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AB6002

Sigma-Aldrich

Anti-MMP-1 Antibody, hinge region

from rabbit, purified by affinity chromatography

Synonym(e):

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

Biologische Quelle

rabbit

Qualitätsniveau

Antikörperform

affinity isolated antibody

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Aufgereinigt durch

affinity chromatography

Speziesreaktivität

human

Methode(n)

western blot: suitable

NCBI-Hinterlegungsnummer

UniProt-Hinterlegungsnummer

Versandbedingung

wet ice

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... MMP1(4312)

Allgemeine Beschreibung

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.

Spezifität

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.

Anwendung

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

Qualität

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.

Zielbeschreibung

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

Verlinkung

Replaces: 04-1122

Sonstige Hinweise

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

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Lagerklassenschlüssel

12 - Non Combustible Liquids

WGK

WGK 1

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

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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
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
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
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Spicuglia, S; Vincent-Fabert, C; Benoukraf, T; Tiberi, G; Saurin, AJ; Zacarias-Cabeza et al.
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