IFN-α10, Agonist of Interferon-α/β receptor, CAS No.rp174250, Agonist of Interferon-α/β receptor

CAS: rp174250 Cat. No.: rp174250

GRADE & PURITY Moligand™

Specifications

Product Name

IFN-α10, Agonist of Interferon-α/β receptor, CAS No.rp174250

Synonyme

IFN alpha-10;interferon alpha-10;interferon alpha-6L;interferon alpha-C

Note

Moligand™

Spezifikationen & Reinheit

Moligand™

Aktionsart

AGONIST

Mechanismus der Wirkung

Agonist of Interferon-α/β receptor

CAS

rp174250

Molekültyp

Peptide

Lagerung und Versand

Storage

Room temperature

Zugehörige Ziele (menschlich)

IFNAR2 Tclin Interferon alpha/beta receptor 2 (0 Activities)

Discover Target: IFNAR2

Activity Type	Activity Value -log(M)	Mechanism of Action	Activity Reference	Publications (PubMed IDs)

IFNAR1 Tclin Interferon alpha/beta receptor 1 (0 Activities)

Discover Target: IFNAR1

Activity Type	Activity Value -log(M)	Mechanism of Action	Activity Reference	Publications (PubMed IDs)

Genetische Informationen

• Alternate Names: IFN alpha-10;interferon alpha-10;interferon alpha-6L;interferon alpha-C
• Referenz:
  • 1. Kinetics and inhibition of recombinant human cystathionine gamma-lyase. Toward the rational control of transsulfuration., The Journal of biological chemistry, Steegborn, C C and 7 more authors.
  • 2. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences., Proceedings of the National Academy of Sciences of the United States of America, Strausberg, Robert L RL and 83 more authors.
  • 3. Genomic basis of cystathioninuria (MIM 219500) revealed by multiple mutations in cystathionine gamma-lyase (CTH)., Human genetics, Wang, Jian J and Hegele, Robert A RA.
  • 4. Cloning and nucleotide sequence of human liver cDNA encoding for cystathionine gamma-lyase., Biochemical and biophysical research communications, Lu, Y Y, O'Dowd, B F BF, Orrego, H H and Israel, Y Y.
  • 5. Single nucleotide polymorphism in CTH associated with variation in plasma homocysteine concentration., Clinical genetics, Wang, J J, Huff, A M AM, Spence, J D JD and Hegele, R A RA.
  • 6. Cystathionine gamma-lyase overexpression inhibits cell proliferation via a H2S-dependent modulation of ERK1/2 phosphorylation and p21Cip/WAK-1., The Journal of biological chemistry, Yang, Guangdong G, Cao, Kun K, Wu, Lingyun L and Wang, Rui R.
  • 7. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)., Genome research, Gerhard, Daniela S DS and 115 more authors.
  • 8. Towards a proteome-scale map of the human protein-protein interaction network., Nature, Rual, Jean-François JF and 37 more authors.
  • 9. The DNA sequence and biological annotation of human chromosome 1., Nature, Gregory, S G SG and 178 more authors.
  • 10. Polymorphisms in one-carbon metabolism and trans-sulfuration pathway genes and susceptibility to bladder cancer., International journal of cancer, Moore, Lee E LE and 14 more authors. more
  • 11. Toward a confocal subcellular atlas of the human proteome., Molecular & cellular proteomics : MCP, Barbe, Laurent L and 10 more authors.
  • 12. Kinetic properties of polymorphic variants and pathogenic mutants in human cystathionine gamma-lyase., Biochemistry, Zhu, Weidong W, Lin, Alexander A and Banerjee, Ruma R.
  • 13. Pathway-based evaluation of 380 candidate genes and lung cancer susceptibility suggests the importance of the cell cycle pathway., Carcinogenesis, Hosgood, H Dean HD and 12 more authors.
  • 14. Relationship between cystathionine gamma-lyase gene polymorphism and essential hypertension in Northern Chinese Han population., Chinese medical journal, Li, Yun Y and 8 more authors.
  • 15. Active cystathionine beta-synthase can be expressed in heme-free systems in the presence of metal-substituted porphyrins or a chemical chaperone., The Journal of biological chemistry, Majtan, Tomas T, Singh, Laishram R LR, Wang, Liqun L, Kruger, Warren D WD and Kraus, Jan P JP.
  • 16. MALDI-TOF MS genotyping of polymorphisms related to 1-carbon metabolism using common and mass-modified terminators., Clinical chemistry, Meyer, Klaus K, Fredriksen, Ase A and Ueland, Per Magne PM.
