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Mouse Anti-MYO1E (AA 918-1014) Recombinant Antibody (CBFYM-2986) (CBMAB-M3181-FY)

This product is mouse antibody that recognizes MYO1E. The antibody CBFYM-2986 can be used for immunoassay techniques such as: ELISA, WB.
See all MYO1E antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYM-2986
Antibody Isotype
IgG2a, k
Application
ELISA, WB

Basic Information

Immunogen
Recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.Immunogen sequence: VSIGPGLPKN SRPTRRNTTQ NTGYSSGTQN ANYPVRAAPP PPGYHQNGVI RNQYVPYPHA PGSQRSNQKS LYTSMARPPL PRQQSTSSDR VSQTPES
Specificity
Human
Antibody Isotype
IgG2a, k
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 918-1014

Target

Full Name
myosin IE
Introduction
This gene encodes a member of the nonmuscle class I myosins which are a subgroup of the unconventional myosin protein family. The unconventional myosin proteins function as actin-based molecular motors. Class I myosins are characterized by a head domain, a regulatory domain and a either a short or long tail domain. Among the class I myosins, this protein is distinguished by a long tail domain that is involved in crosslinking actin filaments. This protein localizes to the cytoplasm and may be involved in intracellular movement and membrane trafficking. Mutations in this gene are the cause of focal segmental glomerulosclerosis-6. This gene has been referred to as myosin IC in the literature but is distinct from the myosin IC gene located on chromosome 17.
Entrez Gene ID
4643
UniProt ID
Q12965
Alternative Names
Myosin IE; Myosin-Ic; Unconventional Myosin 1E; MYO1C; Unconventional Myosin-Ie; MYO1E Variant Protein; HuncM-IC; FSGS6
Function
Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. Binds to membranes containing anionic phospholipids via its tail domain. Required for normal morphology of the glomerular basement membrane, normal development of foot processes by kidney podocytes and normal kidney function. In dendritic cells, may control the movement of class II-containing cytoplasmic vesicles along the actin cytoskeleton by connecting them with the actin network via ARL14EP and ARL14.
Biological Process
Actin filament organization Source: GO_Central
Endocytosis Source: UniProtKB
Glomerular basement membrane development Source: UniProtKB
Glomerular filtration Source: UniProtKB
Glomerular visceral epithelial cell development Source: UniProtKB
In utero embryonic development Source: Ensembl
Nitrogen compound metabolic process Source: Ensembl
Platelet-derived growth factor receptor signaling pathway Source: Ensembl
Post-embryonic hemopoiesis Source: Ensembl
Vasculogenesis Source: Ensembl
Vesicle transport along actin filament Source: GO_Central
Cellular Location
Cytoskeleton
Cytoplasm
Other locations
Cytoplasmic vesicle
clathrin-coated vesicle
Cell junction
Note: Colocalizes with F-actin (By similarity). In cultured podocytes, it localizes close to and is associated with the cytoplasmic membrane, with enrichment at the lamellipodia tips. Colocalizes with cytoplasmic vesicles, including endocytic clathrin-coated vesicles. Colocalizes with dynamin at cytoplasmic vesicles.
Involvement in disease
Focal segmental glomerulosclerosis 6 (FSGS6):
A renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and progressive decline in renal function. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation. FSGS6 is a childhood-onset disorder resulting in nephrotic syndrome, which includes massive proteinuria, hypoalbuminemia, hyperlipidemia, and edema.

Garone, M. E., Chase, S. E., Zhang, C., & Krendel, M. (2023). Myosin 1e deficiency affects migration of 4T1 breast cancer cells. Cytoskeleton.

Liu, S., Liu, P., Fei, X., Zhu, C., Hou, J., Wang, X., & Pan, Y. (2023). Analysis and validation of the potential of the MYO1E gene in pancreatic adenocarcinoma based on a bioinformatics approach. Oncology Letters, 26(1), 1-17.

Liu, P. J., Gunther, L. K., Garone, M. E., Zhang, C., Perez, D., Bi-Karchin, J., ... & Krendel, M. (2022). Steroid-Resistant Nephrotic Syndrome–Associated MYO1E Mutations Have Differential Effects on Myosin 1e Localization, Dynamics, and Activity. The Journal of the American Society of Nephrology, 33(11), 1989-2007.

Plante, E. (2022). Examination of the effects of Myosin-1e expression on tumor behavior and computational analysis of MYO1E mutations associated with kidney disease (Doctoral dissertation).

Brzeska, H., Bagnoli, M., Korn, E. D., & Titus, M. A. (2020). Dictyostelium myosin 1F and myosin 1E inhibit actin waves in a lipid‐binding‐dependent and motor‐independent manner. Cytoskeleton, 77(8), 295-302.

Girón-Pérez, D. A., Vadillo, E., Schnoor, M., & Santos-Argumedo, L. (2020). Myo1e modulates the recruitment of activated B cells to inguinal lymph nodes. Journal of Cell Science, 133(5), jcs235275.

Barger, S. R., James, M. L., Pellenz, C. D., Krendel, M., & Sirotkin, V. (2019). Human myosin 1e tail but not motor domain replaces fission yeast Myo1 domains to support myosin-I function during endocytosis. Experimental cell research, 384(2), 111625.

Zhang, Y., Cao, F., Zhou, Y., Feng, Z., Sit, B., Krendel, M., & Yu, C. H. (2019). Tail domains of myosin-1e regulate phosphatidylinositol signaling and F-actin polymerization at the ventral layer of podosomes. Molecular biology of the cell, 30(5), 622-635.

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

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