Analytical Data
-
Gene name
GH2
- Application
-
Alternative Names
GH-V; GHL; GHV; hGH-V; Growth Hormone Variant; Placenta-Specific Growth Hormone; Placental Specific Growth Hormone
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P01242
-
Expression Region
Phe27~Phe217
-
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
The research on GH2 recombinant proteins focuses on the study of growth hormone, specifically the GH2 isoform, which plays a crucial role in growth and metabolic regulation in various species, including humans. Growth hormone is primarily produced by the pituitary gland and is vital for normal physical development and metabolic processes. The GH2 protein exhibits significant structural and functional differences compared to other isoforms, leading to an increased interest in understanding its unique biological roles and therapeutic potential. The recombinant production of GH2 proteins allows for detailed structural studies, functional assays, and the exploration of their applications in biomedical research and clinical therapies. Advances in recombinant DNA technology have enabled scientists to produce these proteins in various host systems, facilitating large-scale production and purification, essential for extensive studies on its effects on growth, metabolism, and various disorders associated with GH deficiencies or abnormalities. Overall, the investigation into GH2 recombinant proteins presents valuable insights into growth modulation, potential treatment options for growth disorders, and applications within regenerative medicine and biopharmaceuticals. This research sheds light on the complex mechanisms of hormone action, allowing for the development of targeted therapies that could improve health outcomes related to growth and development.
