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Mouse Anti-DYSF Recombinant Antibody (C-11) (CBMAB-D2033-YC)

Provided herein is a Mouse monoclonal antibody, which binds to Dysferlin (DYSF). The antibody can be used for immunoassay techniques, such as WB, IP, IF, ELISA.
See all DYSF antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
C-11
Antibody Isotype
IgG
Application
WB, IP, IF, ELISA

Basic Information

Specificity
Human
Antibody Isotype
IgG
Clonality
Monoclonal
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!]

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
Dysferlin
Introduction
DYSF belongs to the ferlin family and is a skeletal muscle protein found associated with the sarcolemma. It is involved in muscle contraction and contains C2 domains that play a role in calcium-mediated membrane fusion events, suggesting that it may be involved in membrane regeneration and repair. In addition, the protein encoded by this gene binds caveolin-3, a skeletal muscle membrane protein which is important in the formation of caveolae. Specific mutations in this gene have been shown to cause autosomal recessive limb girdle muscular dystrophy type 2B (LGMD2B) as well as Miyoshi myopathy.
Entrez Gene ID
8291
UniProt ID
O75923
Alternative Names
Dysferlin; Limb Girdle Muscular Dystrophy 2B (Autosomal Recessive); Fer-1-Like Family Member 1; Fer-1-Like Protein 1; FER1L1; Dystrophy-Associated Fer-1-Like Protein; Dystrophy-Associated Fer-1-Like 1; LGMD2B; MMD1;
Research Area
Key calcium ion sensor involved in the Ca2+-triggered synaptic vesicle-plasma membrane fusion. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress (By similarity).
Biological Process
Macrophage activation involved in immune response Source: MGI
Membrane fusion Source: GO_Central
Monocyte activation involved in immune response Source: MGI
Negative regulation of phagocytosis Source: MGI
Plasma membrane organization Source: GO_Central
Plasma membrane repair Source: GO_Central
T-tubule organization Source: GO_Central
Vesicle fusion Source: GO_Central
Cellular Location
Sarcolemma; Cell membrane; Cytoplasmic vesicle membrane. Colocalizes, during muscle differentiation, with BIN1 in the T-tubule system of myotubules and at the site of contact between two myotubes or a myoblast and a myotube. Wounding of myotubes led to its focal enrichment to the site of injury and to its relocalization in a Ca2+-dependent manner toward the plasma membrane. Colocalizes with AHNAK, AHNAK2 and PARVB at the sarcolemma of skeletal muscle. Detected on the apical plasma membrane of the syncytiotrophoblast. Reaches the plasmma membrane through a caveolin-independent mechanism. Retained by caveolin at the plasmma membrane (By similarity). Colocalizes, during muscle differentiation, with CACNA1S in the T-tubule system of myotubules (By similarity). Accumulates and colocalizes with fusion vesicles at the sarcolemma disruption sites (By similarity).
Involvement in disease
Muscular dystrophy, limb-girdle, autosomal recessive 2 (LGMDR2):
An autosomal recessive degenerative myopathy characterized by weakness and atrophy starting in the proximal pelvifemoral muscles, with onset in the late teens or later, massive elevation of serum creatine kinase levels and slow progression. Scapular muscle involvement is minor and not present at onset. Upper limb girdle involvement follows some years after the onset in lower limbs.
Miyoshi muscular dystrophy 1 (MMD1):
A late-onset muscular dystrophy involving the distal lower limb musculature. It is characterized by weakness that initially affects the gastrocnemius muscle during early adulthood.
Distal myopathy with anterior tibial onset (DMAT):
Onset of the disorder is between 14 and 28 years of age and the anterior tibial muscles are the first muscle group to be involved. Inheritance is autosomal recessive.
Topology
Cytoplasmic: 1-2046
Helical: 2047-2067
Extracellular: 2068-2080

Folland, C., Johnsen, R., Gomez, A. B., Trajanoski, D., Davis, M. R., Moore, U., ... & Ravenscroft, G. (2022). Identification of a novel heterozygous DYSF variant in a large family with a dominantly‐inherited dysferlinopathy. Neuropathology and Applied Neurobiology, e12846.

Muriel, J., Lukyanenko, V., Kwiatkowski, T., Bhattacharya, S., Garman, D., Weisleder, N., & Bloch, R. J. (2022). The C2 domains of dysferlin: roles in membrane localization, Ca2+ signalling and sarcolemmal repair. The Journal of Physiology, 600(8), 1953-1968.

Charnay, T., Blanck, V., Cerino, M., Bartoli, M., Riccardi, F., Bonello-Palot, N., ... & Krahn, M. (2021). Retrospective analysis and reclassification of DYSF variants in a large French series of dysferlinopathy patients. Genetics in Medicine, 23(8), 1574-1577.

Zhong, H., Yu, M., Lin, P., Zhao, Z., Zheng, X., Xi, J., ... & Yuan, Y. (2021). Molecular landscape of DYSF mutations in dysferlinopathy: From a Chinese multicenter analysis to a worldwide perspective. Human Mutation, 42(12), 1615-1623.

Izumi, R., Takahashi, T., Suzuki, N., Niihori, T., Ono, H., Nakamura, N., ... & Aoki, M. (2020). The genetic profile of dysferlinopathy in a cohort of 209 cases: Genotype–phenotype relationship and a hotspot on the inner DysF domain. Human mutation, 41(9), 1540-1554.

Cox, A., Zhao, C., Tolkach, Y., Nettersheim, D., Schmidt, D., Kristiansen, G., ... & Ellinger, J. (2020, August). The contrasting roles of Dysferlin during tumor progression in renal cell carcinoma. In Urologic Oncology: Seminars and Original Investigations (Vol. 38, No. 8, pp. 687-e1). Elsevier.

Xiao, Y., Zhu, H., Li, L., Gao, S., Liu, D., Dai, B., ... & Zuo, X. (2019). Global analysis of protein expression in muscle tissues of dermatomyositis/polymyosisits patients demonstrated an association between dysferlin and human leucocyte antigen A. Rheumatology, 58(8), 1474-1484.

Lee, J. J., Maruyama, R., Duddy, W., Sakurai, H., & Yokota, T. (2018). Identification of novel antisense-mediated exon skipping targets in DYSF for therapeutic treatment of dysferlinopathy. Molecular Therapy-Nucleic Acids, 13, 596-604.

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

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