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AB6002

Sigma-Aldrich

Anti-MMP-1 Antibody, hinge region

from rabbit, purified by affinity chromatography

Synonym(s):

Fibroblast collagenase, Matrix metalloproteinase-1, matrix metallopeptidase 1, interstitial collagenase, matrix metalloprotease 1

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About This Item

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

biological source

rabbit

Quality Level

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

purified by

affinity chromatography

species reactivity

human

technique(s)

western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... MMP1(4312)

General description

All cells within tissues are surrounded by an extracellular matrix (ECM) giving the tissues shape and structure. The ECM is constantly being remodeled and constant communication is maintained between cells through this matrix. Secreted proteins, termed matrix metalloproteinases (MMPs), are involved in the modulation of cell matrix interactions. MMPs are Zn2+ binding endopeptidases that degrade various components of the ECM. MMPs are enzymes implicated in normal and pathologic tissue remodeling processes, wound healing, angiogenesis, and tumor invasion. These enzymes are very potent when active, and are associated with extracellular space inhibitors called TIMPs (tissue inhibitors of matrix metalloproteinases). MMP1, also known as interstitial collagenase, is the only enzyme able to initiate the breakdown of the interstitial collagens, types I, II, and III.

Specificity

Additional sequence homology is noted with mouse (81%) and rat (75%).
The antibody recognizes an internal domain of human MMP-1 containing the hinge region. It does not cross react with MMP-2, MMP-9, or MMP-13.

Immunogen

KLH-conjugated synthetic peptide corresponding to the hinge region of human MMP-1.

Application

Anti-MMP-1 Antibody, hinge region is an antibody against MMP-1 for use in WB.

Quality

Evaluated on a representative lot by Western blot on A431 cell lysate.

Western Blot Analysis: 0.5 µg/ml of this antibody detected MMP-1 on 10 µg of A431 cell lysate.

Target description

54 kDa In Western Blot, bands around 53 kDa and 51 kDa (proenzyme) are observed in reduced proteins.

Linkage

Replaces: 04-1122

Other Notes

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

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

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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Katherine Bleavins et al.
Biological trace element research, 145(2), 257-267 (2011-09-02)
The purpose of this study was to assess insoluble salts containing gadolinium (Gd(3+)) for effects on human dermal fibroblasts. Responses to insoluble Gd(3+) salts were compared to responses seen with Gd(3+) solubilized with organic chelators, as in the Gd(3+)-based contrast
Seniz Inanc et al.
BioTechniques, 63(4), 174-180 (2017-10-20)
Collagen zymography is an SDS-PAGE-based method for detecting both the proenzyme and active forms of collagenases. Although collagen zymography is used for assessment of the matrix metalloproteinases MMP-1 and MMP-13, it can be difficult to detect these collagenases due to
Xiaozhen Gu et al.
Cell death & disease, 10(9), 671-671 (2019-09-13)
Compromised learning and memory is a common feature of multiple neurodegenerative disorders. A paradigm spatial memory impairment could be caused by developmental lead (Pb) exposure. Growing evidence implicates epigenetic modifications in the Pb-mediated memory deficits; however, how histone modifications exemplified
Characterisation of genome-wide PLZF/RARA target genes.
Spicuglia, S; Vincent-Fabert, C; Benoukraf, T; Tiberi, G; Saurin, AJ; Zacarias-Cabeza et al.
Testing null
Ling Zhang et al.
Scientific reports, 8(1), 10041-10041 (2018-07-04)
Lysine-specific demethylase 1 (LSD1) exerts dual effects on histone H3, promoting transcriptional repression via Lys4 (H3K4) demethylation or transcriptional activation through Lys9 (H3K9) demethylation. These activities are often exerted at transcriptional start sites (TSSs) and depend on the type of

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