  • 17. Structural basis for the inhibition mechanism of human cystathionine gamma-lyase, an enzyme responsible for the production of H(2)S., The Journal of biological chemistry, Sun, Qingxiang Q and 10 more authors.
  • 18. Oral facial clefts and gene polymorphisms in metabolism of folate/one-carbon and vitamin A: a pathway-wide association study., Genetic epidemiology, Boyles, Abee L AL and 16 more authors.
  • 19. Large-scale proteomics and phosphoproteomics of urinary exosomes., Journal of the American Society of Nephrology : JASN, Gonzales, Patricia A PA and 7 more authors.
  • 20. An association study of 45 folate-related genes in spina bifida: Involvement of cubilin (CUBN) and tRNA aspartic acid methyltransferase 1 (TRDMT1)., Birth defects research. Part A, Clinical and molecular teratology, Franke, Barbara B and 7 more authors.
  • 21. Polymorphisms in innate immunity genes and lung cancer risk in Xuanwei, China., Environmental and molecular mutagenesis, Shen, Min M and 12 more authors.
  • 22. H2S biogenesis by human cystathionine gamma-lyase leads to the novel sulfur metabolites lanthionine and homolanthionine and is responsive to the grade of hyperhomocysteinemia., The Journal of biological chemistry, Chiku, Taurai T and 5 more authors.
  • 23. Variations in folate pathway genes are associated with unexplained female infertility., Fertility and sterility, Altmäe, Signe S and 7 more authors.
  • 24. Bile-acid-activated farnesoid X receptor regulates hydrogen sulfide production and hepatic microcirculation., World journal of gastroenterology, Renga, Barbara B, Mencarelli, Andrea A, Migliorati, Marco M, Distrutti, Eleonora E and Fiorucci, Stefano S.
  • 25. Cystathionine gamma-lyase: Clinical, metabolic, genetic, and structural studies., Molecular genetics and metabolism, Kraus, Jan P JP and 14 more authors.
  • 26. Relative contributions of cystathionine beta-synthase and gamma-cystathionase to H2S biogenesis via alternative trans-sulfuration reactions., The Journal of biological chemistry, Singh, Sangita S, Padovani, Dominique D, Leslie, Rachel A RA, Chiku, Taurai T and Banerjee, Ruma R.
  • 27. PTEN identified as important risk factor of chronic obstructive pulmonary disease., Respiratory medicine, Hosgood, H Dean HD, Menashe, Idan I, He, Xingzhou X, Chanock, Stephen S and Lan, Qing Q.
  • 28. Genetic susceptibility to distinct bladder cancer subphenotypes., European urology, Guey, Lin T LT and 18 more authors.
  • 29. Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip., American journal of human genetics, Talmud, Philippa J PJ and 38 more authors.
  • 30. Integrative predictive model of coronary artery calcification in atherosclerosis., Circulation, McGeachie, Michael M and 13 more authors.
  • 31. Cystathionine beta-synthase 844Ins68 polymorphism is not associated with the levels of homocysteine and cysteine in an Indian population., Biomarkers : biochemical indicators of exposure, response, and susceptibility to chemicals, Kumar, Jitender J, Garg, Gaurav G, Karthikeyan, Ganesan G and Sengupta, Shantanu S.
  • 32. The expression and activity of cystathionine-γ-lyase and 3-mercaptopyruvate sulfurtransferase in human neoplastic cell lines., Amino acids, Jurkowska, Halina H, Placha, Wojciech W, Nagahara, Noriuki N and Wróbel, Maria M.
  • 33. Ancient origin of the CTH alelle carrying the c.200C>T (p.T67I) variant in patients with cystathioninuria., Clinical genetics, Espinós, C C and 8 more authors.
  • 34. Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study., Diabetes care, Bailey, Swneke D SD and 11 more authors.
  • 35. Maternal genes and facial clefts in offspring: a comprehensive search for genetic associations in two population-based cleft studies from Scandinavia., PloS one, Jugessur, Astanand A and 12 more authors.
  • 36. [Expression of cystathionine-γ-lyase/hydrogen sulfide pathway in CVB3-induced myocarditis in mice]., Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics, Hua, Wang W and 6 more authors.
  • 37. Folate-metabolizing gene variants and pregnancy outcome of IVF., Reproductive biomedicine online, Laanpere, M M and 5 more authors.
