Recombinant Human Growth/differentiation factor 11 (GDF11)

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Code CSB-EP009344HU
MSDS
Size $224
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP009344HU 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 CSB-EP009344HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) GDF11.
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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
GDF11
Uniprot No.
Research Area
Neuroscience
Alternative Names
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)
Source
E.coli
Expression Region
299-407aa
Target Protein Sequence
NLGLDCDEHSSESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGQCEYMFMQKYPHTHLVQQANPRGSAGPCCTPTKMSPINMLYFNDKQQIIYGKIPGMVVDRCGCS
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
28.5kDa
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-SUMO-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description

Discover the remarkable quality of our Recombinant Human GDF11, meticulously designed for optimal performance in neuroscience research. This product features the full length of mature Growth/differentiation factor 11 (GDF-11), a critical protein involved in the regulation of cellular growth and differentiation, particularly in the nervous system.

Produced in E.coli, the Recombinant Human GDF11 covers an expression region of 299-407 amino acids and is equipped with an N-terminal 6xHis-SUMO tag to ensure efficient purification and detection. With a purity greater than 90% as determined by SDS-PAGE, our product is available in both liquid and lyophilized powder formats, catering to diverse research requirements. Choose the precision-crafted Recombinant Human GDF11 to elevate your neuroscience research with confidence and consistency.

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Target Background

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.
Gene References into Functions
  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

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Subcellular Location
Secreted.
Protein Families
TGF-beta family
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.
Database Links

HGNC: 4216

OMIM: 603936

KEGG: hsa:10220

STRING: 9606.ENSP00000257868

UniGene: Hs.600883

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