Recombinant Human Oncostatin-M-Specific Receptor Subunit Beta (OSMR) Protein (His&Myc)

Name: Recombinant Human Oncostatin-M-Specific Receptor Subunit Beta (OSMR) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-01917P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Cytokines, Cytokines and growth factors, Growth factors and receptors, Recombinant proteins

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Product Overview

Description	Recombinant Human Oncostatin-M-Specific Receptor Subunit Beta (OSMR) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q99650
Target Symbol	OSMR
Synonyms	Interleukin-31 receptor subunit beta
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	KSQWIKETCYPDIPDPYKSSILSLIKFKENPHLIIMNVSDCIPDAIEVVSKPEGTKIQFLGTRKSLTETELTKPNYLYLLPTEKNHSGPGPCICFENLTYNQAASDSGSCGHVPVSPKAPSMLGLMTSPENVLKALEKNYMNSLGEIPAGETSLNYVSQLASPMFGDKDSLPTNPVEAPHCSEYKMQMAVSLRLALPPPTENSSLSSITLLDPGEHYC
Expression Range	762-979aa
Protein Length	partial
Mol. Weight	31.3 kDa
Research Area	Immunology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
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	Associates with IL31RA to form the IL31 receptor. Binds IL31 to activate STAT3 and possibly STAT1 and STAT5. Capable of transducing OSM-specific signaling events.
Subcellular Location	Membrane; Single-pass type I membrane protein.
Protein Families	Type I cytokine receptor family, Type 2 subfamily
Database References	HGNC: 8507 OMIM: 105250 KEGG: hsa:9180 STRING: 9606.ENSP00000274276 UniGene: Hs.120658
Associated Diseases	Amyloidosis, primary localized cutaneous, 1 (PLCA1)
Tissue Specificity	Expressed in keratinocytes (at protein level). Expressed at relatively high levels in all neural cells as well as fibroblast and epithelial cells.

Gene Functions References

Polymorphisms of the OSMR rs2292016 locus are related to the development and outcome of DCM. PMID: 29652994
Missense mutatios were found in exon 10 of the oncostatin-M specific receptor beta subunit (OSMR) gene in all of the six patients from family 1, and in exon 14 of the OSMR gene in all of the four patients from family 2. PMID: 29419851
The PLAC1 expression has been demonstrated for the first time in cervical cancers. This preliminary study has further revealed a complex relationship between PLAC1 expression, cervical cancer histologic type, p53, and HPV type that requires further investigation. PMID: 28375929
OSMR-beta deficiency in macrophages improved high-fat diet-induced atherogenesis and plaque vulnerability PMID: 28258089
OSM and OSMR are highly expressed in inflammatory bowel disease intestinal mucosa compared to control mucosa. Intestinal stromal cells express abundant OSMR. PMID: 28368383
OSM:OSMR interactions are able to induce EMT, increased cancer stem cell-like properties and enhanced lung colonisation in SCC cells PMID: 27351213
the RET p.S891A mutation combined with OSMR p.G513D may underlie a novel phenotype manifesting as familial medullary thyroid carcinoma and cutaneous amyloidosis PMID: 26356818
this study offers new findings on the molecular genetics and disease relevance of mutations in OSMR in Familial primary localized cutaneous amyloidosis. PMID: 25792357
Oncostatin M and interleukin-31: Cytokines, receptors, signal transduction and physiology. PMID: 26198770
OSMRBeta in neurons is critical for neuronal survival during cerebral ischemic/reperfusion. PMID: 26311783
primary localized cutaneous amyloidosis has a missense mutation in oncostatin M receptor beta PMID: 25054142
The interleukin IL-31/IL-31receptor axis contributes to tumor growth in human follicular lymphoma. PMID: 25283844
oncostatin M is a cytokine possessing vigorous antiviral and immunostimulatory properties which is released by APC upon interaction with CD40L present on activated CD4+ T cells. PMID: 24418171
The disease severity of rheumatoid arthritis and systemic lupus erythematosus can be partially affected by the OSMR promoter polymorphisms. PMID: 24219225
We conclude that an OSMR/TGM2/integrin-alpha5beta1/fibronectin pathway is of biological significance in cervical squamous cell carcinoma PMID: 23765377
A unique loop structure in oncostatin M determines binding affinity toward oncostatin M receptor and leukemia inhibitory factor receptor. PMID: 22829597
enhanced production by beta-defensin-2 in T cells PMID: 22137028
This study identified a new heterozygous OSMR missense mutation in primary localized cutaneous amyloidosis. PMID: 22062952
An alternatively spliced variant of OSMR transcribing a soluble form of this receptor has been characterized in esophageal squamous cell carcinoma. PMID: 21394648
We conclude that OSMR overexpression in cervical SCC cells provides increased sensitivity to OSM, which induces pro-malignant changes. PMID: 21952923
Aberrant methylation of the OSMR gene is associated with non-invasive colorectal cancer. PMID: 21508378
Two new pathogenic heterozygous missense mutations in the OSMR gene (p.Val631Leu and p.Asp647Tyr) were identified in two Dutch familial primary localized cutaneous amyloidosis families. PMID: 20507362
study provides evidence for the existence of a novel pathogenic mutation in the OSMR gene in a caucasian family with familial primary cutaneous amyloidosis PMID: 19466957
The identification of OSMR and IL31RA gene pathology provides an explanation of the high prevalence of primary cutaneous amyloidosis in Taiwan as well as new insight into disease pathophysiology. PMID: 19690585
provides a biologic rationale for silencing of OSMR in colon cancer progression and highlight a new therapeutic target. Moreover, detection and quantification of OSMR promoter methylation in fecal DNA is a highly specific diagnostic biomarker for CRC PMID: 19662090
expression and evidence for STAT3 activation in human ovarian carcinomas PMID: 12061840
The expression of OSM and its receptor in ovarian tissue from fetuses and women suggests a possible role of OSM in growth initiation of human primordial follicles. PMID: 15831292
sOSMR is able to bind OSM and interleukin-31 when associated to soluble gp130 or soluble interleukin-31R, respectively, and to neutralize both cytokine properties PMID: 17028186
FPLCA has been mapped to 5p13.1-q11.2, and by candidate gene analysis, study identified missense mutations in the OSMR gene, encoding oncostatin M-specific receptor beta (OSMRbeta), in three families. PMID: 18179886
murine OSMR initiates STAT5 activation directly via the receptor bound Janus kinases. Intriguingly, the murine receptor preferentially recruits JAK2, whereas the human receptor seems to have a higher affinity for JAK1. PMID: 18430728
IL-6 and Oncostatin M individually affect the profile of leukocyte trafficking PMID: 18641356
The renal parenchyma is capable of generating a strong acute phase response, likely mediated via OSM/OSMR. PMID: 19158344
Epigenetic silencing and DNA methylation of OSMR is associated with colorectal cancers. PMID: 19223499
study reporta a Japanese family with familial primary localized cutaneous amyloidosis in whom a novel OSMR mutation was observed PMID: 19375894

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.