  • 38. Specificity protein-1 as a critical regulator of human cystathionine gamma-lyase in smooth muscle cells., The Journal of biological chemistry, Yang, Guangdong G, Pei, Yanxi Y, Teng, Huajian H, Cao, Qiuhui Q and Wang, Rui R.
  • 39. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium., Briefings in bioinformatics, Gaudet, Pascale P, Livstone, Michael S MS, Lewis, Suzanna E SE and Thomas, Paul D PD.
  • 40. Expression of cystathionine β-synthase and cystathionine γ-lyase in human pregnant myometrium and their roles in the control of uterine contractility., PloS one, You, Xing-Ji XJ and 8 more authors.
  • 41. MicroRNA-21 represses human cystathionine gamma-lyase expression by targeting at specificity protein-1 in smooth muscle cells., Journal of cellular physiology, Yang, Guangdong G, Pei, Yanxi Y, Cao, Qiuhui Q and Wang, Rui R.
  • 42. H2S-Induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response., Science signaling, Krishnan, Navasona N, Fu, Cexiong C, Pappin, Darryl J DJ and Tonks, Nicholas K NK.
  • 43. Characterization of hydrogen sulfide and its synthases, cystathionine β-synthase and cystathionine γ-lyase, in human prostatic tissue and cells., Urology, Guo, Hui H and 5 more authors.
  • 44. Sp1 is involved in regulation of cystathionine γ-lyase gene expression and biological function by PI3K/Akt pathway in human hepatocellular carcinoma cell lines., Cellular signalling, Yin, Peng P and 12 more authors.
  • 45. H₂S protects against pressure overload-induced heart failure via upregulation of endothelial nitric oxide synthase., Circulation, Kondo, Kazuhisa K and 14 more authors.
  • 46. Reduced cystathionine γ-lyase and increased miR-21 expression are associated with increased vascular resistance in growth-restricted pregnancies: hydrogen sulfide as a placental vasodilator., The American journal of pathology, Cindrova-Davies, Tereza T and 5 more authors.
  • 47. Dysregulation of hydrogen sulfide producing enzyme cystathionine γ-lyase contributes to maternal hypertension and placental abnormalities in preeclampsia., Circulation, Wang, Keqing K and 14 more authors.
  • 48. Regulation of cystathionine γ-lyase in mammalian cells by hypoxia., Biochemical genetics, Wang, Maoxian M, Guo, Zhanyun Z and Wang, Shilong S.
  • 49. A genome-wide association study of chemotherapy-induced alopecia in breast cancer patients., Breast cancer research : BCR, Chung, Suyoun S and 6 more authors.
  • 50. [Cystathionine γ-lyase]., Postepy higieny i medycyny doswiadczalnej (Online), Jurkowska, Halina H, Kaczor-Kamińska, Marta M, Bronowicka-Adamska, Patrycja P and Wróbel, Maria M.
  • 51. Decreased cystathionine-γ-lyase (CSE) activity in livers of type 1 diabetic rats and peripheral blood mononuclear cells (PBMC) of type 1 diabetic patients., The Journal of biological chemistry, Manna, Prasenjit P, Gungor, Neslihan N, McVie, Robert R and Jain, Sushil K SK.
  • 52. Hydrogen sulfide (H2S)/cystathionine γ-lyase (CSE) pathway contributes to the proliferation of hepatoma cells., Mutation research, Pan, Yan Y and 5 more authors.
  • 53. The cystathionine γ-lyase/hydrogen sulfide system maintains cellular glutathione status., The Biochemical journal, Lee, Zheng-Wei ZW, Low, Yi-Lian YL, Huang, Shufen S, Wang, Tianxiao T and Deng, Lih-Wen LW.
  • 54. The binding site for the transcription factor, NF-κB, on the cystathionine γ-lyase promoter is critical for LPS-induced cystathionine γ-lyase expression., International journal of molecular medicine, Wang, Maoxian M, Guo, Zhanyun Z and Wang, Shilong S.
  • 55. Regulation of cystathionine gamma-lyase/H₂S system and its pathological implication., Frontiers in bioscience (Landmark edition), Zhao, Kexin K, Li, Hongzhu H, Li, Shuangshuang S and Yang, Guangdong G.
  • 56. Dysregulation of hydrogen sulphide metabolism impairs oviductal transport of embryos., Nature communications, Ning, Nannan N and 5 more authors.
  • 57. Wnt/β-catenin signaling induces the transcription of cystathionine-γ-lyase, a stimulator of tumor in colon cancer., Cellular signalling, Fan, Kun K and 7 more authors.
