Recombinant Human Tumor Necrosis Factor Receptor Superfamily Member 11A Protein (TNFRSF11A), Active

Name: Recombinant Human Tumor Necrosis Factor Receptor Superfamily Member 11A Protein (TNFRSF11A), Active
Brand: Beta LifeScience
SKU: BLC-06041P
Price: 744.8 USD
Availability: InStock

Collections: Cytokines, Cytokines and growth factors, Growth factors and receptors, Recombinant proteins, Tumor necrosis factors and receptors (tnfs)

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Product Overview

Description	Recombinant Human Tumor Necrosis Factor Receptor Superfamily Member 11A Protein (TNFRSF11A), Active is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 98% as determined by SDS-PAGE and HPLC.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	Fully biologically active when compared to standard. The ED50 as determined by its ability to inhibit sRANK Ligand induced nuclear factor kappa B(NFkappaB) in RAW 264.7 cells is less than 50 ng/ml, corresponding to a specific activity of >2.0x10 4 IU/mg in the presence of 15 ng/ml of recombinant sRANK Ligand.
Uniprotkb	Q9Y6Q6
Target Symbol	TNFRSF11A
Synonyms	CD 265; CD265; FEO; LOH18CR1; Loss of heterozygosity 18 chromosomal region 1; mRANK; ODFR; OFE; OPTB7; Osteoclast differentiation factor receptor; OSTS; Paget disease of bone 2; PDB 2; PDB2; RANK; Receptor activator of NF KB; Receptor activator of NF-KB; receptor activator of nuclear factor kappa B; TNF receptor superfamily member 11a; TNFRSF11A; TNR11_HUMAN; TRANCER; Tumor necrosis factor receptor superfamily member 11a NFKB activator; Tumor necrosis factor receptor superfamily member 11a activator of NFKB; Tumor necrosis factor receptor superfamily member 11A
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	Tag-Free
Complete Sequence	QIAPPCTSEK HYEHLGRCCN KCEPGKYMSS KCTTTSDSVC LPCGPDEYLD SWNEEDKCLL HKVCDTGKAL VAVVAGNSTT PRRCACTAGY HWSQDCECCR RNTECAPGLG AQHPLQLNKD TVCKPCLAGY FSDAFSSTDK CRPWTNCTFL GKRVEHHGTE KSDAVCSSSL PARK
Expression Range	29-202aa
Protein Length	Partial
Mol. Weight	19.1 kDa
Research Area	Cancer
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 µm filtered 20 mM Tris-HCl, pH 8.0, 150mM NaCl
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Receptor for TNFSF11/RANKL/TRANCE/OPGL; essential for RANKL-mediated osteoclastogenesis. Involved in the regulation of interactions between T-cells and dendritic cells.
Subcellular Location	[Isoform 1]: Cell membrane; Single-pass type I membrane protein.; [Isoform RANK-e5a]: Cell membrane; Single-pass type I membrane protein.
Database References	HGNC: 11908 OMIM: 174810 KEGG: hsa:8792 STRING: 9606.ENSP00000465500 UniGene: Hs.204044
Associated Diseases	Familial expansile osteolysis (FEO); Paget disease of bone 2, early-onset (PDB2); Osteopetrosis, autosomal recessive 7 (OPTB7)
Tissue Specificity	Ubiquitous expression with high levels in skeletal muscle, thymus, liver, colon, small intestine and adrenal gland.

