Datasheet

Biological Description

Specificity	Myoferlin Rabbit mAb detects endogenous levels of total Myoferlin protein.
Background	Myoferlin is a membrane-anchored protein belonging to the ferlin family, encoded by a gene located on chromosome 10q23.33. It shares 69% sequence similarity with dysferlin, a protein whose mutations are linked to Miyoshi myopathy and limb-girdle muscular dystrophy type 2B. Members of the ferlin family—including dysferlin, myoferlin, otoferlin, Fer1L5, and Fer1L6—are characterized by multiple C2 domains and a single-pass transmembrane domain at the C-terminus. Myoferlin and dysferlin are the most structurally similar, each being ~230 kDa, containing seven C2 domains and a DYSF domain, and showing high expression in myoblasts. Functionally, myoferlin is active in various cell types, including myoblasts and endothelial cells. In cancer, it has emerged as a potential biomarker and therapeutic target in malignancies such as non–small-cell lung cancer, breast cancer, pancreatic adenocarcinoma, hepatocellular carcinoma, colorectal cancer, melanoma, head and neck squamous cell carcinoma, clear cell renal cell carcinoma, and endometrioid carcinoma. Mechanistically, myoferlin contributes to tumor progression by promoting angiogenesis, vasculogenic mimicry, metabolic reprogramming, epithelial–mesenchymal transition, and exosome modulation. Its roles in both physiological and pathological contexts highlight its significance as a candidate for novel cancer treatment strategies.

Specificity

Myoferlin Rabbit mAb detects endogenous levels of total Myoferlin protein.

Background

Myoferlin is a membrane-anchored protein belonging to the ferlin family, encoded by a gene located on chromosome 10q23.33. It shares 69% sequence similarity with dysferlin, a protein whose mutations are linked to Miyoshi myopathy and limb-girdle muscular dystrophy type 2B. Members of the ferlin family—including dysferlin, myoferlin, otoferlin, Fer1L5, and Fer1L6—are characterized by multiple C2 domains and a single-pass transmembrane domain at the C-terminus. Myoferlin and dysferlin are the most structurally similar, each being ~230 kDa, containing seven C2 domains and a DYSF domain, and showing high expression in myoblasts. Functionally, myoferlin is active in various cell types, including myoblasts and endothelial cells. In cancer, it has emerged as a potential biomarker and therapeutic target in malignancies such as non–small-cell lung cancer, breast cancer, pancreatic adenocarcinoma, hepatocellular carcinoma, colorectal cancer, melanoma, head and neck squamous cell carcinoma, clear cell renal cell carcinoma, and endometrioid carcinoma. Mechanistically, myoferlin contributes to tumor progression by promoting angiogenesis, vasculogenic mimicry, metabolic reprogramming, epithelial–mesenchymal transition, and exosome modulation. Its roles in both physiological and pathological contexts highlight its significance as a candidate for novel cancer treatment strategies.

Usage Information

Application

WB, IF, FCM

Dilution

WB	IF	FCM
1:2000	1:100	1:400

Reactivity

Mouse, Rat, Human

Source

Rabbit

MW

235 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/31475450/

Myoferlin Rabbit mAb

Biological Description

Usage Information

References

Application Data