Myostatin Human

Myostatin Human Recombinant

Myostatin Human Recombinant produced in E.Coli is a homodimer, non-glycosylated polypeptide chain containing 2 x 109 amino acids and having a total molecular mass of 24814 Dalton.
The GDF-8 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23803
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Myostatin Human, HEK

Myostatin Human Recombinant, HEK

Myostatin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn24-Ser375) containing a total of 360 amino acids, having a calculated molecular mass of 41.1kDa. Myostatin is fused to a 2 aa N-terminal linker and a 6 aa His tag at N-Terminus.
Shipped with Ice Packs
Cat. No.
BT23908
Source
HEK 293.
Appearance
Filtered colorless solution.

Myostatin Human, His

Myostatin Human Recombinant, His Tag

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.
Shipped with Ice Packs
Cat. No.
BT23984
Source
Escherichia Coli.
Appearance
Filtered white lyophilized (freeze-dried) powder.

Myostatin Propeptide Human

Myostatin Propeptide Human Recombinant

Recombinant Human Myostatin Propeptide is a 27.8kDa protein containing 244 amino acid residues of the human Myostatin Propeptide.
Shipped with Ice Packs
Cat. No.
BT24061
Source
Escherichia Coli.
Appearance
Sterile Filtered white lyophilized (freeze-dried) powder.

Myostatin Propeptide Human, HEK

Myostatin Propeptide Human Recombinant, HEK

Myostatin Propetide Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn24-Arg266) containing a total of 253 amino acids, having a calculated molecular mass of 29.1kDa.
Myostatin Propetide is fused to a 10 aa C-terminal His tag.
Shipped with Ice Packs
Cat. No.
BT24164
Source
HEK 293.
Appearance
Filtered colorless solution.
Definition and Classification

Myostatin, also known as growth differentiation factor 8 (GDF8), is a secreted protein that belongs to the transforming growth factor-beta (TGF-β) superfamily . It is primarily known for its role as a negative regulator of skeletal muscle growth . Myostatin is classified under the TGF-β superfamily, which includes other growth and differentiation factors such as bone morphogenetic proteins (BMPs) and activins .

Biological Properties

Key Biological Properties: Myostatin is a myokine produced and released by myocytes, acting on muscle cells to inhibit muscle growth . It is a secreted growth differentiation factor that is assembled and produced in skeletal muscle before being released into the bloodstream .

Expression Patterns and Tissue Distribution: Myostatin is predominantly expressed in skeletal muscle tissue, but it is also found in other tissues such as the heart and adipose tissue . Its expression is tightly regulated and is highest in muscles involved in locomotion and posture .

Biological Functions

Primary Biological Functions: The primary function of myostatin is to inhibit muscle growth and differentiation . It plays a crucial role in regulating muscle mass by limiting the number and size of muscle fibers .

Role in Immune Responses and Pathogen Recognition: While myostatin’s primary role is in muscle regulation, it also has implications in immune responses. It can influence the immune system by modulating the activity of immune cells and cytokines .

Modes of Action

Mechanisms with Other Molecules and Cells: Myostatin exerts its effects through both paracrine and endocrine modes of action . It binds to the activin type II receptor, leading to the recruitment of coreceptors such as Alk-3 or Alk-4 . This binding initiates a signaling cascade involving the activation of SMAD transcription factors, particularly SMAD2 and SMAD3 .

Binding Partners and Downstream Signaling Cascades: Upon binding to its receptors, myostatin activates downstream signaling pathways that inhibit muscle cell growth and promote protein degradation . It inhibits Akt-induced protein synthesis and stimulates ubiquitin-regulated protein degradation .

Regulatory Mechanisms

Regulation of Expression and Activity: Myostatin expression and activity are regulated at multiple levels, including transcriptional and post-translational modifications . Transcriptional regulation involves various transcription factors and promoter elements that control the gene’s expression .

Post-Translational Modifications: Myostatin undergoes several post-translational modifications, including proteolytic processing and glycosylation, which are essential for its activation and function .

Applications

Biomedical Research: Myostatin has significant applications in biomedical research, particularly in understanding muscle-wasting diseases and developing therapeutic strategies to counteract muscle loss .

Diagnostic Tools and Therapeutic Strategies: Myostatin inhibitors are being explored as potential treatments for conditions such as muscular dystrophy, cachexia, and sarcopenia . Diagnostic tools measuring myostatin levels can help in the assessment of muscle health and disease progression .

Role in the Life Cycle

Development to Aging and Disease: Myostatin plays a critical role throughout the life cycle, from embryonic development to aging . During development, it regulates the formation of muscle fibers, while in adulthood, it maintains muscle homeostasis . Dysregulation of myostatin is associated with various muscle-related diseases and conditions, including muscle atrophy and hypertrophy .

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