Analytical Data
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Gene name
IBSP
- Application
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Alternative Names
IBSP;BNSP;Integrin-binding sialoProtein
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P21815
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Expression Region
129-281aa
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AA Sequence
AIQLPKKAGDITNKATKEKESDEEEEEEEEGNENEESEAEVDENEQGINGTSTNSTEAENGNGSSGGDNGEEGEEESVTGANAEDTTETGRQGKGTSKTTTSPNGGFEPTTPPQVYRTTSPPFGKTTTVEYEGEYEYTGANEYDNGYEIYESE
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Molecular Weight
32.4kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
The study of IBSP (Integrin-Binding Sialoprotein) recombinant proteins has gained significant attention in the field of biomedical research due to their pivotal role in bone metabolism and tissue engineering. IBSP, a member of the SIBLING (Small Integrin-Binding N-linked Glycoprotein) family, is primarily expressed in bone and dentin, contributing to the regulation of osteoblast function and mineralization. Its integrin-binding properties suggest that it may play a crucial role in cell-matrix interactions, influencing osteoclast activity and overall bone remodeling processes. Given its importance in bone biology, recombinant forms of IBSP are being explored for their potential therapeutic applications, including enhancing bone regeneration in osteoporosis and other metabolic bone diseases. Additionally, research into the structural and functional characteristics of these recombinant proteins can provide insights into their mechanisms of action, paving the way for the development of novel biomaterials that mimic natural extracellular matrix components. By leveraging advances in protein engineering and recombinant DNA technology, researchers aim to produce IBSP proteins with tailored functionalities that can improve scaffold designs in tissue engineering applications. Understanding IBSP's interactions at the molecular level not only enhances our grasp of bone physiology but also facilitates the design of innovative treatments for skeletal disorders. Thus, the investigation of IBSP-like recombinant proteins represents a promising frontier in the intersection of molecular biology and regenerative medicine.