  • 58. miRNA-30 family inhibition protects against cardiac ischemic injury by regulating cystathionine-γ-lyase expression., Antioxidants & redox signaling, Shen, Yaqi Y and 7 more authors.
  • 59. Role of the cystathionine γ lyase/hydrogen sulfide pathway in human melanoma progression., Pigment cell & melanoma research, Panza, Elisabetta E and 11 more authors.
  • 60. A proteome-scale map of the human interactome network., Cell, Rolland, Thomas T and 69 more authors.
  • 61. Neurodegeneration in Huntington's disease involves loss of cystathionine γ-lyase., Cell cycle (Georgetown, Tex.), Paul, Bindu D BD and Snyder, Solomon H SH.
  • 62. The importance of MTHFR, MTR, MTRR and CSE expression levels in Caucasian women with preeclampsia., European journal of obstetrics, gynecology, and reproductive biology, Seremak-Mrozikiewicz, Agnieszka A and 6 more authors.
  • 63. The importance of rs1021737 and rs482843 polymorphisms of cystathionine gamma-lyase in the etiology of preeclampsia in the Caucasian population., Ginekologia polska, Mrozikiewicz, Przemysław M PM and 8 more authors.
  • 64. Cystathionine γ-lyase, a H2S-generating enzyme, is a GPBAR1-regulated gene and contributes to vasodilation caused by secondary bile acids., American journal of physiology. Heart and circulatory physiology, Renga, Barbara B and 9 more authors.
  • 65. Correlation between the cystathionine-γ-lyase (CES) and the severity of peptic ulcer disease., African health sciences, Chen, Xiong X, Wan, Ying-Chun YC, Guo, Tao T, Xu, Can-Xia CX and Wang, Fen F.
  • 66. MPST but not CSE is the primary regulator of hydrogen sulfide production and function in the coronary artery., American journal of physiology. Heart and circulatory physiology, Kuo, Maggie M MM and 10 more authors.
  • 67. Transcriptional Regulation of Cystathionine-γ-Lyase in Endothelial Cells by NADPH Oxidase 4-Dependent Signaling., The Journal of biological chemistry, Mistry, Rajesh K RK and 8 more authors.
  • 68. LPS Up-Regulates Cystathionine γ -Lyase Gene Expression in Primary Human Macrophages via NF-κB/ERK Pathway., Inflammation & allergy drug targets, Badiei, Alireza A, Gieseg, Steven S, Davies, Sian S, Izani Othman, Mohd M and Bhatia, Madhav M.
  • 69. Radiation Exposure Promotes Hepatocarcinoma Cell Invasion through Epithelial Mesenchymal Transition Mediated by H2S/CSE Pathway., Radiation research, Pan, Yan Y, Zhou, Cuiping C, Yuan, Dexiao D, Zhang, Jianghong J and Shao, Chunlin C.
  • 70. Cystathionine γ-lyase(CSE)/hydrogen sulfide system is regulated by miR-216a and influences cholesterol efflux in macrophages via the PI3K/AKT/ABCA1 pathway., Biochemical and biophysical research communications, Gong, Duo D and 15 more authors.
  • 71. MicroRNA-186 promotes macrophage lipid accumulation and secretion of pro-inflammatory cytokines by targeting cystathionine γ-lyase in THP-1 macrophages., Atherosclerosis, Yao, Yan Y and 9 more authors.
  • 72. Cystathionine γ-lyase is expressed in human atherosclerotic plaque microvessels and is involved in micro-angiogenesis., Scientific reports, van den Born, J C JC and 5 more authors.
  • 73. Dichotomous effects of isomeric secondary amines containing an aromatic nitrile and nitro group on human aortic smooth muscle cells via inhibition of cystathionine-γ-lyase., Biochimie, Ji, Yajing Y and 6 more authors.
  • 74. Distinctive expression pattern of cystathionine-β-synthase and cystathionine-γ-lyase identifies mesenchymal stromal cells transition to mineralizing osteoblasts., Journal of cellular physiology, Gambari, Laura L and 6 more authors.
  • 75. Age-Dependent Allergic Asthma Development and Cystathionine Gamma-Lyase Deficiency., Antioxidants & redox signaling, Wang, Peipei P and 6 more authors.
  • 76. Augmented H2S production via cystathionine-beta-synthase upregulation plays a role in pregnancy-associated uterine vasodilation., Biology of reproduction, Sheibani, Lili L and 7 more authors.
  • 77. Total sulfane sulfur bioavailability reflects ethnic and gender disparities in cardiovascular disease., Redox biology, Rajpal, Saurabh S and 12 more authors.
  • 78. Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides., Gene, Maruyama, K K and Sugano, S S.

