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P0932

Millipore

Protein A-Agarose from Staphylococcus aureus

lyophilized powder

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About This Item

MDL number:
UNSPSC Code:
41106500

form

lyophilized powder

Quality Level

matrix

Immobilized on 4% cross-linked beaded agarose

matrix activation

p-nitrophenyl chloroformate

matrix attachment

amino

matrix spacer

1 atom

capacity

30-40 mg/mL binding capacity (human IgG)

storage temp.

−20°C

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Application

Protein A-agarose is used for affinity chromatography, antibody purification and characterization, and protein A, G and L resins. Protein A-agarose has been used to study the effects of protein A immunoadsorption in patients with chronic dilated cardiomyopathy as well as to study multiple sclerosis and gastric cancer.

Quantity

Swelling: 1 g swells to approx. 4 ml.

Physical form

Supplied as lyophilized powder stabilized with lactose.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Guoxin Shen et al.
The Plant journal : for cell and molecular biology, 49(2), 228-237 (2007-01-24)
Animal CHIP proteins are chaperone-dependent E3 ubiquitin ligases that physically interact with Hsp70, Hsp90 and proteasome, promoting degradation of a selective group of non-native or damaged proteins in animal cells. The plant CHIP-like protein, AtCHIP, also plays important roles in
Xiaohong Shi et al.
Methods in molecular biology (Clifton, N.J.), 379, 137-148 (2007-05-16)
The membrane glycoproteins (Gn and Gc) of viruses in the family Bunyaviridae form projections on the virion envelope and are involved in virus entry and eliciting protective immunity. The glycoproteins are modified by N-linked glycosylation and accumulate in the Golgi
Laurent Garderet et al.
Leukemia & lymphoma, 47(7), 1340-1347 (2006-08-23)
This study evaluated the feasibility of using dendritic cells (DCs) to generate, ex vivo, anti-tumor cytotoxic T lymphocytes (CTL) in patients with stage III multiple myeloma (MM). Nucleated cells from eight patients who had received chemotherapy (three of whom had
K Klaamas et al.
Neoplasma, 55(2), 143-150 (2008-02-02)
All human immunoglobulins are glycosylated. The changes in IgG glycosylation are associated with autoimmune disorders and pregnancy. Little is known about IgG glycosylation in patients with cancer. A lectin enzyme-linked immunosorbent assay (LELISA) based method was developed for measuring the
Yu Ya Kit et al.
Biochemistry. Biokhimiia, 73(8), 950-956 (2008-09-09)
Immunoglobulins IgG and sIgA actively hydrolyzing histone H1 have been detected on analyzing proteolytic activity of antibodies isolated by chromatography on Protein A-agarose from blood serum of patients with multiple sclerosis and from colostrum of healthy mothers. These antibodies hydrolyze

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