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V2260

Sigma-Aldrich

Monoclonal Anti-V5-Peroxidase antibody produced in mouse

clone V5-10, purified immunoglobulin, lyophilized powder

Sinonimo/i:

Monoclonal Anti-V5

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About This Item

Numero MDL:
Codice UNSPSC:
12352203
NACRES:
NA.56

Origine biologica

mouse

Livello qualitativo

Coniugato

peroxidase conjugate

Forma dell’anticorpo

purified immunoglobulin

Tipo di anticorpo

primary antibodies

Clone

V5-10, monoclonal

Forma fisica

lyophilized powder

Confezionamento

vial of 0.5 mL

Concentrazione

5-11 mg/mL

tecniche

western blot: 1:4,000-1:8,000

Temperatura di conservazione

2-8°C

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Descrizione generale

The V5 tag is a 14-amino acid long peptide sequence (GKPIPNPLLGLDST) that is derived from an epitope on the P and V proteins of simian virus 5 (SV5), which belongs to the paramyxovirus family. Monoclonal Anti-V5 Peroxidase conjugate reacts with V5-tagged recombinant fusion proteins expressed in transfected mmmalian cells or produced by in vitro translation.

Specificità

Recognizes V5 Tag (GKPIPNPLLGLDST) fusion proteins

Applicazioni

Suitable for immunoblotting.

Stato fisico

Lyophilized from a 0.01 M phosphate buffered saline solution, pH 7.4, containing 1% BSA and 0.05% MIT

Nota sulla preparazione

Prepared by the two-step glutaraldehyde method described by Avrameas, S., et al., Scand. J. Immunol., 8, Suppl. 7, 7 (1978).
Reconstitute with 0.5 mL of distilled water.

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Pittogrammi

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Avvertenze

Warning

Indicazioni di pericolo

Classi di pericolo

Skin Sens. 1

Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 2

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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Adaptation of viruses to their hosts can result in specialization and a restricted host range. Species-specific polymorphisms in the influenza virus polymerase restrict its host range during transmission from birds to mammals. ANP32A was recently identified as a cellular co-factor
Mauricio P Contreras et al.
Science advances, 9(18), eadg3861-eadg3861 (2023-05-03)
Parasites counteract host immunity by suppressing helper nucleotide binding and leucine-rich repeat (NLR) proteins that function as central nodes in immune receptor networks. Understanding the mechanisms of immunosuppression can lead to strategies for bioengineering disease resistance. Here, we show that

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