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Mouse TNFSF11 (RANKL) (Yeast-derived Recombinant Protein) - 25 micrograms

Catalog No.RP0437M-025

Price$300.00

AvailabilityIn Stock

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Tumor necrosis factor ligand superfamily member 11 (TNFSF11) also known as Receptor Activator of Nuclear factor Kappa-B Ligand (RANKL), TNF-related activation-induced cytokine (TRANCE), osteoprotegerin ligand (OPGL), and osteoclast differentiation factor (ODF) is a member of the tumor necrosis factor ligand (TNF) ligand family. Nineteen cytokines have been identified as part of the TNF family on the basis of sequence, functional, and structural similarities. Family members include TNF beta (TNFSF1), TNF alpha (TNFSF2), Lymphotoxin beta (TNFSF3), OX40 Ligand (TNFSF4), CD40 Ligand (TNFSF5), Fas Ligand (TNFSF6), CD27 Ligand (TNFSF7), CD30 Ligand (TNFSF8), 4-1BB Ligand (TNFSF9), TRAIL (TNFSF10), TRANCE/RANKL (TNFSF11), TWEAK (TNFSF12), APRIL(TNFSF13), BAFF (TNFSF13B), LIGHT (TNFSF14), TL1A/VEGI (TNFSF15), and GITR Ligand (TNFSF18). RANKL regulates bone remodelling and the development of the thymus, lymph nodes and mammary glands. Overproduction of RANKL is implicated in a variety of degenerative bone diseases, such as rheumatoid arthritis and psoriatic arthritis.

Alternate Names - TNFSF11, CD254, ODF, OPGL, OPTB2, RANKL, TRANCE, hRANKL2, sOdf, TNLG6B, tumor necrosis factor superfamily member 11, TNF superfamily member 11

Mouse TNFSF11 (RANKL) (Yeast-derived Recombinant Protein) - 25 micrograms

Product Information
Citations
Ordering Information

Catalog No.:

RP0437M-025

Quantity:

25 ug

Source:

The Mouse TNFSF11 recombinant protein was produced in yeast and therefore does not have endotoxin, is naturally folded, and post-translationally modified.

MW:

The Mouse TNFSF11 recombinant protein has a predicted molecular weight of 19.8 kDa.

Protein Sequence:

FSGAPAMMEG SWLDVAQRGK PEAQPFAHLT INAASIPSGS HKVTLSSWYH DRGWAKISNM TLSNGKLRVN QDGFYYLYAN ICFRHHETSG SVPTDYLQLM VYVVKTSIKI PSSHNLMKGG STKNWSGNSE FHFYSINVGG FFKLRAGEEI SIQVSNPSLL DPDQDATYFG AFKVQDID (178)

Alias:

RANKL, TRANCE, OPGL

Country of Origin:

USA

Applications:

The Mouse TNFSF11 (RANKL, TRANCE, OPGL) protein can be used in cell culture, as an TNFSF11 ELISA Standard, and as a Western Blot Control.

Epidermal growth factor receptor (EGFR) signaling is a key mediator of hormone-induced leukocyte infiltration in the pubertal female mammary gland.

Applications:

Abstract

It is well documented that macrophages and eosinophils play important roles in normal murine

pubertal mammary gland development. Although it is accepted that estrogen (E) and progesterone

(P) are key players in mammary gland development, the roles these hormones might play in

regulating the actions of leukocytes in that process is an understudied area. We show here that P

and E, respectively, induce unique, but overlapping, sets of proinflammatory and angiogenic

cytokines and chemokines, in the pubertal female BALB/c mammary gland, as well as induce

infiltration of macrophages and eosinophils to the mammary periepithelium. This extends earlier

studies showing P induction of proinflammatory products in pubertal and adult mammary epithelial

organoids and P-induced in vivo infiltration of leukocytes to the adult mammary periepithelium.

Importantly, epidermal growth factor receptor-signaling, which is likely mediated by

amphiregulin (Areg), a downstream mediator of E and P, is both necessary and sufficient for both

E- and P-induced recruitment of macrophages and eosinophils to the pubertal mammary periepithelium.We

further show that receptor activator of nuclear factor B ligand (RANKL), although not

sufficient of itself to cause macrophage and eosinophil recruitment, contributes to an optimal

response to P. The potency of Areg is highlighted by the fact that it is sufficient to induce macrophage

and eosinophil recruitment at levels equivalent to that induced by either E or P. Our

finding of a dominant role for Areg in hormonally induced leukocyte recruitment to the pubertal

mammary gland parallels its dominance in regulating ductal outgrowth and its role in P-induced

proliferation in the pubertal gland. (Endocrinology 155: 2301–2313, 2014)

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USA

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