Recombinant Human Bone sialoprotein 2 (IBSP),Partial

In Stock
Code CSB-EP010945HU(A4)
Size $1812
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names IBSP
Uniprot No. P21815
Research Area others
Alternative Names
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
Species Homo sapiens (Human)
Source E.coli
Expression Region 129-281aa
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 32.4kDa
Protein Length Partial
Tag Info N-terminal 6xHis-SUMO-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
and FAQs
Protein FAQs
Storage Condition Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time 3-7 business days
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

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Target Background

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.
Gene References into Functions
  1. These data indicate that secretome derived from salivary gland cancer cells can influence the expression of two potential biomarkers of oral cancer-namely, bone sialoprotein (BSP) and dentin sialoprotein (DSP)-in normal salivary gland cells. PMID: 27881474
  2. In conclusion, serum levels of BSP, ALP, ICTP, and PSA increased in patients with bone metastases, and combined detection of all markers could improve the positive-predictive value. PMID: 27323113
  3. Preameloblast-Derived Factors Mediate Osteoblast Differentiation of Human Bone Marrow Mesenchymal Stem Cells by Runx2-Osterix-BSP Signaling. PMID: 26413977
  4. Two significant SNPs within IBSP, rs1054627 and rs17013181, were associated with BMD and postmenopausal osteoporosis by the two-stage strategy, and rs17013181 was also significantly associated with serum IBSP levels. PMID: 26568273
  5. Our results suggest that SSEA-4 is a specific cell surface antigen that can be used to identify dental pulp stem cells. PMID: 22266579
  6. the strong correlation between bone sialoprotein and OPN and papillary thyroid carcinoma suggests a role for BSP and OPN in calcification and tumor progression of papillary thyroid carcinoma PMID: 25973097
  7. oxidized low-density lipoprotein-induced expression dependent on Runx2 expression PMID: 25504218
  8. Bone sialoprotein could be a key mediator of the hypertrophic chondrocytes-induced angiogenesis of osteoarthritis. PMID: 24530278
  9. Current evidence demonstrates that BSP and OPN, play significant roles in bone metastasis of osteotropic malignancies derived from breast, prostate, lung, thyroid, and multiple myeloma. [review] PMID: 24071501
  10. High expression of bone sialoprotein in breast neoplasms was associated with cytokeratin-positive cells in bone marrow, but not with lymph node metastasis. PMID: 23726130
  11. results indicate that FGF2 increases BSP transcription by targeting the FRE and AP1 elements in the proximal promoter of the human BSP gene. PMID: 23485603
  12. BSP silencing decreased the integrin alphavbeta3 and beta3 levels, in turn inhibiting cell migration and invasion and decreasing the ability of the cells to metastasize to bone. PMID: 23667544
  13. IBSP mRNA is over expressed in carotid atheroma plaque (3.74 fold, p = 1.41E-09) in an intraindividual comparison. PMID: 23314561
  14. High BSP expression occurs in a significant subset of high-grade glioma patients and predicts a poorer outcome PMID: 23119009
  15. HTRA1 has a central role in osteogenesis through modification of proteins within the extracellular matrix, in particular, ibsp. PMID: 22865667
  16. human primary cementoblasts subjected to compression and IL-1beta stimulation impeded BSP and CEMP-1 expression, proteins that are associated with cementogenesis. PMID: 22349547
  17. OPN plasma levels are associated with the genetic polymorphisms in integrin-binding sialoprotein gene locus (IBSP) PMID: 20967421
  18. BSP protein expression in the primary resected non-small-cell lung cancer is strongly associated with bone metastasis and could be used to identify high-risk patients. PMID: 19376608
  19. RT-PCR analysis of human bone marrow stromal cells during osteogenesis in vitro: the mRNA levels of bone morphogenetic protein-2 (BMP-2), bone sialoprotein-II (BSP), osteopontin (OP) and cbfa-1 increased with culture time in osteogenic medium. PMID: 11968014
  20. has RGD sequence, affinity to collagen, and induces mineral crystal formation PMID: 11979972
  21. Osteoblast-related transcription factors Runx2 (Cbfa1/AML3) and MSX2 mediate the expression of bone sialoprotein in human metastatic breast cancer cells. PMID: 12750290
  22. BSP is expressed in breast and prostate cancer and has a role as a stimulator of bone mineralisation PMID: 14524533
  23. The time course of the expression of BSP wss visualized after dental implnt implatation in mandibular bone fibroblasts. PMID: 15795688
  24. Data show that RUNX2 is a direct regulator of bone sialoprotein in osteoblasts and that it functions in cooperation with DLX5 or a related factor to activate osteoblast-specific gene expression. PMID: 16000302
  25. Bone sialoprotein is involved in migration of bone marrow stromal cells through Matrigel and collagen barriers. PMID: 16995818
  26. bone sialoprotein expression in the primary resected NSCLC is strongly associated with BM progression and could be useful in identifying high-risk patients who could benefit from novel modalities of surveillance and preventive treatment PMID: 17050866
  27. May be a prognostic marker for bone metastasis in breast cancer. PMID: 17213971
  28. Runx2 and HDAC3 repress BSP gene expression and that this repression is suspended upon osteoblastic cell differentiation. PMID: 17956871
  29. has an angiogenic capacity; important in the differentiation of osteoblasts, bone matrix mineralization and tumor metastasis [review] PMID: 18302613
  30. PTH stimulates human BSP gene transcription by targeting the two cAMP response elements in the promoter of the human BSP gene. PMID: 19127545
  31. Studies do not support a role for BSP in promoting metastasis through interactions with pro-MMP-2. PMID: 19386107
  32. cooperative mechanisms by which BSP can enhance specific factors associated with a metastatic phenotype in tumor cell lines, an effect that is increased by circulating TGF-beta1 and EGF. PMID: 19492334
  33. Eight threonines modified by O-glycans were identified, leaving the C terminus of the protein free of glycans. The recombinant protein showed similar secondary structures as bone-derived BSP PMID: 11459848

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Subcellular Location Secreted.
Database Links

HGNC: 5341

OMIM: 147563

KEGG: hsa:3381

STRING: 9606.ENSP00000226284

UniGene: Hs.518726

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