Human TIMP-1 Platinum ELISA

Also known as: Tissue inhibitor of metalloproteinases, EPA

RUO: For Research Use Only. Not for use in diagnostic procedures.

SKU# BMS2018*

Cat. No. Size
BMS2018 96 tests
BMS2018TEN 10 x 96 tests
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Data for Human TIMP-1 Platinum ELISA.

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  • Data for Human TIMP-1 Platinum ELISA.
Description

Description: The human TIMP-1 ELISA is an enzyme-linked immunosorbent assay for the quantitative detection of human tissue inhibitior of metallo-proteinase-1 (TIMP-1). The human TIMP-1 ELISA is for research use only. Not for diagnostic or therapeutic procedures.

The tissue inhibitions of metalloproteinases (TIMPs) are naturally occurring proteins that specifically inhibit matrix metalloproteinases, thus maintaining balance between matrix destruction and formation. An imbalance between MMPs and the associated TIMPs may play a significant role in the invasive phenotype of malignant tumors.

TIMP-1 has been shown to inhibit tumor-induced angiogenesis. An imbalance of MMP/TIMP regulation has been implicated in several inflammatory diseases of the nervous system. In the pathogenesis of vascular diseases TIMP-1 seems to be down regulated.

Details
Reactivity Human
Sample Volume 20 uL (1:100 prediluted)
Suitable Sample Types cell culture supernatant, serum, plasma (EDTA, heparin)
Sensitivity 10.0 pg/mL
Standard Curve Range 39 - 2,500 pg/mL
Expected Value 172 ng/ml
Components Aluminium pouch(es) with a Microwell Plate coated with monoclonal antibody to human TIMP-1
Biotin-Conjugate anti-human TIMP-1 polyclonal antibody
Streptavidin-HRP
Human TIMP-1 Standard lyophilized, 5 ng/ml upon reconstitution
Assay Buffer Concentrate 20x (PBS with 1% Tween 20 and 10% BSA)
Wash Buffer Concentrate 20x (PBS with 1% Tween 20)
Substrate Solution (tetramethyl-benzidine)
Stop Solution (1M Phosphoric acid)
Blue-Dye
Green-Dye
Red-Dye
Adhesive Films
Reported Applications ELISA
Documentation
TDS Link Download TDS
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References

References: Wojtowicz-Praga,S.M.; Dickson,R.B.; Hawkins,M.J.. Matrix metalloproteinase inhibitors. Invest New Drugs 1997;15:61-75. (Link)

Hornebeck,W.. Down-regulation of tissue inhibitor of matrix metalloprotease-1 (TIMP-1) in aged human skin contributes to matrix degradation and impaired cell growth and survival. Pathol.Biol.(Paris) 2003;51:569-573. (Link)

Yan,L.; Moses,M.A.. A case of tumor betrayal: biphasic effects of TIMP-1 on Burkitt's lymphoma. Am.J.Pathol. 2001;158:1185-1190. (Link)

Shin,W.S.; Szuba,A.; Rockson,S.G.. The role of chemokines in human cardiovascular pathology: enhanced biological insights. Atherosclerosis 2002;160:91-102. (Link)

Nagase,H.; Meng,Q.; Malinovskii,V.; Huang,W.; Chung,L.; Bode,W.; Maskos,K.; Brew,K.. Engineering of selective TIMPs. Ann.N.Y.Acad.Sci. 1999;878:1-11. (Link)

Thorgeirsson,U.P.; Lindsay,C.K.; Cottam,D.W.; Gomez,D.E.. Tumor invasion, proteolysis, and angiogenesis. J.Neurooncol. 1994;18:89-103. (Link)

Gardner,J.; Ghorpade,A.. Tissue inhibitor of metalloproteinase (TIMP)-1: the TIMPed balance of matrix metalloproteinases in the central nervous system. J.Neurosci.Res. 2003;74:801-806. (Link)

Arthur,M.J.; Iredale,J.P.. Hepatic lipocytes, TIMP-1 and liver fibrosis. J.R.Coll.Physicians Lond 1994;28:200-208. (Link)

Nagase,H.; Brew,K.. Designing TIMP (tissue inhibitor of metalloproteinases) variants that are selective metalloproteinase inhibitors. Biochem.Soc.Symp. 2003;201-212. (Link)


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