Analytical Data
-
Gene name
GDF5
- Application
-
Alternative Names
CDMP1; LAP4; SYNS2; BMP14; Radotermin; Cartilage-Derived Morphogenetic Protein-1; Bone morphogenetic protein 14; Lipopolysaccharide-associated protein 4
-
Species
Mouse
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 95% as determined by SDS-PAGE.
-
Uniprot
P43027
-
Expression Region
Gln358~Arg495
-
Protein Length
Partial
-
Molecular Weight
26kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
GDF5 (Growth and Differentiation Factor 5) is a member of the TGF-β superfamily, playing a crucial role in various biological processes, including bone and cartilage development, stem cell differentiation, and tissue regeneration. The importance of GDF5 in skeletal formation and repair has prompted significant research into its potential therapeutic applications, particularly in orthopedics and regenerative medicine. The recombinant production of GDF5 has garnered attention as it enables the generation of biologically active protein for in vitro studies and potential clinical use. This involves using advanced biotechnological methods, such as recombinant DNA technology, to produce GDF5 in suitable host systems, such as bacteria or mammalian cells, thereby ensuring proper folding and bioactivity. The characterization of recombinant GDF5, including its molecular structure, activity, and interaction with downstream signaling pathways, is essential for understanding its function and therapeutic potential. Moreover, research has indicated that GDF5 can enhance the healing of bone fractures and cartilage defects, making it a promising candidate for developing novel treatments. As a result, ongoing studies aim to optimize the production and delivery methods of GDF5, assess its safety and efficacy in clinical settings, and explore its broader implications in regenerative therapies, ultimately contributing to advancements in tissue engineering and clinical interventions.
