Analytical Data
-
Gene name
SNIP
- Application
-
Alternative Names
p130Cas associated protein; p130Cas-associated protein; P140; p140Cap; SNAP-25-interacting protein; SNIP; SRC kinase signaling inhibitor 1; SRCIN1; SRCN1_HUMAN
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9C0H9
-
Expression Region
1-257 aa
-
AA Sequence
MRVSEAARRQEDPLQRQRTLVEEERLRYLNDEELITQQLNDLEKSVEKIQRDVSHNHRLVPGPELEEKALVLKQLGETLTELKAHFPGLQSKMRVVLRVEVEAVKFLKEEPQRLDGLLKRCRGVTDTLAQIRRQVDEGVWPPPNNLLSQSPKKVTAETDFNKSVDFEMPPPSPPLNLHELSGPAEGASLTPKGGNPTKGLDTPGKRSVDKAVSVEVLGPGIVGGAMSQVHTFLRPSFLEWGVPILWVFFLGGGGPVP
-
Molecular Weight
55 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
SNIP (SMAD Nuclear Interacting Protein) is a key player in various biological processes, including signal transduction and transcription regulation. It has gained attention in recent years due to its role in the TGF-β (Transforming Growth Factor-beta) signaling pathway, which is crucial for cellular processes such as proliferation, differentiation, and apoptosis. Abnormalities in this pathway are often associated with various diseases, including cancer and fibrotic disorders. Research on SNIP has primarily focused on its function as a co-regulator that interacts with SMAD proteins, influencing their activity and thus modulating gene expression. Additionally, the study of SNIP-derived recombinant proteins offers potential therapeutic avenues, as these proteins can be engineered to disrupt maladaptive signaling in pathological conditions. Advances in recombinant protein technology have enabled researchers to produce SNIP variants with enhanced stability and specificity, facilitating the exploration of its functional domains and interaction partners. These investigations could lead to the development of novel strategies for treating diseases linked to dysregulated TGF-β signaling, underscoring the significance of SNIP in both basic and applied biomedical research. The insights gained from SNIP studies are pivotal for understanding its multifaceted roles within the cellular context and could ultimately pave the way for innovative therapeutic interventions. As research progresses, a deeper understanding of SNIP’s mechanisms and pathways will be crucial for leveraging its potential in clinical applications.
