Myostatin Human, His

Myostatin Human Recombinant, His Tag
Cat. No.
BT23984
Source
Escherichia Coli.
Synonyms
GDF-8, MSTN, Growth/Differentiation Factor 8,MSTN Muscle Hypertrophy.
Appearance
Filtered white lyophilized (freeze-dried) powder.
Purity
Greater than 95% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Total 152AA. M.W. 16.7kDa (calculated). N-terminal His-tag and spacer (43AA – highlighted). The AA sequence of the human myostatin part of the fusion protein is corresponding to the UniProtKB/Swiss-Prot entry O14793.

Product Specs

Introduction
Myostatin (GDF-8), a member of the transforming growth factor β superfamily, is a 12 kDa mature glycoprotein composed of 113 amino acid residues. It is exclusively expressed in human skeletal muscle and secreted into the plasma. Myostatin plays a crucial role in regulating skeletal muscle mass. Research indicates that myostatin may also be involved in cardiac development and function.
Description
This protein consists of a total of 152 amino acids, with a molecular weight of 16.7 kDa (calculated). It features an N-terminal His-tag and a spacer (43AA, highlighted). The amino acid sequence of the human myostatin portion within the fusion protein aligns with the UniProtKB/Swiss-Prot entry O14793.
Physical Appearance
White lyophilized powder (freeze-dried) after filtration.
Formulation
The protein solution (0.5 mg/ml in 0.05M acetate buffer, pH 4.5) is filtered through a 0.4 μm filter and then lyophilized.
Solubility
To prepare a working stock solution of around 0.5 mg/mL, add 0.1M Acetate buffer (pH 4) to the lyophilized pellet and allow it to dissolve completely. For use at higher pH values, dilute the solution with the appropriate buffer to a concentration of 10 μg/ml. Note that the solubility of this antigen is limited at higher concentrations.
Stability
Store the lyophilized protein at -20°C. After reconstitution, aliquot the product to prevent repeated freeze-thaw cycles. The reconstituted protein remains stable at 4°C for a limited time and shows no significant change after two weeks at this temperature.
Purity
Purity determined by SDS-PAGE is greater than 95%.
Synonyms
GDF-8, MSTN, Growth/Differentiation Factor 8,MSTN Muscle Hypertrophy.
Source
Escherichia Coli.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDPSSRSAVR SRRDFGLDCD EHSTESRCCR YPLTVDFEAFGWDWIIAPKR YKANYCSGEC EFVFLQKYPH THLVHQANPR GSAGPCCTPT KMSPINMLYF NGKEQIIYGKIPAMVVDRCG CS.

Product Science Overview

Structure and Function

Myostatin is synthesized as a large precursor molecule that undergoes proteolytic cleavage to generate an N-terminal propeptide and a disulfide-linked C-terminal dimer, which is the biologically active form of the protein . The circulating form of myostatin consists of a latent complex of the C-terminal dimer and other proteins, including its propeptide, which maintain the C-terminal dimer in an inactive state. Activation of myostatin requires additional cleavage of the prodomain by a tolloid-like metalloproteinase .

Biological Role

Myostatin acts as a negative regulator of skeletal muscle growth. It inhibits the differentiation of myoblasts into mature muscle fibers, thereby controlling muscle mass. Studies have shown that myostatin could also play an important role in cardiac development and physiology . The inhibition of myostatin activity has been explored as a potential therapeutic approach for muscle-wasting diseases and conditions characterized by muscle loss.

Recombinant Myostatin (Human, His Tag)

Recombinant human myostatin is produced using various expression systems, such as Escherichia coli. The recombinant protein typically includes a His tag, which is a sequence of histidine residues added to the protein to facilitate purification and detection . The His tag allows for easy purification of the protein using affinity chromatography techniques, which are based on the binding affinity between histidine residues and metal ions.

Recombinant myostatin is used in research to study its mechanisms of action, its role in muscle development, and its potential therapeutic applications. It is also used as a positive control in assays such as Western blots and ELISA .

Applications and Research

The study of myostatin has significant implications for understanding muscle biology and developing treatments for muscle-related diseases. Researchers use recombinant myostatin to investigate its effects on muscle cells, identify potential inhibitors, and explore its role in various physiological processes. The availability of high-purity recombinant myostatin with a His tag has facilitated these studies by providing a reliable and consistent source of the protein for experimental use .

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