Application Protocols

Manufacturer-tested applications, recommended dilutions, and positive control details are Not specified for this item; refer to CoA/Spec Sheet.

Because protocols are assay- and matrix-specific, users should develop or adapt internal SOPs. Common research workflows with interferon-α family proteins include (general, not item-specific):

• Cell stimulation followed by phospho-STAT1 Western blot or flow cytometry.
• ISRE-luciferase reporter assays for dose–response curves and EC50 estimation.
• qPCR of canonical ISGs (e.g., MX1, OAS1, IFIT1) to confirm transcriptional responses.

These examples are provided as general context only and do not constitute validated instructions for this item.

Biological Roles

General biology (literature; not item-specific)

• IFN-α10 is a member of the type I interferon family (IFN-α subtypes) that signals through the IFNAR1/IFNAR2 receptor complex to activate JAK–STAT pathways, leading to transcription of interferon-stimulated genes (ISGs).
• Functional outcomes studied in research include establishment of an antiviral state, modulation of antigen presentation, and regulation of innate/adaptive immune crosstalk—mechanistically through ISG induction and secondary cytokine networks.
• Different IFN-α subtypes can show quantitative differences in receptor affinity and signaling potency; IFN-α10-specific dynamics are the subject of ongoing basic research (literature).

Assay contexts (research use only)

• Cell-based reporter assays (e.g., ISRE/ISG54 luciferase) to quantify pathway activation.
• Phospho-STAT1/STAT2/IRF9 complex formation studies by immunoblot or flow cytometry.
• Gene expression profiling (qPCR/RNA-seq) to map ISG signatures and dose–response behavior.

No medical or clinical claims are made for this product. Use is restricted to laboratory research applications.

