Analytical Data
-
Gene name
GFP
- Application
-
Alternative Names
GFP；NIDHPO;Nidogen-1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P42212
-
Expression Region
1-238aa
-
AA Sequence
MSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTFSYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITHGMDELYK
-
Molecular Weight
42.9kDa
-
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
Green Fluorescent Protein (GFP) was originally discovered in the jellyfish Aequorea victoria and has since become a revolutionary tool in molecular and cellular biology. Its natural fluorescence, due to the intrinsic chromophore that forms through spontaneous post-translational modification, allows researchers to visualize and track proteins and cellular processes in real-time, without the need for additional labels or dyes. The ability to genetically encode GFP into target proteins has enabled the development of a wide variety of GFP fusion proteins, facilitating studies in diverse fields such as gene expression, protein localization, and cellular dynamics. Furthermore, advancements in the engineering of GFP have led to the creation of various derivatives with altered spectral properties, improving their versatility in multi-color imaging applications. The study of GFP and its derivatives has not only provided insights into fundamental biological processes but has also paved the way for innovative approaches in medicine, biotechnology, and environmental monitoring. As research continues, the applications of GFP and its recombinant variants are expected to expand, offering new avenues for exploration in the life sciences.
