MAB3317
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
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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
Cell Structure
Research Sub Category
MMPs & TIMPs
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.
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
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
Manufactured by Daiichi Fine Chemical Co., Ltd
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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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