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Mouse Anti-MYO6 (AA 1188-1285) Recombinant Antibody (CBFYM-2992) (CBMAB-M3187-FY)

This product is mouse antibody that recognizes MYO6. The antibody CBFYM-2992 can be used for immunoassay techniques such as: ELISA, WB.
See all MYO6 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYM-2992
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: KKKGWWYAHF DGPWIARQME LHPDKPPILL VAGKDDMEMC ELNLEETGLT RKRGAEILPR QFEEIWERCG GIQYLQNAIE SRQARPTYAT AMLQSLLK
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 1188-1285

Target

Full Name
myosin VI
Introduction
This gene encodes a reverse-direction motor protein that moves toward the minus end of actin filaments and plays a role in intracellular vesicle and organelle transport. The protein consists of a motor domain containing an ATP- and an actin-binding site and a globular tail which interacts with other proteins. This protein maintains the structural integrity of inner ear hair cells and mutations in this gene cause non-syndromic autosomal dominant and recessive hearing loss. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
Entrez Gene ID
4646
UniProt ID
Q9UM54
Alternative Names
Myosin VI; Unconventional Myosin-6; Deafness, Autosomal Recessive 37; Myosin VI Transcript Variant 007; Myosin VI Transcript Variant 008; Unconventional Myosin-VI
Function
Myosins are actin-based motor molecules with ATPase activity (By similarity).

Unconventional myosins serve in intracellular movements (By similarity).

Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments (PubMed:10519557).

Has slow rate of actin-activated ADP release due to weak ATP binding (By similarity).

Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration (By similarity).

Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway (PubMed:16507995).

Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells (PubMed:11447109).

May act as a regulator of F-actin dynamics (By similarity).

As part of the DISP complex, may regulate the association of septins with actin and thereby regulate the actin cytoskeleton (PubMed:29467281).

May play a role in transporting DAB2 from the plasma membrane to specific cellular targets (By similarity).

May play a role in the extension and network organization of neurites (By similarity).

Required for structural integrity of inner ear hair cells (By similarity).

Modulates RNA polymerase II-dependent transcription (PubMed:16949370).
Biological Process
Actin filament-based movement Source: UniProtKB
Actin filament organization Source: GO_Central
DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
Endocytosis Source: UniProtKB
Inner ear auditory receptor cell differentiation Source: GO_Central
Inner ear morphogenesis Source: GO_Central
Intracellular protein transport Source: UniProtKB
Positive regulation of transcription by RNA polymerase II Source: UniProtKB
Regulation of secretion Source: UniProtKB
Sensory perception of sound Source: UniProtKB-KW
Vesicle transport along actin filament Source: GO_Central
Cellular Location
Nucleus
Plasma membrane
ruffle membrane
cytosol
Golgi apparatus
trans-Golgi network membrane
Golgi apparatus
Other locations
perinuclear region
clathrin-coated pit
clathrin-coated vesicle
filopodium
microvillus
Note: Also present in endocyctic vesicles (PubMed:16507995). Translocates from membrane ruffles, endocytic vesicles and cytoplasm to Golgi apparatus, perinuclear membrane and nucleus through induction by p53 and p53-induced DNA damage (PubMed:16507995). Recruited into membrane ruffles from cell surface by EGF-stimulation (PubMed:9852149). Colocalizes with DAB2 in clathrin-coated pits/vesicles (PubMed:11967127). Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane (By similarity).
Isoform 3:
Other locations
clathrin-coated vesicle membrane
Isoform 4:
Plasma membrane
ruffle membrane
Other locations
clathrin-coated vesicle membrane
Involvement in disease
Deafness, autosomal dominant, 22 (DFNA22):
A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA22 is progressive and postlingual, with onset during childhood. By the age of approximately 50 years, affected individuals invariably have profound sensorineural deafness.
Deafness, autosomal recessive, 37 (DFNB37):
A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.
Deafness, autosomal dominant 22, with hypertrophic cardiomyopathy (DFNHCM):
An autosomal dominant sensorineural deafness associated with hypertrophic cardiomyopathy.
PTM
Phosphorylation in the motor domain, induced by EGF, results in translocation of MYO6 from the cell surface to membrane ruffles and affects F-actin dynamics. Phosphorylated in vitro by p21-activated kinase (PAK).

Canon, L., Kikuti, C., Planelles-Herrero, V. J., Lin, T., Mayeux, F., Sirkia, H., ... & Houdusse, A. (2023). How myosin VI traps its off-state, is activated and dimerizes. Nature Communications, 14(1), 6732.

Zhan, X. J., Wang, R., Kuang, X. R., Zhou, J. Y., & Hu, X. L. (2023). Elevated expression of myosin VI contributes to breast cancer progression via MAPK/ERK signaling pathway. Cellular Signalling, 106, 110633.

Karatsai, O., Lehka, L., Wojton, D., Grabowska, A. I., Duda, M. K., Lenartowski, R., & Redowicz, M. J. (2023). Unconventional myosin VI in the heart: Involvement in cardiac dysfunction progressing with age. Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease, 1869(6), 166748.

Seki, Y., Shitara, H., Ishii, R., Ouchi, T., Yasuda, S. P., & Kikkawa, Y. (2021). Myosin VI haploinsufficiency reduced hearing ability in mice. Neuroscience, 478, 100-111.

Zakrzewski, P., Lenartowska, M., & Buss, F. (2021). Diverse functions of myosin VI in spermiogenesis. Histochemistry and cell biology, 155, 323-340.

Magistrati, E., & Polo, S. (2021). Myomics: myosin VI structural and functional plasticity. Current Opinion in Structural Biology, 67, 33-40.

Zakrzewski, P., Suwińska, A., Lenartowski, R., Rędowicz, M. J., Buss, F., & Lenartowska, M. (2020). Myosin VI maintains the actin-dependent organization of the tubulobulbar complexes required for endocytosis during mouse spermiogenesis. Biology of Reproduction, 102(4), 863-875.

Zakrzewski, P., Rędowicz, M. J., Buss, F., & Lenartowska, M. (2020). Loss of myosin VI expression affects acrosome/acroplaxome complex morphology during mouse spermiogenesis. Biology of reproduction, 103(3), 521-533.

Lehka, L., Topolewska, M., Wojton, D., Karatsai, O., Alvarez-Suarez, P., Pomorski, P., & Rędowicz, M. J. (2020). Formation of aberrant myotubes by myoblasts lacking myosin VI is associated with alterations in the cytoskeleton organization, myoblast adhesion and fusion. Cells, 9(7), 1673.

Rogez, B., Würthner, L., Petrova, A. B., Zierhut, F. B., Saczko-Brack, D., Huergo, M. A., ... & Veigel, C. (2019). Reconstitution reveals how myosin-VI self-organises to generate a dynamic mechanism of membrane sculpting. Nature communications, 10(1), 3305.

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

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