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10791156001

Roche

内切蛋白酶Glu-C(V8蛋白酶)

from Staphylococcus aureus V8

同義詞:

V8蛋白酶, 蛋白酶v8

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About This Item

酶委員會編號:
分類程式碼代碼:
23201100

形狀

lyophilized (salt-free)

比活性

20 U/mg

分子量

30 kDa

包裝

pkg of 2 mg

製造商/商標名

Roche

最適pH

8.0-8.5

一般說明

内切蛋白酶Glu-C是一种葡萄球菌丝氨酸蛋白酶。其抑制剂包括DFP、α2-巨球蛋白、以及TLCK。
Approximately 20 U/mg lyophilizate at +25°C with Z-Phe-Leu-Glu-4-nitranilide as the substrate (approximately 500 U/mg lyophilizate at +37°C with casein as the substrate).
At 25 °C with Z-Phe-Leu-Glu-4-nitranilide as the substrate (approximately 500 U/mg lyophilizate at 37 °C with casein as the substrate).

特異性

热灭活:通过煮沸10分钟使内切蛋白酶Glu-C失活。

應用

使用内切蛋白酶Glu-C(V8蛋白酶)进行蛋白结构分析和序列分析。

生化/生理作用

内切蛋白酶Glu-C可特异性地水解Glu(或同时水解Glu和Asp)羧基侧的肽和酯键,其取决于所用的缓冲液。

準備報告

激活剂:该酶在SH试剂存在下具有最大活性
工作浓度:1 至 5 mM
工作溶液: 推荐的溶剂是50mM乙酸铵(pH 4.0,2mg/ml)。
储存条件(工作溶液):-15至-25°C
分液冷冻保存并仅解冻一次,酶(2mg/ml,溶于50mM乙酸铵中,pH 4.0)可稳定保存至少一个月。

儲存和穩定性

在2°C至8°条件下储存。 (请保持干燥!)

其他說明

仅用于生命科学研究。不可用于诊断。

象形圖

Exclamation markHealth hazard

訊號詞

Danger

危險分類

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

標靶器官

Respiratory system

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 1

閃點(°F)

does not flash

閃點(°C)

does not flash


分析證明 (COA)

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存取文件庫

Rosalynn C Molden et al.
Current protocols in protein science, 77, 23-23 (2014-08-02)
Histones are chromatin proteins that are highly modified with many different types of post-translational modifications. These modifications act in concert to regulate a number of chromatin-related processes. However, identification and quantification of co-occurring histone post-translational modifications is challenging because there
Marion Avril et al.
PLoS pathogens, 9(6), e1003430-e1003430 (2013-07-05)
During blood stage infection, Plasmodium falciparum infected erythrocytes (IE) bind to host blood vessels. This virulence determinant enables parasites to evade spleen-dependent killing mechanisms, but paradoxically in some cases may reduce parasite fitness by killing the host. Adhesion of infected
Tianshi Wang et al.
Molecular cell, 75(4), 823-834 (2019-07-16)
Sirt3, as a major mitochondrial nicotinamide adenine dinucleotide (NAD)-dependent deacetylase, is required for mitochondrial metabolic adaption to various stresses. However, how to regulate Sirt3 activity responding to metabolic stress remains largely unknown. Here, we report Sirt3 as a SUMOylated protein in

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