IBSP Human, HEK
HEK293 Cells.
Integrin Binding Sialoprotein, Integrin-Binding Sialoprotein, Bone Sialoprotein II, Cell-Binding Sialoprotein, BSP II , BNSP, Bone Sialoprotein, BSP-II, SP-II, BSP.
Greater than 90.0% as determined by SDS-PAGE.
Description
IBSP Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain (17-317 a.a) containing a total of 307 amino acids and having a molecular mass of 34.3 kDa.
IBSP is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Product Specs
Recombinant human IBSP protein, expressed in HEK293 cells, is a single glycosylated polypeptide chain. It consists of amino acids 17 to 317, totaling 307 amino acids, with a molecular weight of 34.3 kDa. The IBSP protein has a 6-amino acid His-tag fused at its C-terminus. Purification is achieved using proprietary chromatographic methods.
The IBSP protein is provided as a solution at a concentration of 0.5 mg/ml in a buffer composed of 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To further enhance stability during long-term storage, adding a carrier protein like HSA or BSA (0.1%) is advised. It's crucial to minimize repeated cycles of freezing and thawing.
The purity of this protein is greater than 90%, as determined by SDS-PAGE analysis.
The biological activity of this protein is greater than 40%, as measured by its ability to support the adhesion of MCF7 human breast cancer cells to a surface coated with the protein at a concentration of 3 µg/ml.
Integrin Binding Sialoprotein, Integrin-Binding Sialoprotein, Bone Sialoprotein II, Cell-Binding Sialoprotein, BSP II , BNSP, Bone Sialoprotein, BSP-II, SP-II, BSP.
HEK293 Cells.
FSMKNLHRRV KIEDSEENGV FKYRPRYYLY KHAYFYPHLK RFPVQGSSDS SEENGDDSSE EEEEEEETSN EGENNEESNE DEDSEAENTT LSATTLGYGE DATPGTGYTG LAAIQLPKKA GDITNKATKE KESDEEEEEE EEGNENEESE AEVDENEQGI NGTSTNSTEA ENGNGSSGGD NGEEGEEESV TGANAEDTTE TGRQGKGTSK TTTSPNGGFE PTTPPQVYRT TSPPFGKTTT
VEYEGEYEYT GANEYDNGYE IYESENGEPR GDNYRAYEDE YSYFKGQGYD GYDGQNYYHH QHHHHHH.
Product Science Overview
Integrin Binding Sialoprotein, also known as Bone Sialoprotein II, is a significant structural protein found in the bone matrix. It is encoded by the IBSP gene and is synthesized by various skeletal-associated cell types, including hypertrophic chondrocytes, osteoblasts, osteocytes, and osteoclasts . The recombinant form of this protein, produced in Human Embryonic Kidney 293 cells, is often used in research due to its high purity and biological activity .
Integrin Binding Sialoprotein is known for its rich sialic acid content and multiple functional domains. These include an RGD (arginine-glycine-aspartic acid) cell-binding domain and polyglutamic acid stretches . These structural features enable the protein to interact with various cells, affecting adhesion and migration. The recombinant form produced in Human Embryonic Kidney 293 cells is a single, glycosylated polypeptide chain containing 307 amino acids and has a molecular mass of 34.3 kDa .
Integrin Binding Sialoprotein plays a crucial role in bone mineralization. It acts as a nucleator for calcium phosphate crystals, providing a scaffold for bone formation . This protein binds tightly to hydroxyapatite, a major component of bone, and appears to form an integral part of the mineralized matrix . It also promotes the adhesion and migration of various cells via the alpha-V/beta-3 integrin receptor .
Integrin Binding Sialoprotein is involved in several cell signaling pathways. It has been linked to processes such as angiogenesis, inflammation, and cellular differentiation . These signaling pathways highlight the broader physiological roles of this protein beyond its structural functions in the bone matrix.
Research on Integrin Binding Sialoprotein has significant biomedical implications. It is being investigated for its potential roles in bone disorders such as osteoporosis and periodontal disease . Understanding how this protein influences mineralization and cell signaling can provide insights into bone health and disease mechanisms.
