219467
Cathepsin V, His•Tag®, Human, Recombinant, NSO Cells
recombinant human, expressed in NSO cells
Sinônimo(s):
Cathepsin L2, Cathepsin U
Faça loginpara ver os preços organizacionais e de contrato
About This Item
Produtos recomendados
recombinante
expressed in NSO cells
Nível de qualidade
Ensaio
≥95% (SDS-PAGE)
forma
frozen liquid
atividade específica
≥300 units/μg
fabricante/nome comercial
Calbiochem®
condição de armazenamento
OK to freeze
avoid repeated freeze/thaw cycles
Impurezas
≤1.0 EU/μg Endotoxins (EU/μg Cathepsin V)
Condições de expedição
wet ice
temperatura de armazenamento
−70°C
Descrição geral
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.
Embalagem
Please refer to vial label for lot-specific concentration.
Advertência
Toxicity: Standard Handling (A)
Definição da unidade
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.
forma física
In 800 mM NaCl, 25 mM sodium acetate, 0.8 M NaCl, pH 5.0.
Reconstituição
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).
Outras notas
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.
Informações legais
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
HIS TAG is a registered trademark of Merck KGaA, Darmstadt, Germany
Código de classe de armazenamento
12 - Non Combustible Liquids
Classe de risco de água (WGK)
WGK 1
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Certificados de análise (COA)
Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.
Já possui este produto?
Encontre a documentação dos produtos que você adquiriu recentemente na biblioteca de documentos.
Nossa equipe de cientistas tem experiência em todas as áreas de pesquisa, incluindo Life Sciences, ciência de materiais, síntese química, cromatografia, química analítica e muitas outras.
Entre em contato com a assistência técnica