Gene Functions References

Reduced miR-144-3p expression in serum and bone mediates osteoporosis pathogenesis by targeting RANK. PMID: 29334613
findings indicate that C/EBPalpha is a stronger inducer of osteoclast differentiation than c-Fos, partly via C/EBPalpha regulation by the RANK (535)IVVY(538) motif PMID: 29122885
gammadelta T cells suppressed iDCs osteoclastogenesis by downregulation of the RANK/cFos/ATP6V0D2 signaling pathway. PMID: 30066839
RANK protein expression increased from normal to malignant endometrium, and the expression level was related with tumor grade but not with stage or the age of subjects in endometrial cancer. PMID: 29932437
study identified the second disease gene for DOS. TNFRSF11A isoforms may have the different roles in skeletal development and metabolism PMID: 29568001
The mRNA expression of RANK was highest in prostate tumour tissue from patients with bone metastases as compared to BPH or locally confined tumours, also shown in clinical subgroups distinguished by Gleason Score or PSA level. PMID: 29204705
RANK 575C>T polymorphisms did not show any statistically significant differences between the study groups (Osteoporosis and Osteopenia) and Postmenopausal women. PMID: 27304650
For the RANK gene, the AGTGC haplotype was associated with the lowest risk of presenting chronic joint pain in individuals without TMD (P=0.03). This study supports the hypothesis that changes in the OPG and RANK genes influence the presence of chronic joint pain in individuals with and without TMD. PMID: 28464982
In this study, whole exome sequencing (WES) was successfully used in six patients with malignant infantile osteopetrosis (MIOP) and identified mutations in four MIOP-related genes (CLCN7, TCIRG1, SNX10, and TNFRSF11A). PMID: 27187610
RANK is increased in hormone receptor negative and basal breast cancer, and correlates with worse recurrence-free survival and risk of bone metastasis. PMID: 28577080
RANK SNP rs34945627 has a high allelic frequency in patients with breast cancer and Bone metastases, and is associated with decreased disease-free survival and Overall Survival. PMID: 27191503
RANK rewires energy homeostasis in human lung cancer cells and promotes expansion of lung cancer stem-like cells. PMID: 29118048
EGFR and RANK combinatorial in vitro analyses revealed a significant upregulation of AKT and ERK signaling after EGF stimulation in cell lines and also an increase of breast cancer cell invasiveness. PMID: 29025596
In histologically normal tissue of BRCA1-mutation carriers and showed that RANK(+) cells are highly proliferative, have grossly aberrant DNA repair and bear a molecular signature similar to that of basal-like breast cancer. PMID: 27322743
Vav3 is a novel TRAF6 interaction partner that functions in the activation of cooperative signaling between T6BSs and the IVVY motif in the RANK signaling complex. PMID: 27507811
RANK and CCR6 expressed on monocytes may be novel targets for the regulation of bone resorption in rheumatoid arthritis and osteoporosis. PMID: 27822475
High RANK expression is associated with endometrial metastasis. PMID: 26734994
Study showed that endogenous RANK expression changes might influence prostate cancer cell behavior since reduced RANK expression resulted in significantly increased PC-3 cell proliferation and adhesion. PMID: 26977008
genetic variation associated with hypertension in Chinese women PMID: 25810067
we could not identify any association between external apical root resorption and two SNPs, rs1805034 from TNFRSF11A (encoding RANK) and rs3102735 from TNFRSF11B (encoding OPG). PMID: 24118270
Results suggest that Cbl-b improves the prognosis of RANK-expressing breast cancer patients by inhibiting RANKL-induced breast cancer cell migration and metastasis. PMID: 26087197
Based on our findings, the functional SNP RANK rs1805034 T>C may be an indicator for individual susceptibility to GCA. PMID: 26451891
Functional polymorphisms RANK rs1805034 T>C may be an indicator for individual susceptibility to esophageal squamous cell carcinoma. PMID: 25019155
These findings indicate that epidermal leukocytes gradually acquire RANK during gestation - a phenomenon previously observed also for other markers on LCs in prenatal human skin. PMID: 25722033
this study is the first to identify RANK overexpression as a novel esophageal cancer marker in both Kazakh and Han ethnic esophageal squamous cell carcinoma patients. PMID: 25973136
RANK/OPG ratio of expression in primary ccRCC is associated with BM. PMID: 26528707
Three single nucleotide polymorphisms of TNFRSF11A (rs4500848, rs6567270 and rs1805034) are associated with Age at menarche and Age at natural menopause in Chinese women. PMID: 25884698
Microcomputed tomography analysis demonstrated that the mice treated with rhRANK exhibited an increased bone volume and structure model index, and decreased trabecular spacing compared with those treated with rhOPG-Fc. PMID: 25738879
results indicate that the RANK IVVY motif cooperates with the TRAF-binding motifs to promote osteoclastogenesis, which provides novel insights into the molecular mechanism of RANK signaling in osteoclastogenesis. PMID: 26276390
Response to sRANKL in normal and tumor cells suggests a role for RANK/ERK-mediated signaling in normal osteoblasts chemotactic migration during bone remodeling that is altered or lost during osteosarcoma tumorigenesis. PMID: 25893522
Higher RANK expression in the primary breast tumor is associated with a higher sensitivity to chemotherapy, but also a higher risk of relapse and death. PMID: 24737168
Changes in bone markers, OPG, sRANKL and/or the OPG/sRANKL ratio exhibited by girls with Anorexia nervosa have been found to be associated with changes in the levels of the selected adipose tissue hormones. PMID: 24549600
Genetic polymorphism in TNFRSF11A influences bone mineral density in post-menopausal women. PMID: 25138264
Single nucleotide polymorphisms of RANK and PTGS1 show genetic associations with osteoproliferative changes in ankylosing spondylitis. PMID: 24651623
he top hit rs17069906 (p = 5.6 e-10) is located within the genomic region of RANK, recently demonstrated to be an important player in the adaptive recovery response in podocytes and suggested as a promising therapeutic target in glomerular diseases. PMID: 25478860
This review study has focused on the association of RANKL-RANK-OPG pathway in the pathogenesis and progression of giant cell tumor of bone as well as discussed the possible therapeutic strategies by targeting this pathway PMID: 25618600
The urinary mRNA of RANK might be used to differentiate histologic subtypes of glomerulonephritis, particularly between minimal change disease and membranous nephropathy. PMID: 25171769
RANKL and IL-6 mediate direct paracrine-autocrine signaling between cells of the osteoblast lineage and cancer cells. PMID: 24676805
PGRN and PIRO form a new regulatory axis in osteoclastogenesis that is included in RANK signaling in cell fusion and OC resorption of osteoclastogenesis PMID: 25406312
we identified RANK expression as a negative prognostic factor regarding disease-free survival in osteosarcoma PMID: 24842377
High RANK protein expression is associated with breast cancer. PMID: 25111682
RANKL, either derived from the prostate tumor or from the host, plays a key role in cancer bone metastasis. PMID: 24478054
The involvement of TNFRSF11A in hereditary recurrent fever highlights the key role of this receptor in innate immunity. PMID: 24891336
Mechanistic studies showed that IL-10 downregulated RANK expression in monocytes and thus, inhibited RANKL-induced OC formation PMID: 24340030
silencing of miR-503 using a specific antagomir in ovariectomy (OVX) mice increased RANK protein expression, promoted bone resorption PMID: 23821519
The genotypes, combined genotypes and allele frequencies of C421T and C575T polymorphisms of the RANK gene have not been found to be associated with bone mineral density in Turkish women. PMID: 23553199
RANK signaling interferes with mammary cell commitment, contributing to breast carcinogenesis. PMID: 23766243
High RANK expression is associated with Avascular Necrosis of Femur Head. PMID: 24200492
The atrial expression of RANK (and RANKL/osteoprotegerin ratio) was higher in normal controls compared to persistent atrial fibrillation patients. PMID: 22178057
One mechanism of RANK inhibition by 1,25(OH)2D3 is down-regulation of the M-CSF receptor c-Fms, which is required for the expression of RANK. PMID: 23116709

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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