Recombinant Mouse Tumor necrosis factor receptor superfamily member 11B (Tnfrsf11b)

Code CSB-YP023969MO
MSDS
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Source Yeast
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Code CSB-EP023969MO
MSDS
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Source E.coli
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Code CSB-EP023969MO-B
MSDS
Size Pls inquire
Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP023969MO
MSDS
Size Pls inquire
Source Baculovirus
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Code CSB-MP023969MO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Tnfrsf11b
Uniprot No.
Alternative Names
Tnfrsf11b; Ocif; Opg; Tumor necrosis factor receptor superfamily member 11B; Osteoclastogenesis inhibitory factor; Osteoprotegerin
Species
Mus musculus (Mouse)
Expression Region
22-401
Target Protein Sequence
ETLPPKYLH YDPETGHQLL CDKCAPGTYL KQHCTVRRKT LCVPCPDHSY TDSWHTSDEC VYCSPVCKEL QSVKQECNRT HNRVCECEEG RYLEIEFCLK HRSCPPGSGV VQAGTPERNT VCKKCPDGFF SGETSSKAPC IKHTNCSTFG LLLIQKGNAT HDNVCSGNRE ATQKCGIDVT LCEEAFFRFA VPTKIIPNWL SVLVDSLPGT KVNAESVERI KRRHSSQEQT FQLLKLWKHQ NRDQEMVKKI IQDIDLCESS VQRHLGHSNL TTEQLLALME SLPGKKISPE EIERTRKTCK SSEQLLKLLS LWRIKNGDQD TLKGLMYALK HLKTSHFPKT VTHSLRKTMR FLHSFTMYRL YQKLFLEMIG NQVQSVKISC L
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
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 before Lyophilization
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℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and 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
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
Acts as decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF10/TRAIL and protect against apoptosis. TNFSF10/TRAIL binding blocks the inhibition of osteoclastogenesis.
Gene References into Functions
  1. lactation increases physiological maxillary bone remodeling and orthodontic tooth movement, and both require activation of RANK/RANKL/OPG system PMID: 29382610
  2. Hdac3-depletion in osteoblasts increases expression of Opg, subsequently preserving insulin sensitivity. PMID: 28840938
  3. Epithelial rests of Malassez may be associated with root resorption via OPG, thus helping to explain the mechanism underlying root resorption. PMID: 29644561
  4. findings demonstrate that mTORC1 activation-stimulated RANKL expression in B cells is sufficient to induce bone loss and osteoporosis. The study also established a link between mTORC1 and the RANKL/OPG axis via negative regulation of beta-catenin. PMID: 26825871
  5. RANK/RANKL signaling is involved in the androgen deprivation therapy-induced acceleration of bone metastasis in castration-insensitive prostate cancer and is inhibited by osteoprotegerin to prevent bone metastasis. PMID: 28373003
  6. endocortical resorption is driven by reduced OPG rather than elevated RANKL expression PMID: 27460899
  7. Diabetes significantly increased OPG and the OPG/TRAIL ratio expression in the aorta, while dyslipidemia was the major determinant of the changes observed in the heart, where it significantly increased OPG and reduced TRAIL expression, thus increasing cardiac OPG/TRAIL ratio. PMID: 28070143
  8. These discoveries strongly suggest that Heparan Sulfate plays an active role in regulating OPG-RANKL interaction and osteoclastogenesis. PMID: 27697839
  9. OPG plays an important role in regulating bone marrow mesenchymal stem cells differentiation and bone marrow adipogenesis. PMID: 27898403
  10. These data suggested that OPG played an important role in maintaining the homeostasis of articular cartilage of femoral head. PMID: 27541035
  11. Data show that p38alpha mitogen-activated protein kinase (MAPK) in paired related homeobox 1 protein (Prx1+) bone marrow-derived mesenchymal stromal cells acts to preserve the bone by sustaining osteoprotegerin (OPG) production. PMID: 26947973
  12. OPG expression in chondrocyte increases bone mass in the proximal metaphysis of tibiae through negative regulation of osteoclast formation. PMID: 26329493
  13. the generation of Rag2GFP+ regulatory T cells is unaltered in Tnfrsf11b(-/-) mice PMID: 26254339
  14. identify osteoprotegerin as a HIF target gene capable of directing osteoblast-mediated osteoclastogenesis to regulate bone homeostasis PMID: 25846796
  15. Osteoprotegerin is increased in metabolic syndrome and promotes adipose tissue proinflammatory changes. PMID: 24998520
  16. These results indicate that OPG derived either from the bone marrow or from the vessel wall is sufficient to slow down lesion progression and vascular calcification independent of bone turnover. PMID: 23990207
  17. High concentrations of alendronate decrease the expressions of OPG and RANKL in cultured osteoblasts. PMID: 23268391
  18. In a xenograft model, increased osteoprotegerin expression correlated with a delay to pathologic fracture suggesting a potential role for mTOR inhibitors in the treatment of neuroblastoma bone metastases. PMID: 23331792
  19. Coptisine inhibits RANKL-induced NF-kappaB phosphorylation in osteoclast precursors and suppresses function through the regulation of RANKL and OPG gene expression in osteoblastic cells. PMID: 21656335
