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AB78789

Recombinant Human EPF protein

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Recombinant Human EPF protein is a Human Full Length protein, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.

View Alternative Names

Hsp10, 10 kDa chaperonin, Chaperonin 10, Early-pregnancy factor, Heat shock protein family E member 1, CPN10, EPF, HSPE1

1 Images
SDS-PAGE - Recombinant Human EPF protein (AB78789)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human EPF protein (AB78789)

3ug by SDS-PAGE under reducing conditions and visualized by coomassie blue stain.

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P61604

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.29% Sodium chloride, 0.242% Tris

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>" } } }
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Sequence info

[{"sequence":"MAGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGSKGKGGEIQPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDGDILGKYVD","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P61604","tags":[]}]
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Properties and storage information

Shipped at conditions
Blue 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.

EPF also known as Embryo Paracrine Factor is a protein with a mass of approximately 18-20 kDa. This protein primarily expresses in embryonic tissues and certain adult tissues with regeneration and repair abilities. EPF functions as a signaling molecule and plays a role in cellular communication influencing different cellular behaviors like proliferation differentiation and migration.
Biological function summary

EPF impacts multiple cellular processes during embryogenesis and tissue regeneration. It does not function as a part of a larger protein complex but interacts directly with surface receptors to initiate signal transduction pathways. EPF activities help in regulating cell cycle transitions balancing cell growth with apoptosis for proper tissue formation and healing. By mediating these activities EPF is critical for normal development and efficient repair processes.

Pathways

Several molecular networks engage with EPF to exert its influence. One of the primary pathways involving EPF is the Wnt signaling pathway which contributes to the regulation of gene expression cellular growth and differentiation. Through this pathway EPF interacts with proteins like β-catenin. Additionally EPF also associates with the PI3K/Akt pathway which further highlights its involvement in controlling cellular survival and growth dynamics.

Abnormal EPF function is linked with cancer progression and regenerative disorders. Dysregulation of EPF can lead to uncontrolled cell proliferation and has been observed in certain cancers such as colorectal cancer. Furthermore impaired EPF signaling might affect wound healing processes leading to chronic wounds. During these disease processes EPF interacts with other important signaling molecules such as p53 in cancer to influence disease outcomes.
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Specifications

Form

Liquid

Additional notes

ab78789 is purified using conventional chromatography techniques.

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General info

Function

Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed : 11422376, PubMed : 1346131, PubMed : 7912672). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable).

Sequence similarities

Belongs to the GroES chaperonin family.

Subcellular localisation

Mitochondrion matrix

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Product protocols

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Target data

Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed : 11422376, PubMed : 1346131, PubMed : 7912672). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable).
See full target information HSPE1
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Primary Antibodies

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Secondary Antibodies

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