Analytical Data
-
Gene name
SAMHD1
- Application
-
Alternative Names
MOP5
-
Species
Human
-
Source
Baculovirus
-
Tag
N-His;N-Strep
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9Y3Z3-1
-
Expression Region
Q2-M626
-
Protein Length
Partial
-
Molecular Weight
75.3 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
SAMHD1 (SAM domain and HD domain-containing protein 1) is a crucial host factor that plays a significant role in innate immunity, particularly in the context of viral infections. It is known for its ability to hydrolyze deoxynucleotide triphosphates (dNTPs), thereby limiting the availability of these building blocks for viral replication, particularly in retroviruses like HIV-1. The importance of SAMHD1 has gained attention in recent years due to its dual role as both a restriction factor and a potential mediator of immune responses. Mutations or dysregulation of SAMHD1 can lead to enhanced susceptibility to infections and have been implicated in certain disorders, including some forms of immunodeficiency and cancer. Researchers have focused on the structure and enzymatic activity of SAMHD1, aiming to understand the molecular mechanisms underlying its antiviral functions. Furthermore, the study of SAMHD1 is significant for developing therapeutic strategies against viral infections and understanding how viruses, particularly HIV, evolve mechanisms to counteract host defenses. Advances in protein engineering and structural biology are facilitating deeper insights into the functionality and regulation of SAMHD1, making it a target of interest for both basic and applied research in virology and immunology. Understanding the interactions between SAMHD1 and viral components can potentially lead to innovative antiviral therapies and contribute to our broader knowledge of immune regulation.











