Analytical Data
-
Gene name
SPARCL1
- Application
-
Alternative Names
SC1; PIG33; Mast9; Hevin; High endothelial venule protein
-
Species
Rat
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 95% as determined by SDS-PAGE.
-
Uniprot
P24054
-
Expression Region
Ser402~Asp627
-
Molecular Weight
30kDa
-
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
SPARCL1, or SPARC-like 1, is a matricellular protein that plays a crucial role in cell adhesion, migration, and interaction with the extracellular matrix. Its expression is often associated with various physiological processes, including tissue repair, development, and inflammation. Notably, SPARCL1 has gained attention in cancer research due to its potential tumor-suppressive properties; it is frequently downregulated in several malignancies, suggesting a role in inhibiting cancer progression and metastasis. Additionally, SPARCL1 has been implicated in neuronal development, with studies suggesting its involvement in synaptic regulation and neurogenesis. Given its diverse roles in various biological contexts, researchers have increasingly focused on characterizing SPARCL1 through recombinant protein studies, which involve producing SPARCL1 in a controlled environment to investigate its biochemical properties and interactions. By elucidating the functional mechanisms of SPARCL1, researchers aim to uncover its potential as a therapeutic target or biomarker in cancer and other diseases, thereby advancing our understanding of its contributions to cellular processes and pathology. The exploration of SPARCL1's structure-function relationship, along with its regulatory mechanisms, remains a significant area of interest, reflecting the growing recognition of matricellular proteins in health and disease.
