cancer Research null
White matter microglia produce membrane-type matrix metalloprotease, an activator of gelatinase A, in human brain tissues.
Yamada, T, et al.
Acta neuropathologica, 90, 421-424 (1995)
Carla S Ceron et al.
Matrix biology : journal of the International Society for Matrix Biology, 31(4), 261-270 (2012-02-22)
Increased vascular matrix metalloproteinases (MMPs) levels play a role in late phases of hypertensive vascular remodeling. However, no previous study has examined the time course of MMPs in the various phases of two-kidney, one-clip hypertension (2K1C). We examined structural vascular
Amit Ranjan et al.
BioMed research international, 2014, 804680-804680 (2014-09-03)
Matrix remodeling and invasion of basement membrane are the major determinants of malignant progression. Matrix degrading enzymes play a pivotal role in this process and have been shown to be regulated at multiple levels. Using high metastatic B16F10 and its

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