Recombinant Human IL-10 Protein, >95% (SDS-PAGE), high purity

Features and benefits
  • Expression System: E.coli
  • Accession #: P22301
  • Protein Tag: No tag
  • Bioactivity: 1. Measured in a cell proliferation assay using MC/9-2 mouse mast cells. The ED₅₀ for this effect is typically 1.0 - 8.0 ng/mL. 2. Immobilized Recombinant Human IL-10 Protein (rp147355) at 2 μg/mL can bind Recombinant Rhesus IL10RA Protein (Fc Tag) the E
  • Endotoxin Concentration: <1.0 EU/μg
Item Number
rp147355
Grouped product items
SKUSizeAvailabilityPrice Qty
rp147355-10μg
10μg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$569.90
rp147355-50μg
50μg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$2,089.90
rp147355-100μg
100μg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$3,349.90
rp147355-1mg
1mg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$16,499.90

Animal Free, >95% (SDS-PAGE), Active, E.coli, No tag, 19-178 aa

Basic Description

Product NameRecombinant Human IL-10 Protein, >95% (SDS-PAGE), high purity
SynonymsCSIF | CSIFMGC126450 | Cytokine synthesis inhibitory factor | GVHDS | IL10 | IL-10 | IL10A | IL-10MGC126451 | interleukin 10 | interleukin-10 | TGIF | CSIF | Cytokine synthesis inhibitory factor | IL-10
GradeActiBioPure™, Animal Free, Azide Free, Bioactive, Carrier Free, High Performance
Product Description

Purity
>95% (SDS-PAGE)
Endotoxin level
<1.0 EU/μg
Function
Inhibits the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF produced by activated macrophages and by helper T-cells.

Specifications & PurityActiBioPure™, Bioactive, Animal Free, Carrier Free, Azide Free, High performance, ≥95%(SDS-PAGE)
Purity>95% (SDS-PAGE)
Bioactivity1. Measured in a cell proliferation assay using MC/9-2 mouse mast cells. The ED₅₀ for this effect is typically 1.0 - 8.0 ng/mL. 2. Immobilized Recombinant Human IL-10 Protein (rp147355) at 2 μg/mL can bind Recombinant Rhesus IL10RA Protein (Fc Tag) the E
Endotoxin Concentration<1.0 EU/μg
Expression SystemE.coli
SpeciesHuman
Amino Acids19-178 aa
SequenceSPGQGTQSENSCTHFPGNLPNMLRDLRDAFSRVKTFFQMKDQLDNLLLKESLLEDFKGYLGCQALSEMIQFYLEEVMPQAENQDPDIKAHVNSLGENLKTLRLRLRRCHRFLPCENKSKAVEQVKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTMKIRN
Protein TagNo tag
Accession #P22301
Predicted molecular weight18.6 KDa
SDS-PAGE15.9 kDa, under reducing conditions; 14.7 kDa, under non-reducing conditions.

Images

Recombinant Human IL-10 Protein (rp147355) - Protein Bioactivity
Measured in a cell proliferation assay using MC/9-2 mouse mast cells. The ED₅₀ for this effect is typically 1.0 - 8.0 ng/mL.


Recombinant Human IL-10 Protein (rp147355) - Protein Bioactivity
Immobilized Recombinant Human IL-10 Protein (rp147355) at 2 μg/mL can bind Recombinant Rhesus IL10RA Protein (Fc Tag) the EC₅₀ for this effect is 100.0 - 300.0 ng/mL.

Recombinant Human IL-10 Protein (rp147355) - SDS-PAGE
3 μg/lane of Recombinant Human IL-10 Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing the band at 15.9 kDa under reducing conditions and 14.7 kDa under non-reducing conditions.

Product Specifications

FormLyophilized
ReconstitutionIt is recommended that sterile water be added to the vial to prepare a stock solution of 0.25mg/mL.
Storage TempStore at -20°C,Avoid repeated freezing and thawing
Shipped InIce chest + Ice pads
Stability And StorageSamples are stable for twelve months from date of receipt at -20℃ to -80℃. Upon delivery aliquot. Avoid freeze/thaw cycle.

