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MAB1810

Sigma-Aldrich

Anti-ADAMTS-1 Antibody, clone 5D4E11B6

serum, clone 5D4E11B6, Chemicon®

Sinónimos:

METH-1

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About This Item

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

biological source

mouse

Quality Level

antibody form

serum

antibody product type

primary antibodies

clone

5D4E11B6, monoclonal

species reactivity

human, mouse, rat

manufacturer/tradename

Chemicon®

technique(s)

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

isotype

IgG

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... ADAMTS1(9510)

General description

ADAMTS-1 is a member of a family of extracellular proteases known as ADAMTS (a disintegrin and metalloprotease with thrombospondin motifs). Members of the ADAMTS family share distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TSP) motif. Individual members of this family differ in the number of C-terminal TSP motifs, and some have unique C-terminal domains. The protein encoded by this gene contains two disintegrin loops and three C-terminal TSP motifs. ADAMTS-1 cleaves aggrecan, a cartilage proteoglycan and appears to demonstrate angiogenesis inhibitory activity. The maturation of ADAMTS-1 requires two independent and sequential processing events that may release two forms of the protein. With the cleavage of the prodomain from the 110 kDa zymogen, an 87 kDa active form remains which can be further processed by removal of the catalytic subunit from the TSP repeats, leaving the C-termianl 65 kDa soluble form. The proteolytic deletion of the last two TSP repeats, is probably significant for the in vivo function of this protein.

Specificity

Clone 5D4E11B6 recognizes human ADAMTS-1.
Reactivity with other species has not been tested.

Immunogen

Myc-His carboxyl tagged full-length recombinant protein based on the human sequence.

Application

Detect ADAMTS-1 using this Anti-ADAMTS-1 Antibody, clone 5D4E11B6 validated for use in ELISA, IP & WB.
Western blot: 1:2000 - 1:4000 dilution on A431 cell lysate

Note: MW bands detected vary by cell line or sample with detection of zymogen and/or active forms.

Immunoprecipitation: confirm by immunoblot using clone 5D4E11B6; 1:50 using clone 5C6D5 (Catalog # MAB1771) to immunoprecipitate ADAMTS-1 from 500 µg of HEK293 whole cell lysate or PC-12 whole cell lysate

Target description

110 / 87 / 65 kDa

Physical form

Ascites. Liquid containing 0.05% NaN3.

Analysis Note

Control
A431 cell lysate

HEK293 cell lysate

PC-12 cell lysate

Embryonic mouse brain lysate

MCF-7 cell lysate

Legal Information

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

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Storage Class

12 - Non Combustible Liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


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Yunjie Qiu et al.
Frontiers in aging neuroscience, 14, 896522-896522 (2022-08-27)
Amyloid-β (Aβ) derived from amyloid precursor protein (APP) hydrolysis is acknowledged as the predominant hallmark of Alzheimer's disease (AD) that especially correlates to genetics and daily activities. In 2019, meta-analysis of AD has discovered five new risk loci among which
Tie-Gang Meng et al.
Cell death & disease, 8(6), e2846-e2846 (2017-06-02)
The process of follicular development involves communications between oocyte and surrounding granulosa cells. FURIN is a member of the family of proprotein convertases that is involved in the activation of a large number of zymogens and proproteins by cleavage at
Maíra de Assis Lima et al.
Cellular signalling, 77, 109827-109827 (2020-11-09)
ADAMTSs (A Disintegrin And Metalloproteinase with ThromboSpondin motifs) are secreted proteases dependent on Zn2+/Ca2+, involved in physiological and pathological processes and are part of the extracellular matrix (ECM). Here, we investigated if ADAMTS-1 is required for invasion and migration of
Suély V Silva et al.
PloS one, 11(10), e0165061-e0165061 (2016-10-21)
Proteins secreted in the extracellular matrix microenvironment (ECM) by tumor cells are involved in cell adhesion, motility, intercellular communication and invasion. The tumor microenvironment is expansively modified and remodeled by proteases, resulting in important changes in both cell-cell and cell-ECM

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