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胃蛋白酶

胃蛋白酶(9001-75-6,Pepsin)是在消化系统中发现的一种蛋白水解酶。 胃蛋白酶消化后,可以减少支气管组织的非特异性背景染色。胃蛋白酶通常用于制备抗体Fab片段。胃蛋白酶与其他酶一起可以在免疫组织化学测定中显示固定和酶消化的作用。
货品编码 规格 纯度 价格 (¥) 现价(¥) 特价(¥) 库存描述 数量 总计 (¥)
SS2232-500g 500g 来源于猪胃,1:10000 ¥ 2890.00 ¥ 2890.00 3-5days
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¥ 0.00
SS2232-100g 100g 来源于猪胃,1:10000 ¥ 578.00 ¥ 578.00 3-5days
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¥ 0.00
SS2232-25g 25g 来源于猪胃,1:10000 ¥ 168.00 ¥ 168.00 3-5days
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¥ 0.00
SS2231-500g 500g 来源于猪胃,1:3000 ¥ 1196.00 ¥ 1196.00 3-5days
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¥ 0.00
SS2231-100g 100g 来源于猪胃,1:3000 ¥ 316.00 ¥ 316.00 Instock
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¥ 0.00
SS2231-25g 25g 来源于猪胃,1:3000 ¥ 78.00 ¥ 78.00 Instock
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¥ 0.00
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中文别名 胃蛋白酶(9001-75-6,Pepsin);胃液素;胃朊酶;蛋白酵素;酸腈酶;胃酶;胃蛋白酶 A
英文别名 Pepsin (9001-75-6);Pepsin from Porcine Stomach;Pepsin A
CAS号 9001-75-6
Inchi No data available
InchiKey No data available
分子式 Molecular Weight
分子量 Formula
溶解度Solubility No data available
性状 白色至淡黄色固体粉末
储藏条件 Storage conditions 储存温度2-8℃

胃蛋白酶(9001-75-6,Pepsin)实验注意事项:
1.实验前需戴好防护眼镜,穿戴防护服和口罩,佩戴手套,避免与皮肤接触。
2.实验过程中如遇到有毒或者刺激性物质及有害物质产生,必要时实验操作需要手套箱内完成以免对实验人员造成伤害。
3.取样品的移液枪头需及时更换,必要时为避免交叉污染尽可能选择滤芯吸头。
4.称量药品时选用称量纸,并无风处取药和称量以免扬撒,试剂的容器使用前务必确保干净,并消毒。
5.取药品时尽量采用多个药勺分别使用,使用后清洗干净后,烘干消毒存放。
6.实验后产生的废弃物需分类存储,并交于专业生物废气物处理公司处理,以免造成环境污染。

Pepsin (9001-75-6) Experimental considerations:
1. Wear protective glasses, protective clothing and masks, gloves, and avoid contact with the skin during the experiment.
2. The waste generated after the experiment needs to be stored separately, and handed over to a professional biological waste gas treatment company to avoid environmental pollution.

Tag:胃蛋白酶(9001-75-6,Pepsin),胃蛋白酶 来源于猪胃,胃蛋白酶的活性,胃蛋白酶的价格,胃蛋白酶的注意事项,胃蛋白酶的储存条件,胃蛋白酶的生产,胃蛋白酶的厂家,胃蛋白酶的外观,胃蛋白酶的作用
产品说明 胃蛋白酶(9001-75-6,Pepsin)是在消化系统中发现的一种蛋白水解酶,9001-75-6的MSDS及应用等参数见主页。
IntroductionPepsin (9001-75-6,胃蛋白酶) is a proteolytic enzyme found in the digestive system. The MSDS and application parameters of 9001-75-6 can be found on the homepage.
Application1用于产生抗体的 F(ab′)2 片段
Application2
Application3
1.UV fluorescence excitation imaging of healing of wounds in skin: Evaluation of wound closure in organ culture model.
2.Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin, a blue-colored biliprotein of microalga Spirulina.
3.Microparticles based on chitosan/carboxymethylcellulose polyelectrolyte complexes for colon delivery of vancomycin.
4.Effect of heat and homogenization on in vitro digestion of milk.

