推薦產品
生物源
microbial (fermentation)
plant
品質等級
形狀
saline suspension
技術
affinity chromatography: suitable
基質
cross-linked 4% beaded agarose
基質活化
cyanogen bromide
基質結合
carboxyl
基質墊片
9 atoms
容量
20-40 mg/mL binding capacity (pepsin)
適合性
suitable for chromatography
儲存溫度
2-8°C
應用
胃酶抑制剂 A-琼脂糖用于蛋白质色谱、亲和色谱和特种树脂中。胃酶抑制剂 A-琼脂糖已被用于表征从商业化的粗制胃蛋白酶中分离得到的三种壳聚糖酶同工酶。
外觀
混悬于含防腐剂的0.5M NaCl中。
儲存類別代碼
10 - Combustible liquids
水污染物質分類（WGK）
WGK 3
P Geldhof et al.
International journal for parasitology, 33(2), 129-136 (2003-03-14)
A pepstatin A-agarose column was used in an attempt to purify a previously described antibody-degrading aspartyl proteinase from excretory-secretory material from the L4 and the adult stages of the bovine abomasal nematode Ostertagia ostertagi. However, no aspartyl proteinase activity was
N Hiraiwa et al.
European journal of biochemistry, 246(1), 133-141 (1997-05-15)
To understand the mechanism of the maturation of various proteins in protein-storage vacuoles, we purified a 48-kDa aspartic endopeptidase composed of 32-kDa and 16-kDa subunits from castor bean. Immunocytochemical and cell fractionation analyses of the endosperm of maturing castor bean
C J Morrison et al.
Journal of general microbiology, 139 Pt 6, 1177-1186 (1993-06-01)
Aspartyl proteinase (AP) is an extracellular enzyme of Candida albicans implicated as a pathogenic factor. Previous reports on the purification and characterization of AP suggested that a single DEAE-Sephadex chromatographic step was sufficient for the removal of extraneous proteins and
Liliana Rojo et al.
Marine biotechnology (New York, N.Y.), 12(6), 696-707 (2010-02-20)
Acid digestive proteinases were studied in the gastric fluids of two species of clawed lobster (Homarus americanus and Homarus gammarus). An active protein was identified in both species as aspartic proteinase by specific inhibition with pepstatin A. It was confirmed
O Carnevali et al.
Biology of reproduction, 60(1), 140-146 (1998-12-22)
Oocyte growth within the follicle is preponderantly due to the accumulation of hepatically derived yolk protein (vitellogenin, VTG) by receptor-mediated endocytosis; once in the oocyte, VTG is partially processed and stored in yolk globules. In some pelagic egg-laying marine teleosts
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