Active Recombinant Rat Tnfsf11 protein, His-tagged

• Cat.No.: Tnfsf11-196R
• Product Overview: Recombinant Rat Tnfsf11(Arg72-Asp318) fused with His tag at N-terminal was expressed in CHO.

Specification

• Description: RANK L (receptor activator of NF-kappa B ligand), also called TRANCE (TNF-related activation-induced cytokines), OPGL (osteoprotegerin ligand), or ODF (osteoclast differentiation factor), is a 39-45 kDa type II transmembrane (TM) protein in the tumor necrosis factor family, designated TNFSF11. RANK L, produced by osteoblasts and bone marrow stromal cells, is required for differentiation of osteoclasts and stimulates bone resorption. It is also produced by activated T cells and augments dendritic cell stimulation; RANK L-/- mice lack lymph nodes and have impaired thymocyte development. The rat RANK Ligand cDNA encodes a type II transmembrane protein of 318 amino acids with a predicted cytoplasmic domain of 47 amino acids, a 21 amino acids transmembrane region, and an extracellular domain of 250 amino acids. The extracellular domain contains two potential N-linked glycosylation sites. Rat and human RANK Ligand and rat and mouse RANK Ligand share 83% and 95% amino acid identity respectively. RANK L can stimulate human osteoclast differentiation (4). Like most TNF family members, RANK L can form trimers. Soluble 31, 25 and 24 kDa forms of RANK L can be created by usage of alternate start sites at aa 74 or 146, or proteolytic cleavage by osteoblast- or stromal cell-derived ADAM10 (after aa 139) or MMP14 (aa 146), or bone metastatic prostate tumor-derived MT1-MMP (aa 146). Both TM and soluble extracellular RANK L act by engaging RANK receptors and are antagonized by the decoy receptor, OPG (osteoprotegrin). In resting cells, the majority of RANK L is stored in secretory lysosomes. In mammary epithelia, RANK L is up-regulated by pregnancy hormones and is essential for the formation of a lactating mammary gland. In the brain, astrocyte RANK L mediates body temperature regulation. Pathologically, RANK L is thought to mediate post-menopausal osteoporosis, vascular calcification, progestin-induced breast cancer, cancer-induced bone disease, and osteopetrosis (in RANK L deficiencies).
• Source: CHO
• Species: Rat
• Tag: His
• Predicted N Terminal: His
• Form: Lyophilized from a 0.2 μm filtered solution in NaH2PO4, NaCl and EDTA.
• Bio-activity: Measured by its ability to induce osteoclast differentiation of RAW 264.7 mouse monocyte/macrophage cells. The ED50 for this effect is 2.5-15 ng/mL.
• Molecular Mass: Predicted Molecular Mass: 29 kDa
  SDS-PAGE: 33-38 kDa, reducing conditions
• Endotoxin: <0.1 EU per 1 μg of the protein by the LAL method.
• Purity: >85%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  12 months from date of receipt, -20 to -70 centigrade as supplied.
  1 month, 2 to 8 centigrade under sterile conditions after reconstitution.
  3 months, -20 to -70 centigrade under sterile conditions after reconstitution.
• Reconstitution: Reconstitute at 100 μg/mL in PBS.

Gene Information

• Gene Name: Tnfsf11 tumor necrosis factor (ligand) superfamily, member 11 [ Rattus norvegicus ]
• Official Symbol: Tnfsf11
• Synonyms: TNFSF11; tumor necrosis factor (ligand) superfamily, member 11; tumor necrosis factor ligand superfamily member 11; ODF; OPGL; TRANCE; osteoprotegerin ligand; osteoclast differentiation factor; TNF-related activation-induced cytokine; receptor activator of nuclear factor kappa B ligand; receptor activator of nuclear factor kappa-B ligand; RANKL
• Gene ID: 117516
• mRNA Refseq: NM_057149
• Protein Refseq: NP_476490
• UniProt ID: Q9ESE2

Reviews

10/14/2022

The reproducibility of TNFSF11 is so good that the results are highly consistent regardless of the conditions under which the experiment or application is performed, greatly reducing the experimental error.

11/24/2020

Green production process of TNFSF11 is highly commendable, which uses the most advanced biotechnology to increase production efficiency and reduce environmental impact.

07/22/2020

The short half-life and high clearance of TNFSF11 make it better able to adapt to changing treatment needs and provide patients with more flexible treatment options.

Q&As

How can the expression level of TNFSF11 protein be used for disease diagnosis and prognosis assessment?

It is possible to detect the expression level of TNFSF11 protein to help diagnose tumors and other diseases, and to assess their prognosis and treatment effectiveness.

How to use the activity of TNFSF11 protein for disease treatment?

At present, a variety of drugs have been developed to target TNFSF11 proteins and their related signaling pathways, including inhibiting their expression and inhibiting their binding to receptors, etc., for the treatment of tumors and other bone metabolism-related diseases.

What is the relationship between TNFSF11 proteins and infectious diseases?

Studies have shown that TNFSF11 proteins can be involved in the regulation of infectious diseases, such as playing a role in some viral infections.

How well are TNFSF11 proteins expressed in different tissues and organs?

There are differences in the expression of TNFSF11 proteins in different tissues and organs, and they are expressed in tissues and organs such as the immune system, bones, and teeth, and the expression level may be affected by many factors.

What is the relationship between TNFSF11 proteins and autoimmune diseases?

Studies have shown that TNFSF11 proteins can be involved in the regulation of autoimmune diseases, such as in autoimmune diseases such as rheumatoid arthritis.

What is the relationship between TNFSF11 proteins and other TNF superfamily members?

TNFSF11 protein belongs to the TNF superfamily and has certain structural and functional similarities with other members of the TNF superfamily.