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Merck
CN

P3296

Millipore

蛋白G琼脂糖凝胶,快速流动

recombinant, expressed in E. coli, aqueous ethanol suspension

别名:

蛋白G琼脂糖,快速流动 来源于链球菌

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关于此项目

MDL编号:
UNSPSC代码:
41106500
NACRES:
NA.56
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重组

expressed in E. coli

质量水平

表单

aqueous ethanol suspension

分析物化学类别

proteins (Immunoglobulins of various mammalian species)

标记范围

~2 mg per mL

技术

affinity chromatography: suitable

基质

Sepharose 4B Fast Flow

基质活化

cyanogen bromide

基质附着

amino

基质隔离区

1 atom

储存温度

2-8°C

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一般描述

蛋白G是从G组链球菌菌株G-148中分离得到的细菌胞壁蛋白,它能与免疫球蛋白(IgG)结合。通过木瓜蛋白酶消化从细胞中提取该蛋白,并依次使用DEAE-Sephadex离子交换层析、琼脂糖凝胶偶联人IgG亲和层析以及Sephadex G-200凝胶层析进行纯化。蛋白G与各种多克隆和单克隆IgG结合的pH条件基本在2.8-10之间,在pH 4-5时结合最强,在pH 10时结合最弱。它是强大的IgG检测试剂。

P3296-5Ml的最新产品编号为GE17-0618-01

应用

蛋白G琼脂糖凝胶 被用于亲和层析,蛋白质层析,抗体纯化和表征,免疫亲和基质,蛋白A、G和L树脂,蛋白质相互作用以及纯化和检测。蛋白G琼脂糖凝胶 已被用于开发一种可确认人血清中是否存在抗促红细胞生成素中和抗体的方法,以及比较马血清中白蛋白和IgG消耗的方法。

外形

悬浮于20%乙醇中

制备说明

使用重组链球菌蛋白G制备,其中白蛋白结合区已被移除

法律信息

Sepharose is a trademark of Cytiva

象形图

Flame

警示用语:

Warning

危险声明

危险分类

Flam. Liq. 3

储存分类代码

3 - Flammable liquids

WGK

WGK 3

闪点(°F)

115.0 °F - closed cup

闪点(°C)

46.1 °C - closed cup

法规信息

常规特殊物品
此项目有

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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G Yang et al.
Oncogene, 26(1), 91-101 (2006-06-27)
The t(8;21) chromosomal translocation that generates the fusion oncoprotein RUNX1-ETO predominates in leukemia patients of the French-American-British (FAB) class M2 subtype. The oncoprotein has the capacity to promote expansion of hematopoietic stem/progenitor cells and induces leukemia in association with other
B Akerström et al.
The Journal of biological chemistry, 261(22), 10240-10247 (1986-08-05)
Protein G, an IgG-binding molecule, was prepared from the cell walls of a group G streptococcal strain, G-148. The protein could be extracted from the cells by papain digestion and purified by the sequential use of ion-exchange chromatography on DEAE-Sephadex
Cristina Hidalgo-Carcedo et al.
Nature cell biology, 13(1), 49-58 (2010-12-21)
Collective cell migration occurs in a range of contexts: cancer cells frequently invade in cohorts while retaining cell-cell junctions. Here we show that collective invasion by cancer cells depends on decreasing actomyosin contractility at sites of cell-cell contact. When actomyosin
Yi-Jye Chern et al.
Cell death & disease, 10(7), 504-504 (2019-06-28)
Therapy-refractory disease is one of the main contributors of treatment failure in cancer. In colorectal cancer (CRC), SPARC can function as a sensitizer to conventional chemotherapy by enhancing apoptosis by interfering with the activity of Bcl-2. Here, we examine a
B Akerström et al.
Journal of immunology (Baltimore, Md. : 1950), 135(4), 2589-2592 (1985-10-01)
Protein G is an immunoglobulin (IgG)-binding bacterial cell wall protein recently isolated from group G streptococci. We have investigated the avidity of protein G for various monoclonal and polyclonal Ig of the IgG class, and compared it with the binding

实验方案

Techniques for protein antigen molecular weight determination, protein interactions, enzymatic activity, and post-translational modifications.

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