Recombinant Human/Mouse/Rat GDF-11 Protein

Beta LifeScience SKU/CAT #: BL-1835NP
BL-1835NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-1835NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human/Mouse/Rat GDF-11 Protein

Beta LifeScience SKU/CAT #: BL-1835NP
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Product Overview

Description Recombinant Human/Mouse/Rat Growth Differentiation Factor 11 is produced by our Mammalian expression system and the target gene encoding Asn299-Ser407 is expressed.
Accession O95390
Synonym Growth/differentiation factor 11; GDF-11; Bone morphogenetic protein 11; BMP-11
Gene Background Growth/differentiation factor 11(GDF-11) is a secreted protein, which belongs to the transforming growth factor beta superfamily. GDF-11 controls anterior-posterior patterning by regulating the expression of Hox genes. The secreted signal acts globally to specify positional identity along the anterior/posterior axis during development. GDF11 has been shown to suppress neurogenesis through a pathway similar to that of myostatin, including stopping the progenitor cell-cycle during G-phase. The similarities between GDF11 and myostatin imply a likelihood that the same regulatory mechanisms are used to control tissue size during both muscular and neural development.
Molecular Mass 12.5 KDa
Apmol Mass 13-20 KDa, reducing conditions
Formulation Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 50% glycerol, pH 7.4.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution
Storage Store at ≤-70°C, stable for 6 months after receipt.Store at ≤-70°C, stable for 3 months under sterile conditions after opening.Please minimize freeze-thaw cycles.
Shipping The product is shipped on dry ice/polar packs.Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

Target Details

Target Function Secreted signal that acts globally to regulate anterior/posterior axial patterning during development. May play critical roles in patterning both mesodermal and neural tissues. It is required for proper vertebral patterning and orofacial development. Signals through activin receptors type-2, ACVR2A and ACVR2B, and activin receptors type-1, ACVR1B, ACVR1C and TGFBR1 leading to the phosphorylation of SMAD2 and SMAD3.
Subcellular Location Secreted.
Protein Families TGF-beta family
Database References
Tissue Specificity In the embryo, strong expression is seen in the palatal epithelia, including the medial edge epithelial and midline epithelial seam of the palatal shelves. Less pronounced expression is also seen throughout the palatal shelf and tongue mesenchyme.

Gene Functions References

  1. The serum content of GDF11 was much less in esophageal cancer patients than in the control group. Esophageal GDF II in cancer patients was correlated with cancer differentiation: the higher the degree of differentiation, the higher the content of GDF11. PMID: 30213293
  2. Physical inactivity was significantly related to the decreased GDF11 levels in COPD. PMID: 29731621
  3. GDF11 expression was decreased in COPD patients' serum and cells when compared with that of healthy people. PMID: 29680737
  4. GDF11 may be a relevant myostatin-interacting peptide to successful aging in humans PMID: 28701523
  5. The Growth Differentiation Factor 11 (GDF11) and Myostatin (MSTN) in tissue specific aging. PMID: 28472635
  6. Tumor-suppressor inactivation of GDF11 occurs by precursor sequestration in triple-negative breast cancer PMID: 29161592
  7. These studies identify distinctive structural features of GDF11 that enhance its potency, relative to GDF8; however, the biological consequences of these differences remain to be determined. PMID: 28257634
  8. In elderly Chinese women, osteoporosis risk was significantly increased with increases in GDF11 serum levels. PMID: 27557752
  9. A Prodomain Fragment from the Proteolytic Activation of Growth Differentiation Factor 11 Remains Associated with the Mature Growth Factor and Keeps It Soluble PMID: 28715204
  10. MSTN, but not GDF11, declines in healthy men throughout aging. PMID: 27304512
  11. GDF11 is highly concentrated in human platelets. PMID: 27509407
  12. The crystal structure of GDF11 was determined to a resolution of 1.50 A. PMID: 26919518
  13. GDF11 is essential for mammalian development and has been suggested to regulate aging of multiple tissues. It functions in the heart, skeletal muscle, and brain. Review. PMID: 27034275
  14. GDF11 inhibits rather than helps muscle regeneration. PMID: 26001423
  15. Show that there is no age-related cardiac hypertrophy in disease-free 24-month-old C57BL/6 mice and that restoring GDF11 in old mice has no effect on cardiac structure or function. PMID: 26383970
  16. in vitro sprout formation was increased as well by GDF11 treatment PMID: 26026854
  17. Suggest GDF11 functions as encephalic regionalizing factor in neural differentiated mouse embryonic stem cells. PMID: 25352416
  18. GDF11 is a critical rheostat for bone turnover and a key integrator of bone homeostasis. PMID: 25534870
  19. These data demonstrate GDF11 to be a master regulator of neural stem cell transcription that can suppress cell proliferation and migration by regulating the expression of numerous genes involved in both these processes PMID: 24244313
  20. Expression of GDF11, a cytokine which blocks terminal erythroid maturation, was increased in erthyroblasts of thalassemic patients. PMID: 24658077
  21. Quantitative real-time reverse transcription-PCR in colorectal cancer specimens obtained from 130 patients showed that GDF11 mRNA expression in cancer tissue was significantly higher than in normal tissue PMID: 17912435
  22. Members of the transforming growth factor beta (TGFbeta) superfamily, bone morphogenetic protein 2 (BMP2), and growth and differentiation factor 11 (GDF11), can signal cultured RGCs to form dendrites. PMID: 17997109
  23. We propose that Pcsk5, at least in part via GDF11, coordinately regulates caudal Hox paralogs, to control anteroposterior patterning, nephrogenesis, skeletal, and anorectal development. PMID: 18519639
  24. Differential antagonism of activin, myostatin and growth and differentiation factor 11 by wild-type and mutant follistatin. PMID: 18535106
  25. Both WFIKKN1 and WFIKKN2 have high affinity for growth and differentiation factors 8 and 11. PMID: 18596030
  26. Myostatin or 20 ng/mL BMP-11 maintain the colony and cellular morphology of undifferentiated hESC, maintain POU5f1, NANOG, TRA-1-60, and SSEA4 expression, and display increased SMAD2/3 phosphorylation PMID: 19751112

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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