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Primary Antibodies

AKT1 Antibody

Background

Serine/threonine protein kinase; Murine thymoma viral (v-akt) oncogene homolog-1. AKT1 is a serine-threonine protein kinase. It is catalytically inactive in serum-starved primary and immortalized fibroblasts. AKT1 and the related AKT2 are activated by platelet-derived growth factor. The activation is rapid and specific, and it is abrogated by mutations in the pleckstrin homology domain of AKT1. It was shown that the activation occurs through phosphatidylinositol 3-kinase. In the developing nervous system AKT is a critical mediator of growth factor-induced neuronal survival. Survival factors can suppress apoptosis in a transcription-independent manner by activating the serine/threonine kinase AKT1, which then phosphorylates and inactivates components of the apoptotic machinery.

AKT1 Antibody

Description

AKT IgY Antibody

Purification

Antigen affinity-purified

Clonality / Clone

This is a polyclonal antibody.

Host

AKT1 antibody was raised in chicken.

Please use anti-chicken secondary antibodies.

Immunogen

2-200

Application

AKT antibody can be used for the detection of AKT by Western blot, may also work for IHC and ICC.

Tested Application

WB

Buffer

Phosphate-Buffered Saline. No preservatives added.

Storage

AKT1 antibody can be stored at 4˚C for short term (weeks). Long term storage should be at -20˚C. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.

Species Reactivity

H, M, R, B, X

Protein GI Number

4885061

Protein Accession Number

NP_005154.1

Molecular Weight

55.7 kDa (calculated)

Short Description

Serine/threonine protein kinase

This product belongs to the following categories:

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References

  1. Brunet,A., Bonni,A., Zigmond,M. J., Lin,M. Z., Juo,P., Hu,L. S., Anderson,M. J., Arden,K. C., Blenis,J. and Greenberg,M. E. TITLE Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor JOURNAL Cell 96 (6), 857-868 (1999).


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