生物来源
microbial (fermentation)
plant
质量水平
表单
saline suspension
技术
affinity chromatography: suitable
基质
cross-linked 4% beaded agarose
基质活化
cyanogen bromide
基质附着
carboxyl
基质隔离区
9 atoms
容量
20-40 mg/mL binding capacity (pepsin)
适用性
suitable for chromatography
储存温度
2-8°C
应用
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。
外形
混悬于含防腐剂的0.5M NaCl中。
储存分类代码
10 - Combustible liquids
WGK
WGK 3
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
Pepsin-mediated processing of the cytoplasmic histone H2A to strong antimicrobial peptide buforin I.
H S Kim et al.
Journal of immunology (Baltimore, Md. : 1950), 165(6), 3268-3274 (2000-09-07)
The intestinal epithelium forms a first line of innate host defense by secretion of proteins with antimicrobial activity against microbial infection. Despite the extensive studies on the antimicrobial host defense in many gastrointestinal tracts, little is known about the antimicrobial
F Canduri et al.
Biochemistry and molecular biology international, 45(4), 797-803 (1998-08-26)
Cathepsin D, a lysosomal aspartic protease, has been purified from porcine liver using a combination of pepstatin-A agarose and Affi-Gel Blue affinity chromatography, followed by size-exclusion chromatography. The purified protein consists of two polypeptide chains of 15 and 30 kDa
Mark S Pearson et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 23(9), 3007-3019 (2009-04-22)
Hookworms digest hemoglobin from erythrocytes via a proteolytic cascade that begins with the aspartic protease, APR-1. Ac-APR-1 from the dog hookworm, Ancylostoma caninum, protects dogs against hookworm infection via antibodies that neutralize enzymatic activity and interrupt blood-feeding. Toward developing a
Madanan Madathiparambil Gopalakrishnan et al.
The Biochemical journal, 383(Pt. 3), 507-515 (2004-07-17)
Before delivery to endosomes, portions of proCD (procathepsin D) and proSAP (prosaposin) are assembled into complexes. We demonstrate that such complexes are also present in secretions of cultured cells. To study the formation and properties of the complexes, we purified
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
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