Recombinant Mouse GDF 5 Protein

Beta LifeScience SKU/CAT #: BLA-1106P

Recombinant Mouse GDF 5 Protein

Beta LifeScience SKU/CAT #: BLA-1106P
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Product Overview

Host Species Mouse
Accession P43027
Synonym BMP14 Cartilage derived morphogenetic protein 1 Cartilage-derived morphogenetic protein 1 CDMP-1 CDMP1 GDF-5 Gdf5 GDF5_HUMAN Growth differentiation factor 5 Growth/differentiation factor 5 LAP4 OS5 Radotermin SYNS2
Description Recombinant Mouse GDF 5 Protein was expressed in E.coli. It is a Full length protein
Source E.coli
Molecular Weight 27 kDa
Purity Greater than 98% SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Determined by its ability to induce alkaline phosphatase production by ATDC-5 cells. The expected ED50 for this effect is 1.0 - 2.0 µg/ml.
Formulation Lyophilised
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Store at -20°C. buffer containing a carrier protein (example 0.1% BSA) This product is an active protein and may elicit a biological response in vivo, handle with caution.

Target Details

Target Function Growth factor involved in bone and cartilage formation. During cartilage development regulates differentiation of chondrogenic tissue through two pathways. Firstly, positively regulates differentiation of chondrogenic tissue through its binding of high affinity with BMPR1B and of less affinity with BMPR1A, leading to induction of SMAD1-SMAD5-SMAD8 complex phosphorylation and then SMAD protein signaling transduction. Secondly, negatively regulates chondrogenic differentiation through its interaction with NOG. Required to prevent excessive muscle loss upon denervation. This function requires SMAD4 and is mediated by phosphorylated SMAD1/5/8. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes.
Subcellular Location Secreted. Cell membrane.
Protein Families TGF-beta family
Database References
Associated Diseases Defects in Gdf5 are the cause of brachypodism (bp) which alters the length and numbers of bones in the limbs but spares the axial skeleton.

Gene Functions References

  1. Microarray analysis of satellite cells showed that expression of growth differentiation factor 5 (Gdf5) mRNA was markedly increased in Dnmt3a-KO mice. The DNA methylation level of the Gdf5 promoter was markedly decreased in Dnmt3a-KO satellite cells. PMID: 29146735
  2. spatiotemporal dynamics of Gdf5 expression may instruct lineage divergence. PMID: 27292641
  3. he large array of modular enhancers for Gdf5 provide a new foundation for studying the spatial specificity of joint patterning in vertebrates, as well as new candidates for regulatory regions that may also influence osteoarthritis risk in human population PMID: 27902701
  4. Growth differentiation factor 5 is a novel target-derived factor that promotes sympathetic axon growth and branching and makes a distinctive regional contribution to the establishment of sympathetic innervation. PMID: 26878848
  5. Dach2 and Hdac9 mediate the effects of muscle activity on muscle reinnervation; Myog and Gdf5 appear to stimulate muscle reinnervation through parallel pathways PMID: 26483211
  6. Clonal expansion of Gdf5 progenitors contributes to linear growth of the enthesis. PMID: 26141957
  7. GDF5 might play a critical role in 3T3-L1 preadipocyte differentiation PMID: 25078108
  8. These results suggest that PI3K/Akt signals play a role in the GDF5-mediated brown adipogenesis through a mechanism related to activation of the Smad pathway. PMID: 24944017
  9. These results suggest that brown adipogenesis and energy homeostasis are both positively regulated by the GDF5/BMPR/Smad/PGC-1alpha signaling pathway in adipose tissues. PMID: 24062245
  10. apical and basal dendritic arbours of pyramidal cells throughout the hippocampus were stunted in both homozygous and heterozygous Gdf5 null mutants, indicating that dendrite size and complexity are sensitive to the level of endogenous GDF5 synthesis. PMID: 24173804
  11. This work implicates SOX11 as a potential regulator of GDF5 expression in joint maintenance and suggests a possible role in the pathogenesis of osteoarthritis PMID: 23356643
  12. A novel molecular mechanism of a GDF5 mutation affecting chondrogenesis and osteogenesis, is reported. PMID: 21976273
  13. Data show that revealed notochord cells in Gdf-5-null mice correctly form nuclei pulposi. PMID: 21278629
  14. Although GDF-5 deficiency did not compromise long-term fracture healing, a delay in cartilage formation and remodeling supports roles for GDF-5 in the early phase of bone repair. PMID: 21590487
  15. data suggest that decreased GDF5 levels in mice can contribute to osteoarthritis development by different mechanisms including altered loading and subchondral bone changes. PMID: 20805298
  16. potential target gene of HOXA13 PMID: 20034107
  17. These observations indicate that GDF-5 regulates differentiation of both dental papilla and follicle during odontogenesis, co-operatively with other growth factors such as BMP-2. PMID: 19909214
  18. GDF5 deficiency caused a 17% increase in medium diameter (100-225 nm) collagen fibrils in tail tendon, at the expense of larger fibrils. Thus, GDF5 may play a role in tendon homeostasis in mice. PMID: 11913489
  19. GDF-5-deficient femora were weaker (-31%) and more compliant (-57%) than controls when tested to failure in torsion. PMID: 11996912
  20. GDF-5 induced cell cycle arrest in the G1 phase before the appearance of apoptosis in mouse B cell hybridoma HS-72 cells PMID: 12464389
  21. role of single and double mutations in the mouse Gdf6 and Gdf5 genes in multiple joint and skeletal patterning defects PMID: 12606286
  22. GDF5 regulates expression of connexin 43 promoter in osteoblasts ans embryos PMID: 12881039
  23. GDF-5 may play an important role in modulating tendon repair. Data are consistent with previously posited roles for GDF-5 in cell recruitment, migration/adhesion, differentiation, proliferation, and angiogenesis. PMID: 12919870
  24. concordance between the mRNA expression profiles of GDF5 and the gap junction gene, Cx43, in the mouse embryonic limb, spine, and heart, consistent with coordinated functions for these gene products during developmental organogenesis PMID: 14613311
  25. GDF-5 synergistically enhances de novo bone formation capability of bone marrow mesenchymal cells in hyaluronan composites in rats. PMID: 14661262
  26. GDF5 has a role in growth of developing joints, including early joint interzones, adult articular cartilage, and the joint capsule PMID: 15492776
  27. Excessive apoptosis in the absence of GDF5 results in developmental failure of the phalanges. PMID: 15542031
  28. Deficiency in knockout mice affects biomechanical behavior and ultrastructure of mouse skin. PMID: 16112556
  29. Results describe 2 mutations in growth and differentiation factor 5 (GDF5) that alter receptor-binding affinities. PMID: 16127465
  30. Results suggest that CDMP1/GDF5 requires cleavage by two distinct proteolytic enzymes. PMID: 16829522
  31. Study further highlights a critical role of GDF5 in joint formation and the development of osteoarthritis (OA), and this should serve as a good model for OA. PMID: 17656374
  32. association of Gdf5-mediated signaling pathways with Trps1 and the phenotypic changes of ATDC5 cells due to over-expression or suppression of Trps1 PMID: 18363966
  33. Absence of GDF5 does not interfere with lipopolysaccharides toll-like receptor signaling in a mouse model of arthritis. PMID: 19604444

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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