Analytical Data
-
Gene name
Osteonectin
- Application
-
Alternative Names
Osteonectin；ON；SPARC
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P09486
-
Expression Region
18-303aa
-
AA Sequence
MSYYHHHHHH DYDIPTTENL YFQGAMGSA+P QQEALPDETE VVEETVAEVT EVSVGANPVQ VEVGEFDDGA EETEEEVVAE NPCQNHHCKH GKVCELDENN TPMCVCQDPT SCPAPIGEFE KVCSNDNKTF DSSCHFFATK CTLEGTKKGH KLHLDYIGPC KYIPPCLDSE LTEFPLRMRD WLKNVLVTLY ERDEDNNLLT EKQKLRVKKI HENEKRLEAG DHPVELLARD FEKNYNMYIF PVHWQFGQLD QHPIDGYLSH TELAPLRAPL IPMEHCTTRF FETCDLDNDK YIALDEWAGC FGIKQKDIDK DLVI
-
Molecular Weight
36.1 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
Osteonectin, also known as SPARC (Secreted Protein Acidic and Rich in Cysteine), is a glycoprotein that plays a crucial role in bone remodeling and mineralization. It is predominantly expressed in bone and dental tissues, where it interacts with collagen and other extracellular matrix components, thus influencing cell adhesion, proliferation, and differentiation. Research into recombinant osteonectin proteins has gained momentum due to their potential therapeutic applications in bone regeneration and repair. Understanding its structure-function relationship and the molecular pathways it influences is essential for developing strategies to enhance bone healing in various conditions, including fractures and osteoporosis. Recent studies have focused on the production of recombinant osteonectin using recombinant DNA technology to investigate its biochemical properties, functionality, and potential as a biomaterial in tissue engineering. Moreover, insights into osteonectin's role in modulating cell behavior and its interactions with growth factors and cytokines could pave the way for novel treatments that harness its regenerative capabilities. Hence, the exploration of recombinant osteonectin proteins represents a promising frontier in bone biology and regenerative medicine.