Buffer Applications

Buffers are relevant primarily for reconstitution and handling rather than pH-controlled catalysis.

• Item-specific buffer composition or recommended pH: Not specified for this item; refer to CoA/Spec Sheet.

General buffer guidance for cytokine handling (literature; not item-specific):

• Common working buffers: PBS (pH 7.2–7.4), 10–20 mM HEPES (pH 7.2–7.6), or Tris-based buffers at neutral pH. Ionic strength ~100–200 mM NaCl helps maintain solubility.
• Stabilizers: 0.1% carrier protein (BSA/HSA) and/or 5–10% glycerol can reduce adsorption and improve freeze–thaw tolerance.
• Filtration: If sterile work is required, 0.22 μm low-protein-binding filters are preferred; avoid shear/foaming.
• Low-binding plastics and gentle mixing preserve activity, especially at low nanomolar concentrations.

For electrophoresis or cell-culture-specific buffer recipes, adapt to your assay’s requirements and validate recovery/activity post-buffer exchange.

Green Alternatives

This material is a protein/cytokine research reagent; “green solvent” alternatives are not directly relevant. Nevertheless, greener laboratory practice can still be applied.

Greener practice suggestions (general; not item-specific):

• Miniaturize assays to reduce reagent consumption (microplate formats, automated liquid handling).
• Use reusable, validated buffer concentrates to minimize packaging waste; prepare only the volume needed for an experiment.
• Select phosphate or HEPES buffers prepared from high-purity salts; avoid unnecessary organic cosolvents that can complicate waste streams.
• Plan aliquoting to minimize discard due to freeze–thaw degradation, thereby reducing total material usage.

There are no direct “alternative reagents” to a specific cytokine standard. The balance is between experimental fidelity and resource footprint; optimize assay design accordingly.

Pharmaceutical Uses

No therapeutic or clinical use is claimed or supported for this product. Research use only.

Possible roles in pharmaceutical R&D workflows (general; not item-specific):

• Reference cytokine in cell-based potency assays to benchmark pathway activation or to calibrate bioassays for interferon-signaling modulators.
• Control material in formulation screening to study protein stability, adsorption, and excipient effects (e.g., polysorbates, sugars) in small-scale experiments.
• Tool reagent for target-validation studies involving IFNAR signaling.

Regulatory and compendial status: Not specified for this item; refer to CoA/Spec Sheet. This product is not certified to any pharmacopeial monograph and is not intended for human or veterinary use.

Physical Properties

Item-specific physical data

• Appearance: Not specified for this item; refer to CoA/Spec Sheet.
• Density, BP/MP, refractive index, logP, pKa: Not applicable/Not specified for this item; refer to CoA/Spec Sheet.

General properties for interferon-α family proteins (literature; not item-specific)

• Typical molecular mass (mature protein): ~19–20 kDa; exact value depends on sequence and glycosylation.
• Isoelectric point (pI): commonly in the ~5.5–6.5 range, sequence-dependent.
• Solubility: readily soluble in aqueous buffers (e.g., PBS, HEPES) at neutral pH; inclusion of carrier proteins (0.1% BSA or HSA) often improves stability and prevents adsorption to plastics.
• Stability considerations: proteins of this class are sensitive to repeated freeze–thaw and surface adsorption; stability can benefit from glycerol (10–50%), low ionic strength, and avoidance of foaming (literature).

Note: The above are general/literature characteristics of IFN-α family proteins and do not constitute specifications for this particular item. Consult the CoA/Spec Sheet for item-specific measurements.

Quality and Grades

Item-specific grade

• Grade/Purity: Moligand™ (from Product Data).

What Moligand™ typically denotes (general explanation; not item-specific specs)

• Moligand™ is an internal Aladdin designation used for compounds or reagents curated for molecular interaction studies, screening, or ligand discovery workflows. It emphasizes suitability for research applications focused on binding/target engagement rather than certified therapeutic use.

