Description:

Size: 100ul

Catalog no.: bs-10497R-A555

Price: 380 EUR

Product details

Modification Site

None

Crossreactivity

Human

French translation

anticorps

Tested applications

IF(IHC-P)

Clonality

Polyclonal

Modification

Unmodified

Excitation emission

553nm/568nm

Concentration

1ug per 1ul

Target Antigen

Phosphotyrosine

Conjugated with

ALEXA FLUOR® 555

Recommended dilutions

IF(IHC-P)(1:50-200)

Clone

Polyclonal antibody

Purification

Purified by Protein A.

Conjugation

Alexa Fluor,ALEXA FLUOR 555

Category

Conjugated Primary Antibodies

Host Organism

Rabbit (Oryctolagus cuniculus)

Also known as

Anti-Phosphotyrosine PAb ALEXA FLUOR 555

Specificity

This is a highly specific antibody against Phosphotyrosine.

Long name

Phosphotyrosine Polyclonal Antibody, ALEXA FLUOR 555 Conjugated

Synonyms

tyrosine; Phospho tyrosine; tyr; Phospho tyr; p-Tyr; p-tyrosine;

Cross-reactive species details

Due to limited amount of testing and knowledge, not every possible cross-reactivity is known.

Source

This antibody was obtained by immunization of the host with KLH conjugated synthetic peptide derived from human Phosphotyrosine

Storage conditions

Store this antibody in aqueous buffered solution containing 1% BSA, 50% glycerol and 0.09% sodium azide. Keep refrigerated at 2 to 8 degrees Celcius for up to one year.

Properties

For facs or microscopy Alexa 1 conjugate.Very high photo stable ALEXA conjugate.If you buy Antibodies supplied by Bioss Primary Conjugated Antibodies. ALEXA FLUOR they should be stored frozen at - 24°C for long term storage and for short term at + 5°C.

Background of the antigen

The phosphorylation of specific tyrosine residues has been shown to be a primary mechanism of signal transduction during normal mitogenesis, cell cycle progression and oncogenic transformation, its role in other areas such as differentiation and gap junction communication, is a matter of active and ongoing research. that specifically recognize phosphorylated tyrosine residues have proved to be invaluable to the study of tyrosine phosphorylated proteins and the biochemical pathways in which they function.