DAG1 Human

Dystroglycan 1 Human Recombinant
Cat. No.
BT3735
Source
Escherichia Coli.
Synonyms
Dystroglycan, Dystrophin-associated glycoprotein 1, DAG1, A3a, DAG, AGRNR, 156DAG, MDDGC7, MDDGC9.
Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage

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Description

DAG1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 30-312) containing 293 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 31.87kDa (calculated).

Product Specs

Introduction
Dystroglycan 1 (DAG1) is a crucial component of the dystrophin-glycoprotein complex, binding to laminin and connecting the subsarcolemmal cytoskeleton with the extracellular matrix. Alpha-dystroglycan's N-terminal domain is found in cerebrospinal fluid, although its impact on the nervous system is not fully understood. The complete dystroglycan complex, present in various tissues, plays a role in diverse processes, including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization. DAG1 is considered a candidate gene for mutations potentially causing autosomal recessive muscular dystrophies. The significant decrease of DAG1 in Duchenne muscular dystrophy weakens the connection between the sarcolemma and extracellular matrix, leaving muscle fibers vulnerable to necrosis.
Description
Recombinant human DAG1, produced in E. coli, is a single, non-glycosylated polypeptide chain. The sequence encompasses amino acids 30-312, totaling 293 amino acids, and includes a 10 amino acid N-terminal His tag. The calculated molecular mass is 31.87kDa.
Physical Appearance
White, lyophilized powder that has been filtered.
Formulation
DAG1 is filtered through a 0.4 μm filter and lyophilized from a 0.5 mg/ml solution in 0.05 M phosphate buffer and 0.075 M NaCl, at pH 7.4.
Solubility
To prepare a working stock solution, add deionized water to the lyophilized pellet, aiming for a concentration of approximately 0.5 mg/ml, and ensure complete dissolution. Note that DAG1 is not sterile. Before cell culture use, filter the product through an appropriate sterile filter.
Stability
Store the lyophilized protein at -20°C. After reconstitution, aliquot the product to minimize freeze-thaw cycles. The reconstituted protein remains stable at 4°C for a limited period and shows no change after two weeks at this temperature.
Purity
Purity is determined to be greater than 90.0% by SDS-PAGE.
Synonyms
Dystroglycan, Dystrophin-associated glycoprotein 1, DAG1, A3a, DAG, AGRNR, 156DAG, MDDGC7, MDDGC9.
Source
Escherichia Coli.
Amino Acid Sequence
MKHHHHHHASHWPSEPSEAV RDWENQLEAS MHSVLSDLHE AVPTVVGIPD GTAVVGRSFR VTIPTDLIAS SGDIIKVSAA GKEALPSWLH WDSQSHTLEG LPLDTDKGVH YISVSATRLG ANGSHIPQTS SVFSIEVYPE DHSELQSVRT ASPDPGEVVS SACAADEPVT VLTVILDADL TKMTPKQRID LLHRMRSFSE VELHNMKLVP VVNNRLFDMS AFMAGPGNAK KVVENGALLS WKLGCSLNQN SVPDIHGVEA PAREGAMSAQ LGYPVVGWHI ANKKPPLPKR VRR.

Product Science Overview

Introduction

Dystroglycan 1 (DAG1) is a protein encoded by the DAG1 gene, which is located on chromosome 3p21 in humans . This protein plays a crucial role in maintaining the structural integrity of various tissues, including skeletal muscle, by linking the extracellular matrix to the cytoskeleton .

Structure and Function

Dystroglycan is a glycoprotein that is initially synthesized as a single polypeptide and then cleaved into two subunits: α-dystroglycan and β-dystroglycan .

  • α-Dystroglycan: This extracellular subunit binds to laminin, agrin, and perlecan in the extracellular matrix.
  • β-Dystroglycan: This transmembrane subunit interacts with dystrophin and other cytoskeletal proteins inside the cell .

The interaction between these subunits and their respective binding partners is essential for the stability and function of muscle cells and other tissues .

Recombinant Dystroglycan 1

Recombinant Human Dystroglycan 1 is produced using various expression systems, such as yeast or wheat germ . It is often tagged with a 6xHis-tag at the N-terminus to facilitate purification and detection . The biological activity of recombinant dystroglycan 1 is typically assessed through its binding ability in functional assays like ELISA .

Clinical Significance

Mutations in the DAG1 gene are associated with a group of disorders known as dystroglycanopathies . These conditions are characterized by muscle weakness and degeneration due to the disrupted interaction between dystroglycan and the extracellular matrix . Dystroglycanopathies can vary in severity, ranging from mild limb-girdle muscular dystrophy to severe congenital muscular dystrophy .

Research and Applications

Recombinant dystroglycan 1 is used in various research applications to study its role in muscle biology and disease. It is also employed in the development of therapeutic strategies for dystroglycanopathies and other related conditions .

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