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Mouse Anti-CFL1 Recombinant Antibody (CBXC-0389) (CBMAB-C4682-CQ)


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Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
CBXC-0389
Antibody Isotype
IgG2b
Application
WB, ICC/IF, IHC-P, IP

Basic Information

Immunogen
Recombinant protein encompassing a sequence within the center region of human Cofilin 1.
Host Species
Mouse
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG2b
Clonality
Monoclonal Antibody
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:500-1:3,000
IHC-P1:100-1:1,000
IP1:100-1:500

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 20% Glycerol
Preservative
None
Concentration
1 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Cofilin 1
Introduction
The protein encoded by this gene can polymerize and depolymerize F-actin and G-actin in a pH-dependent manner. Increased phosphorylation of this protein by LIM kinase aids in Rho-induced reorganization of the actin cytoskeleton. Cofilin is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. It is involved in the translocation of actin-cofilin complex from cytoplasm to nucleus.[supplied by OMIM, Apr 2004]
Entrez Gene ID
Human1072
Mouse12631
Rat29271
UniProt ID
HumanP23528
MouseP18760
RatP45592
Alternative Names
Cofilin 1; Cofilin, Non-Muscle Isoform; Cofilin 1 (Non-Muscle); 18 KDa Phosphoprotein; P18; CFL;
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).
Biological Process
Actin cytoskeleton organization Source: ProtInc
Actin filament depolymerization Source: UniProtKB
Actin filament fragmentation Source: GO_Central
Actin filament severing Source: GO_Central
Cell motility Source: GO_Central
Cytoskeleton organization Source: UniProtKB
Establishment of spindle localization Source: UniProtKB
Interleukin-12-mediated signaling pathway Source: Reactome
Negative regulation of apoptotic process Source: UniProtKB
Positive regulation by host of viral process Source: AgBase
Positive regulation of embryonic development Source: UniProtKB
Regulation of cell morphogenesis Source: UniProtKB
Regulation of dendritic spine morphogenesis Source: ParkinsonsUK-UCL
Response to virus Source: UniProtKB
Rho protein signal transduction Source: ProtInc
Viral process Source: UniProtKB-KW
Cellular Location
Ruffle membrane; Lamellipodium membrane; Cytoskeleton; Nucleus matrix; Lamellipodium. Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Detected at the cleavage furrow and contractile ring during cytokinesis. Almost completely in nucleus in cells exposed to heat shock or 10% dimethyl sulfoxide.
PTM
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.
More Infomation

Li, Y., Gong, Y., Chen, Y., Qu, B., & Zhang, S. (2022). Identification and functional characterization of Cofilin-1 as a new member of antimicrobial protein. Developmental & Comparative Immunology, 127, 104281.

Yao, B., Li, Y., Chen, T., Niu, Y., Wang, Y., Yang, Y., ... & Tu, K. (2021). Hypoxia‐induced cofilin 1 promotes hepatocellular carcinoma progression by regulating the PLD1/AKT pathway. Clinical and translational medicine, 11(3), e366.

Sousa-Squiavinato, A. C. M., Vasconcelos, R. I., Gehren, A. S., Fernandes, P. V., de Oliveira, I. M., Boroni, M., & Morgado-Díaz, J. A. (2021). Cofilin-1, LIMK1 and SSH1 are differentially expressed in locally advanced colorectal cancer and according to consensus molecular subtypes. Cancer Cell International, 21(1), 1-15.

Werle, S. D., Schwab, J. D., Tatura, M., Kirchhoff, S., Szekely, R., Diels, R., ... & Kestler, H. A. (2021). Unraveling the molecular tumor-promoting regulation of cofilin-1 in pancreatic cancer. Cancers, 13(4), 725.

Cho, H. J., Baek, G. O., Yoon, M. G., Ahn, H. R., Son, J. A., Kim, S. S., ... & Eun, J. W. (2021). Overexpressed proteins in HCC Cell-derived exosomes, CCT8, and Cofilin-1 are potential biomarkers for patients with HCC. Diagnostics, 11(7), 1221.

Zhang, L., Chai, Z., Kong, S., Feng, J., Wu, M., Tan, J., ... & Xu, H. (2021). Nujiangexanthone A Inhibits Hepatocellular Carcinoma Metastasis via Down Regulation of Cofilin 1. Frontiers in Cell and Developmental Biology, 9, 476.

Medina, C., de la Fuente, V., tom Dieck, S., Nassim-Assir, B., Dalmay, T., Bartnik, I., ... & Romano, A. (2020). LIMK, Cofilin 1 and actin dynamics involvement in fear memory processing. Neurobiology of Learning and Memory, 173, 107275.

Rangel, M. P., Antonangelo, L., Acencio, M. M. P., Faria, C. S., de Sá, V. K., Leão, P. S., ... & Capelozzi, V. L. (2018). Detection of sputum cofilin-1 as indicator of malignancy. Brazilian Journal of Medical and Biological Research, 51.

Shishkin, S., Eremina, L., Pashintseva, N., Kovalev, L., & Kovaleva, M. (2017). Cofilin-1 and other ADF/cofilin superfamily members in human malignant cells. International journal of molecular sciences, 18(1), 10.

Wang, H., Tao, L., Jin, F., Gu, H., Dai, X., Ni, T., ... & Liu, Y. (2017). Cofilin 1 induces the epithelial-mesenchymal transition of gastric cancer cells by promoting cytoskeletal rearrangement. Oncotarget, 8(24), 39131.

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For research use only. Not intended for any clinical use.

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