Acceptance criteria and documentation

• Item-specific acceptance criteria (purity method, residual solvents, counterions, endotoxin/bioburden if applicable) are Not specified for this item; refer to CoA/Spec Sheet.
• If the material is supplied in solid or solution form, packaging details, fill accuracy, and stabilizers are Not specified for this item; refer to CoA/Spec Sheet.

Implications for users

• For quantitative bioassays, request and review the CoA to confirm assay-relevant attributes (e.g., concentration, activity units, residuals). Validate performance in your system with internal controls.
• No pharmaceutical or clinical grade claims are made. Research use only.

Reaction and Applications

As a cytokine/protein-standard–type material, IFN-α10 is not a classical synthetic reagent and is not typically used to mediate chemical reactions.

Potential research applications (general/literature; not item-specific):

• Receptor–ligand studies: interrogation of IFNAR1/IFNAR2 binding and downstream JAK–STAT pathway activation in cell-based assays (e.g., STAT1/ISRE reporter readouts).
• Pathway mapping: induction of interferon-stimulated genes (ISGs) and analysis of signaling kinetics, desensitization, and cross-talk with other cytokines.
• Screening: as a positive control ligand or antagonist/agonist counter-screen tool in discovery of IFN pathway modulators.
• Proteomics: benchmarking phospho-proteome changes upon stimulation.

Item-specific application claims from the manufacturer are not provided for this SKU. Validate suitability in your assay system and consult the CoA/Spec Sheet for any additional guidance.

Reaction Conditions

Classical reaction-condition guidance (solvent, temperature, catalysts, yields) is not applicable to a cytokine/protein reagent like IFN-α10.

General experimental conditions for biological assays (literature; not item-specific):

• Temperature: Many cell-based assays are conducted at 37°C (mammalian cells), with cytokine preincubation ranging from minutes to hours depending on readout (e.g., 15–60 min for phospho-STAT; 4–24 h for ISG expression).
• Concentration ranges: Typical working concentrations span from low picomolar to low nanomolar, determined empirically by potency and assay sensitivity.
• Matrix: Serum-containing vs serum-free conditions can markedly affect signaling; include proper vehicle and time-matched controls.

These are general practices only. Item-specific activity, concentration, or potency data are Not specified for this item; refer to CoA/Spec Sheet and perform pilot titrations in your system.

Safety and Handling

GHS and hazard information (from Product Data)

• Signal Word: Not specified for this item; refer to SDS.
• H-Statements: Not specified for this item; refer to SDS.
• GHS Classification/Pictograms: Not specified for this item; refer to SDS.

General lab safety guidance (biochemical reagents)

• Handle with standard laboratory PPE: lab coat, gloves, and safety glasses. Work in a clean area to avoid contamination of biological assays.
• Avoid inhalation of powders/aerosols and contact with skin/eyes. In case of contact, rinse with water and seek medical attention per institutional policy.
• Use low-retention tips/tubes to minimize adsorption losses. Avoid generating aerosols when reconstituting or pipetting.

Storage incompatibilities and precautions (general)

• Avoid strong acids/bases and oxidizing agents that may denature proteins. Do not expose to prolonged elevated temperatures.
• Minimize freeze–thaw cycling; aliquot upon first reconstitution (general best practice; see item-specific storage below).

Always consult the product’s SDS and institutional risk assessments for authoritative safety and disposal guidance. This product is designated for research use only.

Solvent Selection

This product name corresponds to a protein/cytokine (IFN-α10). Organic solvent selection paradigms (e.g., polarity indexes for reaction media) are generally not applicable.

• Item-specific solvent or buffer recommendations: Not specified for this item; refer to CoA/Spec Sheet.

General guidance (literature; not item-specific):

• Reconstitution and handling are typically performed in aqueous buffers such as PBS (pH ~7.2–7.4) or HEPES buffers. Including carrier protein (e.g., 0.1% BSA/HSA) and/or 5–10% glycerol may improve stability and reduce adsorption.
• Avoid high percentages of organic cosolvents (acetonitrile, methanol, DMSO), which can denature many proteins. If a small amount of DMSO is necessary (e.g., to co-solubilize additives), keep it minimal (<5%) and validate activity.
• Use low-binding plastic ware to reduce losses at low concentrations.

