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Merck

O1139

Sigma-Aldrich

Anti-Osteoprotegerin antibody produced in goat

affinity isolated antibody, lyophilized powder

Sinónimos:

Anti-OPG

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About This Item

MDL number:
UNSPSC Code:
51111800
NACRES:
NA.41

biological source

goat

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

lyophilized powder

species reactivity

mouse

technique(s)

immunohistochemistry: 5-15 μg/mL
neutralization: suitable
western blot: 0.1-0.2 μg/mL

UniProt accession no.

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

General description

Osteoprotegerin (OPG) secreted by osteoblasts and osteogenis stromal stem cells belongs to the TNF receptor superfamily. OPG is expressed in bone marrow, osteoblasts, heart, lung, kidney, thymus, B lymphocytes, chondrocytes and smooth muscle cells. The ratio of OPG and receptor activator of NF-κB Ligand (RANKL) is crucial determining the bone mass. Receptor activator of NF-κB (RANK)/RANKL/OPG axis decides the bone biology. OPG binds RANKL and prevents the activation of osteoclasts, the cells that deplete bone mass. Excess levels of OPG lead to osteopetrosis while deficiency results in osteoporosis. The RANK/RANKL/OPG pathway mediates the activation of multiple pathways such as NF-κB, Akt, JNK, and MAPK
Anti-osteoprotegerin specifically reacts with recombinant mouse OPG. The antibody may cross react with human OPG (25% homology).

Specificity

The antibody has the ability to neutralize the biological activity of recombinant mouse OPG.

Immunogen

purified recombinant mouse osteoprotegerin expressed in mouse NSO cells.

Application

Anti-osteoprotegerin antibody may be used to neutralize mouse OPG at neutralization dose (ND50) of 0.5-2 μg/ml. The antibody is suitable for immunoblotting at a working concentration of 0.1-0.2 μg/ml.

Physical form

Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline containing carbohydrates.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Brendan F Boyce et al.
Current osteoporosis reports, 5(3), 98-104 (2007-10-11)
Understanding of osteoclast formation and activation has advanced considerably since the discovery of the RANKL/RANK/OPG system in the mid 1990s. Osteoblasts and stromal stem cells express receptor activator of NF-jB ligand (RANKL), which binds to its receptor, RANK, on the
Shabber Syed et al.
Journal of cardiovascular development and disease, 9(8) (2022-08-26)
Calcific aortic valve disease (CAVD) is a common cardiac defect, particularly in the aging population. While several risk factors, such as bi-leaflet valve structure and old age, have been identified in CAVD pathogenesis, molecular mechanisms resulting in this condition are
I Silva et al.
Acta reumatologica portuguesa, 36(3), 209-218 (2011-11-25)
The discovery of the receptor activator of nuclear factor-kB (RANK)/RANK Ligand (RANKL)/osteoprotegerin (OPG) pathway contributed to the understanding of how bone formation and resorption were processed and regulated. RANKL and OPG are members of the tumor necrosis factor (TNF) and
Anne-Priscille Trouvin et al.
Clinical interventions in aging, 5, 345-354 (2011-01-14)
Bone remodeling requires a precise balance between resorption and formation. It is a complex process that involves numerous factors: hormones, growth factors, vitamins, and cytokines, and notably osteoprotegerin (OPG) and receptor activator for nuclear factor-κB (RANK) ligand. The signaling pathway
Yang Liu et al.
Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology, 45(5), 1759-1771 (2018-03-02)
Bone morphogenetic proteins (BMPs) and BMP receptors widely participate in osteolytic metastasis of breast cancer, while their role in tumor-stromal interaction is largely unknown. In this study, we investigated whether BMP receptor type 1a (BMPR1a) can alter the interaction between

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