Recombinant Human Growth/Differentiation Factor 11 (GDF11) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-02780P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) GDF11.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) GDF11.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) GDF11.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) GDF11.

Recombinant Human Growth/Differentiation Factor 11 (GDF11) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-02780P
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Product Overview

Description Recombinant Human Growth/Differentiation Factor 11 (GDF11) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb O95390
Target Symbol GDF11
Synonyms BMP 11; BMP-11; BMP11; Bone morphogenetic protein 11; GDF 11; GDF-11; Gdf11; GDF11_HUMAN; Growth differentiation factor 11; Growth/differentiation factor 11
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence NLGLDCDEHSSESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGQCEYMFMQKYPHTHLVQQANPRGSAGPCCTPTKMSPINMLYFNDKQQIIYGKIPGMVVDRCGCS
Expression Range 299-407aa
Protein Length Full Length of Mature Protein
Mol. Weight 28.5kDa
Research Area Neuroscience
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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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