推荐产品
應用
用于中和胰蛋白酶/EDTA溶液的作用。
设计用于角质形成细胞传代培养的本品含有Kunitz型大豆胰蛋白酶抑制剂（SBTI），可抑制丝氨酸蛋白酶（如胰蛋白酶和类胰蛋白酶）的催化活性。 它用于细胞培养以终止胰蛋白酶的作用，胰蛋白酶用于在传代过程中从基质中释放细胞。 它也可能用于其他抗丝氨酸蛋白酶研究。
外觀
溶于98.7% DPBS和1.3%大豆胰蛋白酶抑制剂中。
重構
以1:1 TID:胰蛋白酶/EDTA的最小体积比使用。
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訊號詞
Danger
危險聲明
危險分類
Resp. Sens. 1 - Skin Sens. 1
儲存類別代碼
12 - Non Combustible Liquids
水污染物質分類（WGK）
WGK 2
閃點（°F）
Not applicable
閃點（°C）
Not applicable
個人防護裝備
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
其他客户在看
Jolanta Kamińska et al.
Advances in medical sciences, 64(2), 274-279 (2019-03-23)
In vitro expansion is an invaluable method to obtain keratinocytes in amounts necessary for effective transplantation therapies. In vitro cell culturing provokes questions concerning potential epigenetic alterations occurring in expanded cells in the context of usefulness for transplantation and safety.
C L Dumke et al.
Journal of applied physiology (Bethesda, Md. : 1985), 92(2), 657-664 (2002-01-18)
Serum proteins [molecular weight (MW) > 10,000] are essential for increased insulin-stimulated glucose transport after in vitro muscle contractions. We investigated the role of the kallikrein-kininogen system, including bradykinin, which is derived from kallikrein (MW > 10,000)-catalyzed degradation of serum
Maurizio Trovato et al.
Biochemical and biophysical research communications, 302(2), 311-315 (2003-02-27)
The design of minimal units required for enzyme inhibition is a major field of interest in structural biology and biotechnology. The successful design of the cyclic dodecapeptide corresponding to the Phe17-Val28 reactive site amino acid sequence of the low-molecular-mass trypsin
I B Svendsen et al.
Carlsberg research communications, 54(6), 231-239 (1989-01-01)
A trypsin inhibitor with a Km of 5 x 10(-5) M has been isolated from kohlrabi (Brassica napus var. rapifera). Subtilisin DY is inhibited only weakly and chymotrypsin not at all. The inhibitor is closely related to napin as determined
实验方案
Natural trypsin Inhibitors also known as serine protease inhibitors (serpins) are the largest and most diverse family of protease inhibitors. Serpins control the activation and catabolism of proteins by the inhibition of serine proteases in vivo.
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