-
Chinese (Simplified)
-
English
-
German
-
Korean
-
Spanish
Chinese (Simplified)
English
German
Korean
Spanish
Sign up for an account to enjoy easy online shopping and instant order tracking.
Unlock the potential of Bone Sialoprotein 2 (BSP2) in your research with our premium Recombinant Human IBSP protein. BSP2, also known as Integrin-Binding Sialoprotein, is an essential component of the extracellular matrix in bone and dentin, playing a crucial role in the process of bone mineralization, cell adhesion, and integrin-mediated signaling pathways. BSP2 is a key protein in the study of bone metabolism, osteoporosis, and dental pathologies, making it an indispensable tool for researchers in these fields. Our Recombinant Human IBSP protein is expressed in E. coli, ensuring a consistent and reliable product for your research needs. The partial protein length, covering the expression region from 129-281aa, maintains the crucial functional domains of BSP2. An N-terminal 6xHis-SUMO tag has been added to our recombinant IBSP protein to enable straightforward protein purification and detection. With a purity greater than 90% as determined by SDS-PAGE, our Recombinant Human IBSP protein is supplied as a lyophilized powder, providing you with a dependable and effective tool for your bone metabolism and integrin-mediated signaling research endeavors.
Unlock the potential of Bone Sialoprotein 2 (BSP2) in your research with our premium Recombinant Human IBSP protein. BSP2, also known as Integrin-Binding Sialoprotein, is an essential component of the extracellular matrix in bone and dentin, playing a crucial role in the process of bone mineralization, cell adhesion, and integrin-mediated signaling pathways. BSP2 is a key protein in the study of bone metabolism, osteoporosis, and dental pathologies, making it an indispensable tool for researchers in these fields.
Our Recombinant Human IBSP protein is expressed in E. coli, ensuring a consistent and reliable product for your research needs. The partial protein length, covering the expression region from 129-281aa, maintains the crucial functional domains of BSP2. An N-terminal 6xHis-SUMO tag has been added to our recombinant IBSP protein to enable straightforward protein purification and detection. With a purity greater than 90% as determined by SDS-PAGE, our Recombinant Human IBSP protein is supplied as a lyophilized powder, providing you with a dependable and effective tool for your bone metabolism and integrin-mediated signaling research endeavors.
| Cat.No | ACP02337 | Target Name | IBSP |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | E.coli |
| Expression Range | 129-281aa | Mol Weight | 32.4kDa |
| Protein Length | Partial | Purity | Greater than 90% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P21815 |
|---|
Uniprot Id
P21815
Target Species
Human
Target Name
IBSP
Target Full Name
Integrin-binding sialoprotein
Target Function
Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Promotes Arg-Gly-Asp-dependent cell attachment.
Target Subcellular Location
Secreted.
Target Research Area
others
Target Synonyms
BNSP; Bone sialoprotein 2; Bone sialoprotein II; BSP; BSP II; BSPII; Cell binding sialoprotein; Cell-binding sialoprotein; IBSP; Integrin binding sialoprotein; Integrin-binding sialoprotein; SIAL_HUMAN; SPII
Target Background
The protein encoded by this gene is a major structural protein of the bone matrix. It constitutes approximately 12% of the noncollagenous proteins in human bone and is synthesized by skeletal-associated cell types, including hypertrophic chondrocytes, osteoblasts, osteocytes, and osteoclasts. The only extraskeletal site of its synthesis is the trophoblast. This protein binds to calcium and hydroxyapatite via its acidic amino acid clusters, and mediates cell attachment through an RGD sequence that recognizes the vitronectin receptor.
Notification