219467
Cathepsin V, His•Tag®, Human, Recombinant, NSO Cells
Cathepsin V, His•Tag, is a recombinant human procathepsin V (aa 18-334) fused at the N-terminus to a CD33 signal sequence (aa 1-16) & at C-terminus to a His•Tag sequence & expressed in NSO cells.
Synonim(y):
Cathepsin L2, Cathepsin U
Zaloguj sięWyświetlanie cen organizacyjnych i kontraktowych
About This Item
Polecane produkty
rekombinowane
expressed in NSO cells
Poziom jakości
Próba
≥95% (SDS-PAGE)
Formularz
frozen liquid
aktywność właściwa
≥300 units/μg
producent / nazwa handlowa
Calbiochem®
warunki przechowywania
OK to freeze
avoid repeated freeze/thaw cycles
zanieczyszczenia
≤1.0 EU/μg Endotoxins (EU/μg Cathepsin V)
Warunki transportu
wet ice
temp. przechowywania
−70°C
Opis ogólny
Recombinant, human procathepsin V (amino acids 18-334) fused at the N-terminus to a CD33 signal sequence (amino acids 1-16) and at the C-terminus to a His•Tag sequence and expressed in NSO cells. Cat V is predominantly expressed in normal thymus, testis, and corneal epithelium. It is involved in the invariant chain degradation in thymic epithelial cells and its overexpression has been detected in myasthenia gravis. Abnormally wide spread expressions in mammary gland and colon have also been reported in breast and colonrectal carcinomas. Although it shows high amino acid identity with cathepsin L (Cat. No. 219382), these two cathepsins have very different tissue distribution and substrate specificity. As a result of glycosylation, this recombinant enzyme migrates ~40 kDa on SDS-PAGE under either reducing or non-reducing conditions. Requires activation prior to use.
Recombinant, human procathepsin V (amino acids 18-334) fused at the N-terminus to a CD33 signal sequence (amino acids 1-16) and at the C-terminus to a His•Tag sequence and expressed in NSO cells. Cat V is predominantly expressed in normal thymus, testis, and corneal epithelium. It is involved in the invariant chain degradation in thymic epithelial cells and its overexpression has been detected in myasthenia gravis. Abnormally wide spread expressions in mammary gland and colon have also been reported in breast and colonrectal carcinomas. Although it shows high amino acid identity with cathepsin L (Cat. No. 219382), these two cathepsins have very different tissue distribution and substrate specificity. As a result of glycosylation, this recombinant enzyme migrates ~40 kDa on SDS-PAGE under either reducing or non-reducing conditions. Requires activation prior to use.
Opakowanie
Please refer to vial label for lot-specific concentration.
Ostrzeżenie
Toxicity: Standard Handling (A)
Definicja jednostki
One unit is defined as the amount of enzyme that will cleave 1 pmol the fluorescent substrate Z-LR-AMC per min at 25°C, pH 5.5.
Postać fizyczna
In 800 mM NaCl, 25 mM sodium acetate, 0.8 M NaCl, pH 5.0.
Rekonstytucja
To activate rhCathepsin V, pre-incubate it at 20 µg/ml in 25 mM NaOAc, 100 mM NaCl, 5 mM DTT, pH 5.5 at room temperature. Following initial thaw aliquot and freeze (-70°C).
Inne uwagi
Tolosa, E., et al. 2003. J. Clin. Invest.112, 517.
Turk, V., et al. 2001. EMBO J.20, 4629.
Somoza, J.R., et al. 2000. Biochemistry39, 12543.
Bromme, D., et al. 1999. Biochemistry38, 2377.
Adachi, W., et al. 1998. Invest. Ophthalmol. Vis. Sci.39, 1789.
Santamaria, I., et al. 1998. Cancer Res.58, 1624.
Turk, V., et al. 2001. EMBO J.20, 4629.
Somoza, J.R., et al. 2000. Biochemistry39, 12543.
Bromme, D., et al. 1999. Biochemistry38, 2377.
Adachi, W., et al. 1998. Invest. Ophthalmol. Vis. Sci.39, 1789.
Santamaria, I., et al. 1998. Cancer Res.58, 1624.
Informacje prawne
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
HIS TAG is a registered trademark of Merck KGaA, Darmstadt, Germany
Ta strona może zawierać tekst przetłumaczony maszynowo.
Kod klasy składowania
12 - Non Combustible Liquids
Klasa zagrożenia wodnego (WGK)
WGK 1
Temperatura zapłonu (°F)
Not applicable
Temperatura zapłonu (°C)
Not applicable
Certyfikaty analizy (CoA)
Poszukaj Certyfikaty analizy (CoA), wpisując numer partii/serii produktów. Numery serii i partii można znaleźć na etykiecie produktu po słowach „seria” lub „partia”.
Masz już ten produkt?
Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
Nasz zespół naukowców ma doświadczenie we wszystkich obszarach badań, w tym w naukach przyrodniczych, materiałoznawstwie, syntezie chemicznej, chromatografii, analityce i wielu innych dziedzinach.
Skontaktuj się z zespołem ds. pomocy technicznej