P5906
Protein A (extracellular)–Agarose from Staphylococcus aureus
lyophilized powder
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About This Item
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biological source
Staphylococcus aureus
Quality Level
form
lyophilized powder
extent of labeling
~2 mg per mL
matrix
Cross-linked 4% beaded agarose
matrix activation
cyanogen bromide
matrix attachment
amino
matrix spacer
1 atom
capacity
≥20 mg/mL (Human IgG)
storage temp.
2-8°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
Lyophilized powder stabilized with lactose
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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The effect was examined of individual caseins on the rate of plasminogen activation by bovine urokinase-type and tissue-type plasminogen activators. All individual caseins (alpha-CN, beta-CN, and kappa-CN) enhanced the activity of both types of plasminogen activators. Optimal concentrations for alpha-CN
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The Wiskott-Aldrich syndrome protein and SCAR homolog (WASH), an actin nucleation-promoting factor, is present in the nucleus where it regulates gene transcription and maintains nuclear organization. Here, we show that WASH interacts with core non-homologous end-joining (NHEJ) factors including Ku70/Ku80
The Journal of biological chemistry, 278(21), 19266-19271 (2003-03-21)
Glomerular visceral epithelial cells (podocytes) appear to play a central role in maintaining the selective filtration barrier of the renal glomerulus. While the immunoglobulin superfamily member Nephrin was proposed to act as a cell adhesion molecule at the podocyte intercellular
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
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