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종 반응성
human
기술
ELISA: suitable
입력
sample type serum
sample type plasma
sample type cell culture supernatant(s)
assay range
inter-assay cv: <12%
intra-assay cv: <10%
배송 상태
wet ice
저장 온도
−20°C
유전자 정보
human ... CTSZ(1522)
일반 설명
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.[1][2] Cathepsin Z is a cysteine protease, predominantly expressed in immune cells including monocytes, macrophages or dendritic cells.[3][4][5]
This ELISA antibody pair detects Human Cathepsin Z (CTSZ/Cathepsin X/Cathepsin P)
애플리케이션
For research use only. Not for use in diagnostic procedures.
Please refer to the attached Protocolfor details.
Please refer to the attached Protocolfor details.
생화학적/생리학적 작용
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.[6] 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.[3][4][5]
기타 정보
A sample Certificate of Analysis is available for this product. Please type the word sample in the text box provided for lot number.
신호어
Warning
유해 및 위험 성명서
예방조치 성명서
Hazard Classifications
Met. Corr. 1
Storage Class Code
8A - Combustible corrosive hazardous materials
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
가장 최신 버전 중 하나를 선택하세요:
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)
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)
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)
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
활성 필터
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