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RAB1320

Sigma-Aldrich

Human Cathepsin Z ELISA

for serum, plasma and cell culture supernatants

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About This Item

Código UNSPSC:
12352200

reatividade de espécies

human

técnica(s)

ELISA: suitable

entrada

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

assay range

inter-assay cv: <12%
intra-assay cv: <10%

Condições de expedição

wet ice

temperatura de armazenamento

−20°C

Informações sobre genes

human ... CTSZ(1522)

Descrição geral

Cathepsins are normally localized in lysosomes of almost all mammalian cells, but under certain conditions they can be secreted from the cells that take part in local proteolysis. Cathepsin Z is a cysteine protease, predominantly expressed in immune cells including monocytes, macrophages or dendritic cells.
This ELISA antibody pair detects Human Cathepsin Z (CTSZ/Cathepsin X/Cathepsin P)

Aplicação

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

Ações bioquímicas/fisiológicas

Cathepsins are lysosomal proteases that play an important role in the intracellular degradation of exogenous and endogenous proteins, activation of enzyme precursors, and tumor invasion and metastasis. Cathepsin Z is known to be associated with the pathogenesis of cancer and promotes the development and proliferation of tumor cells. Cathepsin Z mediates the process of proliferation, migration, maturation, adhesion, signal transduction and phagocytosis of immune cells.

Outras notas

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

Pictogramas

Corrosion

Palavra indicadora

Warning

Frases de perigo

Declarações de precaução

Classificações de perigo

Met. Corr. 1

Código de classe de armazenamento

8A - Combustible corrosive hazardous materials

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (COA)

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Cysteine cathepsins B and X promote epithelial-mesenchymal transition of tumor cells.
Mitrovic A, et al.
European Journal of Cell Biology, 96(6), 622-631 (2017)
Localization and activity of various lysosomal proteases in Leishmania amazonensis-infected macrophages.
Prina E R I C, et al.
Infection and Immunity, 58(6), 1730-1737 (1990)
Dysregulation of apoptotic signaling pathways by interaction of RPLP0 and cathepsin X/Z in gastric cancer.
Teller A, et al.
Pathology Research and Practice, 211(1), 62-70 (2015)
Cysteine cathepsins and the cutting edge of cancer invasion.
Gocheva V and Joyce J A
Cell Cycle, 6(1), 60-64 (2007)
L Polgár et al.
The Journal of biological chemistry, 262(30), 14448-14453 (1987-10-25)
Negatively charged reactants are sensitive reactivity probes of the active site of cysteine proteases (Halász, P., and Polgár, L. (1977) Eur. J. Biochem. 79, 491-494). Thus, the thiolate-imidazolium ion pair of papain reacts at an enhanced rate with iodoacetate due

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