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Rabbit Anti-MSTN Recombinant Antibody (EPR4567(2)) (CBMAB-1607-CN)

This product is a rabbit antibody that recognizes MSTN of human. The antibody EPR4567(2) can be used for immunoassay techniques such as: FC, IF, IHC-P, WB.
See all MSTN antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Mouse, Rat
Clone
EPR4567(2)
Antibody Isotype
IgG
Application
FC, IF, IHC-P, WB

Basic Information

Immunogen
Synthetic peptide corresponding to Human BMP11 + GDF8/Myostatin aa. 350 to the C-terminus.
Specificity
Human, Mouse, Rat
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!]

Format
Liquid
Buffer
59% PBS, 40% Glycerol, 0.05% BSA, pH 7.2
Preservative
0.01% Sodium azide
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
Myostatin
Introduction
This gene encodes a secreted ligand of the TGF-beta (transforming growth factor-beta) superfamily of proteins. Ligands of this family bind various TGF-beta receptors leading to recruitment and activation of SMAD family transcription factors that regulate gene expression. The encoded preproprotein is proteolytically processed to generate each subunit of the disulfide-linked homodimer. This protein negatively regulates skeletal muscle cell proliferation and differentiation. This protein acts specifically as a negative regulator of skeletal muscle growth.
Entrez Gene ID
Human2660
Mouse17700
Rat29152
UniProt ID
HumanO14793
MouseO08689
RatO35312
Alternative Names
GDF8; MSLHP
Function
Acts specifically as a negative regulator of skeletal muscle growth.
Biological Process
Cellular response to dexamethasone stimulus Source: Ensembl
Muscle cell cellular homeostasis Source: CACAO
Muscle organ development Source: ProtInc
Myoblast migration involved in skeletal muscle regeneration Source: UniProtKB
Negative regulation of insulin receptor signaling pathway Source: Ensembl
Negative regulation of kinase activity Source: Ensembl
Negative regulation of muscle hypertrophy Source: Ensembl
Negative regulation of myoblast differentiation Source: CACAO
Negative regulation of myoblast proliferation Source: AgBase
Negative regulation of protein kinase B signaling Source: CACAO
Negative regulation of satellite cell differentiation Source: AgBase
Negative regulation of skeletal muscle satellite cell proliferation Source: AgBase
Negative regulation of skeletal muscle tissue growth Source: CACAO
Ovulation cycle process Source: Ensembl
Positive regulation of lamellipodium assembly Source: UniProtKB
Positive regulation of macrophage chemotaxis Source: UniProtKB
Positive regulation of pathway-restricted SMAD protein phosphorylation Source: GO_Central
Positive regulation of transcription, DNA-templated Source: HGNC-UCL
Response to electrical stimulus Source: Ensembl
Response to estrogen Source: Ensembl
Response to ethanol Source: Ensembl
Response to gravity Source: Ensembl
Response to heat Source: Ensembl
Response to muscle activity Source: Ensembl
Response to testosterone Source: Ensembl
Skeletal muscle atrophy Source: Ensembl
SMAD protein signal transduction Source: GO_Central
Transforming growth factor beta receptor signaling pathway Source: Ensembl
Cellular Location
Secreted
Involvement in disease
Muscle hypertrophy (MSLHP):
A condition characterized by increased muscle bulk and strength. Affected individuals are exceptionally strong.
PTM
Synthesized as 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 molecule. The circulating form consists of a latent complex of the C-terminal dimer and other proteins, including its propeptide, which maintain the C-terminal dimer in a latent, inactive state. Ligand activation requires additional cleavage of the prodomain by a tolloid-like metalloproteinase.

Maeta, K., Farea, M., Nishio, H., & Matsuo, M. (2023). A novel splice variant of the human MSTN gene encodes a myostatin‐specific myostatin inhibitor. Journal of Cachexia, Sarcopenia and Muscle, 14(5), 2289-2300.

Baig, M. H., Ahmad, K., Moon, J. S., Park, S. Y., Ho Lim, J., Chun, H. J., ... & Choi, I. (2022). Myostatin and its regulation: A comprehensive review of myostatin inhibiting strategies. Frontiers in Physiology, 1277.

Sheng, H., Guo, Y., Zhang, L., Zhang, J., Miao, M., Tan, H., ... & Guo, H. (2021). Proteomic Studies on the Mechanism of Myostatin Regulating Cattle Skeletal Muscle Development. Frontiers in Genetics, 12, 752129.

Bataille, S., Chauveau, P., Fouque, D., Aparicio, M., & Koppe, L. (2021). Myostatin and muscle atrophy during chronic kidney disease. Nephrology Dialysis Transplantation, 36(11), 1986-1993.

Chen, M. M., Zhao, Y. P., Zhao, Y., Deng, S. L., & Yu, K. (2021). Regulation of myostatin on the growth and development of skeletal muscle. Frontiers in Cell and Developmental Biology, 9, 785712.

Lee, S. J. (2021). Targeting the myostatin signaling pathway to treat muscle loss and metabolic dysfunction. The Journal of clinical investigation, 131(9).

Ge, L., Dong, X., Gong, X., Kang, J., Zhang, Y., & Quan, F. (2020). Mutation in myostatin 3′ UTR promotes C2C12 myoblast proliferation and differentiation by blocking the translation of MSTN. International journal of biological macromolecules, 154, 634-643.

Bi, Y., Feng, B., Wang, Z., Zhu, H., Qu, L., Lan, X., ... & Song, X. (2020). Myostatin (MSTN) gene indel variation and its associations with body traits in Shaanbei white cashmere goat. Animals, 10(1), 168.

Bhattacharya, T. K., Shukla, R., Chatterjee, R. N., & Bhanja, S. K. (2019). Comparative analysis of silencing expression of myostatin (MSTN) and its two receptors (ACVR2A and ACVR2B) genes affecting growth traits in knock down chicken. Scientific reports, 9(1), 7789.

hyuck Choi, D., Yang, J., & Kim, Y. S. (2019). Rapamycin suppresses postnatal muscle hypertrophy induced by myostatin-inhibition accompanied by transcriptional suppression of the Akt/mTOR pathway. Biochemistry and Biophysics Reports, 17, 182-190.

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

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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