For this specific item, defer to the CoA/Spec Sheet for any supplied buffer composition or reconstitution solvent instructions.

Storage and Reconstitution

Item-specific storage conditions (from Product Data)

• Storage Conditions: Room temperature.
• Shipped In: Not specified for this item; refer to CoA/Spec Sheet.

Item-specific reconstitution buffer, concentration, and stabilizers: Not specified for this item; refer to CoA/Spec Sheet.

General guidance (literature; not item-specific)

• Upon receipt, verify container integrity. If supplied lyophilized, reconstitute with sterile, neutral pH buffer (e.g., PBS or 10 mM HEPES, pH ~7.2–7.4) optionally containing 0.1% carrier protein (BSA/HSA) and 5–10% glycerol to improve stability.
• Prepare small aliquots to avoid repeated freeze–thaw. Store aliquots according to your lab’s validated practice for proteins of this class (commonly −20°C to −80°C for long-term; short-term at 2–8°C), unless the item’s CoA specifies otherwise.
• Mix gently by slow pipetting; avoid vigorous vortexing or foaming. Use low-binding plasticware.

Always defer to the specific CoA/Spec Sheet for this SKU for authoritative instructions. Research use only.

Structure and Identity

Item-specific identifiers (from Product Data)

• SKU: rp174250
• Product Name: IFN-α10
• CAS: rp174250 (catalog placeholder)
• Grade: Moligand™
• Molecular formula: Not specified for this item; refer to CoA/Spec Sheet.
• Molecular weight: Not specified for this item; refer to CoA/Spec Sheet.
• SMILES/InChI/InChIKey: Not specified for this item; refer to CoA/Spec Sheet.

General structural information (literature; not item-specific)

• IFN-α10 commonly refers to interferon alpha-10, a type I interferon cytokine encoded by IFNA10 (Homo sapiens). It is a single-chain protein that signals via the heterodimeric interferon-α/β receptor (IFNAR1/IFNAR2).
• Typical composition: polypeptide of ~187 amino acids including a signal peptide (literature), adopting a four-helix bundle topology characteristic of class II cytokines.
• Key structural features: helical bundle, conserved cysteines forming disulfide bonds (family-typical) that stabilize the fold; receptor-binding epitopes distributed on helices A–D (literature).

2D/primary structure description (literature)

• Linear amino acid sequence with an N-terminal secretion signal (removed in mature form) and a compact helical core in the mature cytokine. Post-translational modifications (e.g., glycosylation) are isoform- and expression-system dependent (literature).

Synthetic Utility

This product is a cytokine/protein and is not typically used as a building block or reagent in synthetic organic chemistry.

• Not applicable: It does not serve as a protecting group reagent, coupling partner, or catalyst in standard synthetic transformations.
• For chemical biology, it may be used as a biological ligand in binding/functional assays, but this falls outside classical synthetic utility.

If your work requires chemical modification of proteins (e.g., bioconjugation), select reaction chemistries compatible with proteins (maleimide–thiol, NHS–lysine, click chemistry under aqueous conditions) and validate that modifications preserve activity. Item-specific compatibility is Not specified for this item; refer to CoA/Spec Sheet.

Target Specificity

Item-specific target information (e.g., species reactivity, receptor binding constants, epitope/clone if antibody) is Not specified for this item; refer to CoA/Spec Sheet.

General background (literature; not item-specific):

• IFN-α subtypes, including IFN-α10, signal via the type I interferon receptor complex (IFNAR1/IFNAR2), engaging JAK1/TYK2 kinases and STAT1/STAT2/IRF9 to regulate ISG expression.

For quantitative binding metrics (Kd, kinetics) or cross-species activity, consult the specific batch documentation or perform empirical testing.