  20. OPG gene transfer to periodontal tissues could inhibit relapse after orthodontic tooth movement, through the inhibition of osteoclastogenesis PMID: 22196183
  21. Omentin-1 ameliorates arterial calcification and bone loss in vivo through the regulation of the RANK signalling pathway in osteoprotegerin-deficient mice. PMID: 21750093
  22. Increased bone resorption is a noncell autonomous defect, caused by exuberant stimulation of osteo-clastogenesis by Cx43-deficient bone marrow stromal cells, via decreased Opg production. PMID: 21346198
  23. Osteoprotegerin serum levels were decreased in all IL-6 deficient mice and in a highest degree in sham-operated hypothyroid mice. PMID: 21478097
  24. TRAIL and osteoprotegerin are expressed in atherosclerotic plaques in a calcification-prone mouse model PMID: 21426505
  25. RANKL and OPG could have a close relationship with the osteoclast activity during mandibular first molar eruption. PMID: 18788552
  26. distribution of the osteocytic lacunar-canalicular system and osteocyte-secreting molecules--dentin matrix protein 1 and sclerostin--in the epiphyses and cortical bones in osteoprotegerin deficiency PMID: 21079361
  27. overexpression in preosteoblasts promotes their differentiation into mature osteoblasts PMID: 20936961
  28. Co2+ and Cr3+ can stimulate the mRNA expressions of RANKL and osteoprotegerin in osteoblasts. PMID: 20369527
  29. mechanical stretching may play an important role in bone remodeling through the upregulation of OPG and the mechanical signaling leading to OPG induction involves the noncanonical Wnt pathway. PMID: 20200998
  30. Osteoprotegerin(OPG) ex vivo gene therapy may be useful to treat patients for aseptic loosening of prosthetic implants. PMID: 11918293
  31. expression of RANKL and osteoprotegerin mRNAs by marrow stromal cells PMID: 12211438
  32. Osteosclerosis in mice with thrombopoietin overexpression occurs predominantly via up-regulation of osteoprotegerin in host stromal cells leading to disruption of osteoclastogenesis. PMID: 12506018
  33. The presence of OPG on the membrane of these cells was confirmed by western blotting and immunostaining, sRANKL was found to be bound to the OPG on the osteoclast precursors. PMID: 12526098
  34. expression of RANKL and OPG change with age in whole bone and in cultured osteoblast-like cells PMID: 12568404
  35. Runx2 promotes osteoclast differentiation by inducing RANKL and inhibiting OPG PMID: 12697767
  36. osteoprotegerin and RANK ligand have roles in breast cancer bone metastasis PMID: 12923331
  37. bone formation is coupled with bone resorption at local sites in OPG-/- mice, and that serum RANKL levels do not reflect this coupling. PMID: 14500574
  38. OPG secretion is regulated through calmodulin-sensitive protein kinase signaling that depends on the activity of the L-type VSCC and is mediated through the cAMP response element-binding protein. PMID: 14525906
  39. suppression of gene expression affects osteoclastogenic activity of parathyroid hormone PMID: 14969393
  40. Expression in mice with collagen-induced arthritis treated with Kanzo-bushi-to, a Kampo medicine. PMID: 15340228
  41. expression of RANKL and OPG and the formation of osteoclast-like cells do not require Runx2 PMID: 15474477
  42. RANKL inhibitor osteoprotegerin is used to evaluate the role of osteoclast-mediated hypercalcemia in two murine models of hypercalcemia of malignancy. PMID: 15845617
  43. Microorganism-reactive CD4+ T-cells and the RANKL-osteoprotegerin axis provide the molecular basis of the advanced periodontal breakdown in diabetes. PMID: 15855336
  44. findings in OPG knockout mice support the hypothesis that OPG is important in the inhibition of bone remodeling within the otic capsule and the maintenance of normal auditory function PMID: 16467704
  45. Glucocorticoids regulate osteoclast differentiation and expression of receptor activator of nuclear factor-kappaB (NF-kappaB) ligand, osteoprotegerin, and receptor activator of NF-kappaB in mouse calvarial bones PMID: 16614077
  46. OPG inhibits advanced plaque progression by preventing an increase in lesion size and lesion calcification. OPG may act as a survival factor and may modulate MMP9 production in vascular cells. PMID: 16840715
  47. microgravity is capable to indirectly stimulate osteoclast formation and activity by regulating osteoblast secretion of crucial regulatory factors such as RANKL and OPG PMID: 16927271
  48. Altogether, these findings suggest that increased OPG production represents an early event in the natural history of diabetes mellitus, possibly contributing to disease-associated endothelial cell dysfunction. PMID: 17148684
  49. OPG suppresses the shedding of RANKL from osteoblasts and the serum RANKL in OPG(-/-) mice exactly reflects the state of bone resorption. PMID: 17182555
  50. bone resorptive action of Dexamethasone is mediated mainly by the inhibition of OPG by transrepressing the OPG gene through the AP-1 site PMID: 17516544

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Subcellular Location
Secreted.
Tissue Specificity
Highly expressed in liver, lung, stomach, intestines and calvaria. Highly expressed in decidua and placenta, and in embryo.
Database Links
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