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RAB1020

Sigma-Aldrich

Human ADAMTS4 ELISA Kit

for cell culture supernatants, plasma, and serum samples

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About This Item

UNSPSC Code:
41116158
NACRES:
NA.32

species reactivity

human

packaging

kit of 96 wells (12 strips x 8 wells)

technique(s)

ELISA: suitable

input

sample type serum sample(s)
sample type plasma
sample type cell culture supernatant(s)

assay range

inter-assay cv: <12%
intra-assay cv: <10%
sensitivity: 0.12 ng/ml

detection method

colorimetric

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... ADAMTS4(9507)

General description

Human a disintegrin and metalloproteinase with thrombospondin motifs 4 (ADAMTS4) enzyme-linked immunosorbent assay (ELISA) kit is an in vitro ELISA kit for the quantitative measurement of a human ADAMTS4 in biological samples, such as serum, plasma, cell culture supernatants, urine, and/or cell and tissue lysates. ADAMTS4 is a multidomain metalloproteinase that can inhibit the activity of aggrecan. It belongs to the ADAMTS family. ADAMTS4 is made up of a pro-domain, a catalytic metalloproteinase domain, a disintegrin-like (Dis) domain, a thrombospondin type I (TS) domain. It also contains a cysteine-rich (CysR) domain and a spacer (Sp) domain. ADAMTS4 gene is located on the human chromosome at 1q23.3.
This ELISA antibody pair detects Human ADAMTS-4

Application

For research use only. Not for use in diagnostic procedures.
Please refer to the attached Protocolfor details.

Other Notes

A sample Certificate of Analysis is available for this product. Please type the word sample in the text box provided for lot number.

pictograms

Corrosion

signalword

Warning

hcodes

Hazard Classifications

Met. Corr. 1

Storage Class

8A - Combustible corrosive hazardous materials

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

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Single-nucleotide polymorphisms in the coding region of a disintegrin and metalloproteinase with thrombospondin motifs 4 and hepatocellular carcinoma: A retrospective case-control study
Wang X Z, et al.
Cancer Medicine, 8(18), 7869-7880 (2019)
Functional differences of the catalytic and non-catalytic domains in human ADAMTS-4 and ADAMTS-5 in aggrecanolytic activity
Fushimi K, et al.
The Journal of Biological Chemistry, 283(11), 6706-6716 (2008)
Michael Stock et al.
Arthritis & rheumatology (Hoboken, N.J.), 69(6), 1233-1245 (2017-01-14)
Cartilage damage and subchondral bone changes are closely connected in osteoarthritis. Nevertheless, how these processes are interlinked is, to date, incompletely understood. This study was undertaken to investigate the mechanistic role of a cartilage-derived protein, upper zone of growth plate
Jianjun Chen et al.
Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology, 46(4), 1693-1703 (2018-04-26)
ADAMTSs (A disintegrin and metalloprotease domains with thrombospondins motifs) are a family of extracellular proteases that have been related to both oncogenic and tumor-suppressive functions. The aim of the present study was to investigate: 1) the mutation, copy-number alterations, and
Guping Mao et al.
Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology, 44(1), 38-52 (2017-12-15)
Aggrecanase-1 (ADAMTS-4) and aggrecanase-2 (ADAMTS-5) are secreted enzymes belonging to the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) family that play significant roles in the progression of osteoarthritis (OA). Here, we aimed to determine whether the expression of ADAMTS-4/5

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