Analytical Data
-
Gene name
SAH1
- Application
-
Alternative Names
SAH1；KIAA0790；PEPE1；SAM and SH3 domain-containing Protein 1
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P39954
-
Expression Region
1-448aa
-
AA Sequence
MSAPAQNYKIADISLAAFGRKEIELAEHEMPGLMAIRKAYGDVQPLKGARIAGCLHMTIQTAVLIETLVALGAEVTWSSCNIYSTQDHAAAAIAASGVPVFAWKGETEEEYLWCIEQQLFAFKDNKKLNLILDDGGDLTTLVHEKHPEMLEDCFGLSEETTTGVHHLYRMVKEGKLKVPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMLAGKVAVVAGYGDVGKGCAAALRGMGARVLVTEIDPINALQAAMEGYQVVTMEDASHIGQVFVTTTGCRDIINGEHFINMPEDAIVCNIGHFDIEIDVAWLKANAKECINIKPQVDRYLLSSGRHVILLANGRLVNLGCATGHSSFVMSCSFSNQVLAQIALFKSNDKSFREKHIEFQKTGPFEVGVHVLPKILDEAVAKFHLGNLGVRLTKLSKVQSEYLGIPEEGPFKADHYR
-
Molecular Weight
53.0 kDa
-
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
SAH1 recombinase, an important component in the field of molecular biology, has gained attention for its role in homologous recombination and genetic engineering. Understanding its mechanism is crucial for advancing genetic manipulation techniques, such as gene editing and transgenic organism development. Emerging studies have revealed that SAH1 is not only involved in the repair of double-strand breaks but also plays a vital role in maintaining genome stability during cell division. Researchers are particularly interested in its potential applications for improving crop resilience, developing therapies for genetic disorders, and enhancing synthetic biology platforms. The exploration of SAH1's structure and function has been facilitated by advanced techniques like X-ray crystallography and cryo-electron microscopy, further illuminating its interactions with DNA and other protein complexes. As a result, SAH1 is positioned as a key target for biotechnological innovations and therapeutic strategies, underscoring the importance of continued research in this area to unlock its full potential in both agriculture and medicine.
