Recombinant mouse RANKL protein (ab51941)
Key features and details
- Expression system: Escherichia coli
- Purity: >= 98% SDS-PAGE
- Active: Yes
- Suitable for: SDS-PAGE, Functional Studies
Description
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Product name
Recombinant mouse RANKL protein
See all RANKL proteins and peptides -
Biological activity
Measured by its ability to induce osteoclast formation in RAW264.7 cells using a concentration of 5-10 ng/ml.
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Purity
>= 98 % SDS-PAGE.
>98% by SDS-PAGE and HPLC analyses. -
Expression system
Escherichia coli -
Accession
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Protein length
Protein fragment -
Animal free
No -
Nature
Recombinant -
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Species
Mouse -
Sequence
PAMMEGSWLD VAQRGKPEAQ PFAHLTINAA SIPSGSHKVT LSSWYHDRGW AKISNMTLSN GKLRVNQDGF YYLYANICFR HHETSGSVPT DYLQLMVYVV KTSIKIPSSH NLMKGGSTKN WSGNSEFHFY SINVGGFFKL RAGEEISIQV SNPSLLDPDQ DATYFGAFKV QDID -
Predicted molecular weight
19 kDa -
Actual molecular weight
19 kDa -
Additional sequence information
Soluble Receptor Activator of NFkB Ligand
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab51941 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
SDS-PAGE
Functional Studies
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Form
Lyophilized -
Additional notes
This product is manufactured by BioVision, an Abcam company and was previously called 4557 sRANK Ligand, murine recombinant. 4557-10 is the same size as the 10 µg size of ab51941.
The reconstituted solution can be diluted into aqueous buffers and stored at 4°C for 1 week or –20°C for future use.
Endotoxin level is <0.1 ng/µg of sRANK Ligand
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Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Constituents: 0.0605% Tris, 0.435% Sodium chloride
This product is an active protein and may elicit a biological response in vivo, handle with caution.
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ReconstitutionReconstitute in sterile distilled water to a concentration of 0.1-1.0 mg /ml.
General Info
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Alternative names
- CD254
- hRANKL2
- ODF
see all -
Function
Cytokine that binds to TNFRSF11B/OPG and to TNFRSF11A/RANK. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive T-cell proliferation. May be an important regulator of interactions between T-cells and dendritic cells and may play a role in the regulation of the T-cell-dependent immune response. May also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy. -
Tissue specificity
Highest in the peripheral lymph nodes, weak in spleen, peripheral blood Leukocytes, bone marrow, heart, placenta, skeletal muscle, stomach and thyroid. -
Involvement in disease
Defects in TNFSF11 are the cause of osteopetrosis autosomal recessive type 2 (OPTB2) [MIM:259710]; also known as osteoclast-poor osteopetrosis. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. The disorder occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Autosomal recessive osteopetrosis is usually associated with normal or elevated amount of non-functional osteoclasts. OPTB2 is characterized by paucity of osteoclasts, suggesting a molecular defect in osteoclast development. -
Sequence similarities
Belongs to the tumor necrosis factor family. -
Post-translational
modificationsThe soluble form of isoform 1 derives from the membrane form by proteolytic processing (By similarity). The cleavage may be catalyzed by ADAM17. -
Cellular localization
Cytoplasm; Secreted and Cell membrane. - Information by UniProt
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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SDS download
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Datasheet download
References (0)
ab51941 has not yet been referenced specifically in any publications.