1.UV fluorescence excitation imaging of healing of wounds in skin: Evaluation of wound closure in organ culture model.
Wang Y1, Gutierrez-Herrera E2, Ortega-Martinez A1, Anderson RR1, Franco W1. Lasers Surg Med. 2016 Apr 13. doi: 10.1002/lsm.22523. [Epub ahead of print]
BACKGROUND AND OBJECTIVE: Molecules native to tissue that fluoresce upon light excitation can serve as reporters of cellular activity and protein structure. In skin, the fluorescence ascribed to tryptophan is a marker of cellular proliferation, whereas the fluorescence ascribed to cross-links of collagen is a structural marker. In this work, we introduce and demonstrate a simple but robust optical method to image the functional process of epithelialization and the exposed dermal collagen in wound healing of human skin in an organ culture model.

2.Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin, a blue-colored biliprotein of microalga Spirulina.
Minic SL1, Stanic-Vucinic D1, Vesic J1, Krstic M1, Nikolic MR2, Velickovic TC3. J Proteomics. 2016 Apr 13. pii: S1874-3919(16)30111-7. doi: 10.1016/j.jprot.2016.03.043. [Epub ahead of print]
C-phycocyanin, the major protein of cyanobacteria Spirulina, possesses significant antioxidant, anti-cancer, anti-inflammatory and immunomodulatory effects, ascribed to covalently attach linear tetrapyrrole chromophore phycocyanobilin. There are no literature data about structure and biological activities of released peptides with bound chromophore in C-phycocyanin digest. This study aims to identify chromopeptides obtained after pepsin digestion of C-phycocyanin and to examine their bioactivities. C-phycocyanin is rapidly digested by pepsin in simulated gastric fluid. The structure of released chromopeptides was analyzed by high resolution tandem mass spectrometry and peptides varying in size from 2 to 13 amino acid residues were identified in both subunits of C-phycocyanin. Following separation by HPLC, chromopeptides were analyzed for potential bioactivities. It was shown that all five chromopeptide fractions have significant antioxidant and metal-chelating activities and show cytotoxic effect on human cervical adenocarcinoma and epithelial colonic cancer cell lines.

3.Microparticles based on chitosan/carboxymethylcellulose polyelectrolyte complexes for colon delivery of vancomycin.
Cerchiara T1, Abruzzo A2, Parolin C2, Vitali B2, Bigucci F2, Gallucci MC3, Nicoletta FP4, Luppi B2. Carbohydr Polym. 2016 Jun 5;143:124-30. doi: 10.1016/j.carbpol.2016.02.020. Epub 2016 Feb 9.
The aim of this work was to prepare polyelectrolyte complexes based on chitosan (CH) and carboxymethylcellulose (CMC) for colon delivery of vancomycin (VM). Various batches of polyelectrolyte complexes, using three different CH/CMC weight ratios (3:1, 1:1 and 1:3), were prepared and collected as microparticles by spray-drying process. Microparticles were characterized in terms of yield, encapsulation efficiency, drug loading, morphology and mucoadhesion properties. Microparticles water-uptake and VM release as well as its protection against gastric pepsin degradation were also investigated. Finally, the antibacterial activity against Staphylococcus aureus, a Gram-positive model strain, was evaluated. The best formulation CH/CMC 1:3 was selected based on the encapsulation efficiency, water-uptake and drug release rate. Moreover, microparticles were able to prevent VM degradation and showed a good antibacterial activity against S. aureus. Finally, to improve the release of VM in the colon the selected formulation was coated with lauric acid.

4.Effect of heat and homogenization on in vitro digestion of milk.
Tunick MH1, Ren DX2, Van Hekken DL1, Bonnaillie L1, Paul M1, Kwoczak R1, Tomasula PM3. J Dairy Sci. 2016 Apr 6. pii: S0022-0302(16)30140-0. doi: 10.3168/jds.2015-10474. [Epub ahead of print]
Central to commercial fluid milk processing is the use of high temperature, short time (HTST) pasteurization to ensure the safety and quality of milk, and homogenization to prevent creaming of fat-containing milk. Ultra-high-temperature sterilization is also applied to milk and is typically used to extend the shelf life of refrigerated, specialty milk products or to provide shelf-stable milk. The structures of the milk proteins and lipids are affected by processing but little information is available on the effects of the individual processes or sequences of processes on digestibility. In this study, raw whole milk was subjected to homogenization, HTST pasteurization, and homogenization followed by HTST or UHT processing. Raw skim milk was subjected to the same heating regimens. In vitro gastrointestinal digestion using a fasting model was then used to detect the processing-induced changes in the proteins and lipids. Using sodium dodecyl sulfate-PAGE, gastric pepsin digestion of the milk samples showed rapid elimination of the casein and α-lactalbumin bands, persistence of the β-lactoglobulin bands, and appearance of casein and whey peptide bands.

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