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AB62958

Recombinant Human Cofilin protein (His tag N-Terminus)

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(1 Publication)

Recombinant Human Cofilin protein (His tag N-Terminus) is a Human Full Length protein, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, WB.

View Alternative Names

CFL, CFL1, Cofilin-1, 18 kDa phosphoprotein, p18

2 Images
Western blot - Recombinant Human Cofilin protein (His tag N-Terminus) (AB62958)
  • WB

Unknown

Western blot - Recombinant Human Cofilin protein (His tag N-Terminus) (AB62958)

All lanes:

Western blot - Anti-Cofilin antibody - Loading Control (<a href='/en-us/products/primary-antibodies/cofilin-antibody-loading-control-ab42824'>ab42824</a>) at 1 µg/mL

All lanes:

Western blot - Recombinant Human Cofilin protein (His tag N-Terminus) (ab62958) at 0.01 µg

Secondary

All lanes:

Western blot - Goat Anti-Rabbit IgG H&L (HRP) preadsorbed (<a href='/en-us/products/secondary-antibodies/goat-rabbit-igg-h-l-hrp-preadsorbed-ab97080'>ab97080</a>) at 1/5000 dilution

Predicted band size: 18 kDa

true

Exposure time: 30s

SDS-PAGE - Recombinant Human Cofilin protein (His tag N-Terminus) (AB62958)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human Cofilin protein (His tag N-Terminus) (AB62958)

SDS Page analysis of ab62958 (3ug, 15% gel).

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, WB

applications

Biologically active

No

Accession

P23528

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 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>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>ab62958 can be used as a WB positive control in conjunction with <a href='/en-us/products/primary-antibodies/cofilin-antibody-loading-control-ab42824'>ab42824</a>.</p>" } } }
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDVGQTVDDPYATFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P23528","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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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.

Cofilin-1 also known just as cofilin is a small actin-modulating protein with a molecular weight of approximately 19 kDa. It is part of the actin chemical structure regulation and plays an important role in actin filament dynamics by severing and depolymerizing actin filaments. Cofilin-1 expresses widely in both muscle and non-muscle tissues modulating the actin cytoskeleton which is critical for cell movement shape and various signaling pathways. The phosphorylated form of this protein known as phospho-cofilin or p-cofilin is another significant state to consider.
Biological function summary

Through its interaction with actin filaments cofilin-1 functions to regulate the length and turnover of the actin cytoskeleton within cells. Cofilin-1 is part of a critical complex where it binds to actin monomers and filaments to facilitate the disassembly and recycling of actin. This regulation impacts cellular activities such as migration endocytosis and division influencing how cells respond to internal and external signals. Cofilin-1's ability to bind and sever actin filaments forms an important part of its functional mechanism altering the cytoskeletal architecture for various cellular processes.

Pathways

Cofilin-1 participates principally in the actin dynamics component of the cytoskeleton remodeling pathway. Within this framework cofilin-1 acts alongside other proteins like actin-depolymerizing factor (ADF) and tropomyosin influencing assembly and disassembly cycles of actin filaments. The Rho family of GTPases regulates cofilin-1 activity through signaling pathways such as the Rho/ROCK/LIMK pathway. This signaling regulation affects actin filament organization impacting cellular processes like axonal guidance and directed cell movement.

There is a strong connection between cofilin-1 dysregulation and neurodegenerative diseases such as Alzheimer's disease and certain types of cancer. In Alzheimer's disease cofilin-1 activity influenced by abnormal cofilin phosphorylation forms part of the pathological mechanisms that lead to synaptic dysfunction and neurofibrillary tangles. In the context of cancer cofilin-1 collaborates with proteins such as RhoA and LIM kinase contributing to cancer cell invasion and metastasis by reorganizing the actin cytoskeleton to facilitate cell motility. Understanding these interactions helps in targeting therapeutic strategies against these conditions.
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Specifications

Form

Liquid

Additional notes

purified by using conventional chromatography techniques

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General info

Function

Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity (PubMed : 11812157). In conjunction with the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (PubMed : 15580268). Required for the centralization of the mitotic spindle and symmetric division of zygotes (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization in epithelial cells (PubMed : 21834987). Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (PubMed : 23633677). Required for neural tube morphogenesis and neural crest cell migration (By similarity).

Sequence similarities

Belongs to the actin-binding proteins ADF family.

Post-translational modifications

Inactivated by phosphorylation on Ser-3. Phosphorylated on Ser-3 in resting cells (By similarity). Dephosphorylated by PDXP/chronophin; this restores its activity in promoting actin filament depolymerization. The phosphorylation of Ser-24 may prevent recognition of the nuclear localization signal (By similarity). Phosphorylated via a ARRB1-RAC1-LIMK1-PAK1 cascade upon active ligand stimulation of atypical chemokine receptor ACKR2.

Subcellular localisation

Nucleus matrix

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Product protocols

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Target data

Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity (PubMed : 11812157). In conjunction with the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (PubMed : 15580268). Required for the centralization of the mitotic spindle and symmetric division of zygotes (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization in epithelial cells (PubMed : 21834987). Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (PubMed : 23633677). Required for neural tube morphogenesis and neural crest cell migration (By similarity).
See full target information CFL1
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Kidney international 93:81-94 PubMed28739141

2017

AMP-activated protein kinase/myocardin-related transcription factor-A signaling regulates fibroblast activation and renal fibrosis.

Applications

Unspecified application

Species

Unspecified reactive species

Yuguo Wang,Li Jia,Zhaoyong Hu,Mark L Entman,William E Mitch,Yanlin Wang
View all publications
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