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AB172822

Recombinant Human PDCD4 protein

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Recombinant Human PDCD4 protein is a Human Fragment protein, in the 212 to 357 aa range, expressed in Escherichia coli, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, HPLC.

View Alternative Names

H731, PDCD4, Programmed cell death protein 4, Neoplastic transformation inhibitor protein, Nuclear antigen H731-like, Protein 197/15a

Key facts

Purity

>95% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

Escherichia coli

Tags

His tag C-Terminus

Applications

SDS-PAGE, HPLC

applications

Biologically active

No

Accession

Q53EL6

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.4 Constituents: 100% PBS

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "HPLC": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MKASHREMTSKLLSDLCGTVMSTTDVEKSFDKLLKDLPELALDTPRAPQLVGQFIARAVGDGILCNTYIDSYKGTVDCVQARAALDKATVLLSMSKGGKRKDSVWGSGGGQQSVNHLVKEIDMLLKEYLLSGDISEAEHCLKELEVPLEHHHHHH","proteinLength":"Fragment","predictedMolecularWeight":"17 kDa","actualMolecularWeight":null,"aminoAcidEnd":357,"aminoAcidStart":212,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q53EL6","tags":[{"tag":"His","terminus":"C-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The PDCD4 protein also known as Programmed Cell Death 4 is a multifunctional tumor suppressor. With a molecular mass of approximately 64 kDa it plays an important role in regulating gene expression and inhibiting cellular transformation. PDCD4 is expressed in various tissues including the lung kidney and heart where it modulates different cellular pathways. Its ability to bind RNA and interact with eukaryotic initiation factor 4A (eIF4A) highlights its important role in translation regulation.
Biological function summary

PDCD4 inhibits translation by binding to the eIF4A RNA helicase blocking the translation initiation complex. This action stabilizes mRNA and reduces protein synthesis impacting processes such as cell growth and proliferation. Although PDCD4 functions mainly as a monomer it can also interact with other proteins to form complexes that enhance its regulatory activity. More specifically its role in controlling AP-1 transcription factor activity steps into the spotlight in influencing cellular responses.

Pathways

PDCD4 primarily interacts with signaling mechanisms related to apoptosis and inflammation. The protein is integral in the mTOR signaling pathway which governs cell growth in response to nutrient availability. PDCD4 also impacts the PI3K/AKT pathway linking its activity to cellular survival and metabolism. Through these pathways PDCD4 associates with proteins such as p53 and NF-kB connecting it to broader cellular and molecular networks involved in maintaining cellular integrity.

PDCD4 is significantly implicated in cancer progression and inflammation-related conditions. Its downregulation or loss frequently occurs in several cancers including breast and lung cancer leading to unchecked cell proliferation and tumor growth. PDCD4's interaction with proteins like c-Myc further demonstrates its importance in oncogenic pathways. Additionally its role in inflammation positions it as a critical factor in disorders such as Crohn’s disease where abnormal inflammatory responses are prominent.
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Specifications

Form

Liquid

Additional notes

Purity is greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE. Supplied as a 0.2 µM filtered solution.

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General info

Function

Inhibits translation initiation and cap-dependent translation. May excert its function by hindering the interaction between EIF4A1 and EIF4G. Inhibits the helicase activity of EIF4A. Modulates the activation of JUN kinase. Down-regulates the expression of MAP4K1, thus inhibiting events important in driving invasion, namely, MAPK85 activation and consequent JUN-dependent transcription. May play a role in apoptosis. Tumor suppressor. Inhibits tumor promoter-induced neoplastic transformation. Binds RNA (By similarity).

Sequence similarities

Belongs to the PDCD4 family.

Post-translational modifications

Polyubiquitinated, leading to its proteasomal degradation. Rapidly degraded in response to mitogens. Phosphorylation of the phosphodegron promotes interaction with BTRC and proteasomal degradation.. Phosphorylated at Ser-67 by RPS6KB1 in response to mitogens; phosphorylation promotes proteasomal degradation of PDCD4.

Subcellular localisation

Nucleus

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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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Target data

Inhibits translation initiation and cap-dependent translation. May excert its function by hindering the interaction between EIF4A1 and EIF4G. Inhibits the helicase activity of EIF4A. Modulates the activation of JUN kinase. Down-regulates the expression of MAP4K1, thus inhibiting events important in driving invasion, namely, MAPK85 activation and consequent JUN-dependent transcription. May play a role in apoptosis. Tumor suppressor. Inhibits tumor promoter-induced neoplastic transformation. Binds RNA (By similarity).
See full target information PDCD4
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Product promise

We are committed to supporting your work with high-quality reagents, and we're here for you every step of the way. In the unlikely event that one of our products does not perform as expected, you're protected by our Product Promise.
For full details, please see our Terms & Conditions
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Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

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