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Merck

P2921

Sigma-Aldrich

Monoclonal Anti-Protein A antibody produced in mouse

clone SPA-27, ascites fluid

Sinónimos:

Monoclonal Anti-Protein A

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.46

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

SPA-27, monoclonal

contains

15 mM sodium azide

technique(s)

immunocytochemistry: suitable
indirect ELISA: 1:20,000
western blot: suitable

isotype

IgG1

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

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General description

Protein A is a 42 kDa single chain polypeptide isolated from the cell wall of Staphylococcus aureus Cowan I strain.

Specificity

Specific for Protein A and shows no cross-reactivity with Protein G. Reacts with free Protein A or IgG bound Protein A and does not interfere with the Fc binding activity of Protein A.

Immunogen

protein A from Cowan I strain of Staphy­lococcus aureus.

Application

Monoclonal Anti-Protein A antibody produced in mouse has been used in enzyme-linked immunosorbent assay (ELISA). It has also been used in western blot and dot blot analyses.

Biochem/physiol Actions

Protein A is considered as a universal reagent in biochemistry and immunology, due to its affinity for the Fc region of many mammalian immunoglobulins. It is used for different applications such as purification of immunoglobulins by affinity chromatography, cell surface studies, radioimmunoassay (RIA), enzyme immunoassay (EIA), immunoprecipitations and many other procedures. It can be used in these methods either in its native form or conjugated to various markers.

Physical form

Monoclonal Anti-Protein A antibody produced in mouse is provided as ascites fluid with 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

10 - Combustible liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

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Stephanie Marroquin et al.
Infection and immunity, 87(5) (2019-03-06)
Numerous factors have, to date, been identified as playing a role in the regulation of Agr activity in Staphylococcus aureus, including transcription factors, antisense RNAs, and host elements. Herein we investigated the product of SAUSA300_1984 (termed MroQ), a transmembrane Abi-domain/M79
Matthew B Frankel et al.
Molecular microbiology, 78(1), 238-252 (2010-10-07)
The human pathogen Staphylococcus aureus requires cell wall anchored surface proteins to cause disease. During cell division, surface proteins with YSIRK signal peptides are secreted into the cross-wall, a layer of newly synthesized peptidoglycan between separating daughter cells. The molecular
Dane Vassiliadis et al.
BMC genomics, 20(1), 251-251 (2019-03-30)
Optimal glucose metabolism is central to the growth and development of cells. In microbial eukaryotes, carbon catabolite repression (CCR) mediates the preferential utilization of glucose, primarily by repressing alternate carbon source utilization. In fission yeast, CCR is mediated by transcriptional
Jasdeep S Nanra et al.
Human vaccines & immunotherapeutics, 9(3), 480-487 (2012-12-20)
Staphylococcus aureus can cause severe life threatening invasive diseases. The principal immune effector mechanism by which humans are protected from Gram positive bacteria such as S. aureus is antigen specific antibody- and complement-dependent opsonophagocytosis. This process can be measured in
Shan Huang et al.
Frontiers in molecular biosciences, 7, 581095-581095 (2021-01-12)
Hog1 is a mitogen-activated protein kinase in yeast that primarily regulates cellular responses to hyperosmolarity stress. In this study, we have examined the potential involvement of Hog1 in mediating cellular responses to DNA damaging agents. We find that treatment of

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