Certificates

Certificate of Analysis(COA)

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3 results found

Lot NumberCertificate TypeDateItem
ZJ24F0404858Certificate of AnalysisApr 26, 2024 rp147355
ZJ24F0404857Certificate of AnalysisApr 26, 2024 rp147355
ZJ24F0404856Certificate of AnalysisApr 26, 2024 rp147355

Related Documents

References

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2. de Waal Malefyt, R R, Abrams, J J, Bennett, B B, Figdor, C G CG and de Vries, J E JE..  (1991)  Interleukin 10(IL-10) inhibits cytokine synthesis by human monocytes: an autoregulatory role of IL-10 produced by monocytes..  The Journal of experimental medicine,    (1):   [PMID:1940799]
3. Walter, M R MR and Nagabhushan, T L TL..  (1995)  Crystal structure of interleukin 10 reveals an interferon gamma-like fold..  Biochemistry,    (26):   [PMID:7547951]
4. Windsor, W T WT and 9 more authors..  (1993)  Disulfide bond assignments and secondary structure analysis of human and murine interleukin 10..  Biochemistry,    (31):   [PMID:8364028]
5. Zdanov, A A and 5 more authors..  (1995)  Crystal structure of interleukin-10 reveals the functional dimer with an unexpected topological similarity to interferon gamma..  Structure (London, England : 1993),    (15):   [PMID:8590020]
6. Zdanov, A A, Schalk-Hihi, C C and Wlodawer, A A..  (1996)  Crystal structure of human interleukin-10 at 1.6 A resolution and a model of a complex with its soluble receptor..  Protein science : a publication of the Protein Society,      [PMID:8897595]
7. Gesser, B B and 8 more authors..  (1997)  Identification of functional domains on human interleukin 10..  Proceedings of the National Academy of Sciences of the United States of America,    (23):   [PMID:9405662]
8. Josephson, K K, Logsdon, N J NJ and Walter, M R MR..  (2001)  Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor binding site..  Immunity,      [PMID:11485736]
9. van der Linde, K K and 6 more authors..  (2003)  A Gly15Arg mutation in the interleukin-10 gene reduces secretion of interleukin-10 in Crohn disease..  Scandinavian journal of gastroenterology,      [PMID:12825869]
10. Lin, Ming-Tseh MT and 6 more authors..  (2003)  Relation of an interleukin-10 promoter polymorphism to graft-versus-host disease and survival after hematopoietic-cell transplantation..  The New England journal of medicine,    (4):   [PMID:14657427]
11. Zhang, Zemin Z and Henzel, William J WJ..  (2004)  Signal peptide prediction based on analysis of experimentally verified cleavage sites..  Protein science : a publication of the Protein Society,      [PMID:15340161]
12. Yoon, Sung Il SI, Jones, Brandi C BC, Logsdon, Naomi J NJ and Walter, Mark R MR..  (2005)  Same structure, different function crystal structure of the Epstein-Barr virus IL-10 bound to the soluble IL-10R1 chain..  Structure (London, England : 1993),      [PMID:15837194]
13. Yoon, Sung Il SI, Logsdon, Naomi J NJ, Sheikh, Faruk F, Donnelly, Raymond P RP and Walter, Mark R MR..  (2006)  Conformational changes mediate interleukin-10 receptor 2 (IL-10R2) binding to IL-10 and assembly of the signaling complex..  The Journal of biological chemistry,    (17):   [PMID:16982608]
14. El Kasmi, Karim C KC and 9 more authors..  (2007)  Cutting edge: A transcriptional repressor and corepressor induced by the STAT3-regulated anti-inflammatory signaling pathway..  Journal of immunology (Baltimore, Md. : 1950),    (1):   [PMID:18025162]
15. Sundberg, Thomas B TB and 16 more authors..  (2016)  Development of Chemical Probes for Investigation of Salt-Inducible Kinase Function in Vivo..  ACS chemical biology,    (19):   [PMID:27224444]

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