Recombinant Human IFN alpha2a Protein

Name: Recombinant Human IFN alpha2a Protein
Brand: Beta LifeScience
SKU: BL-1773NP
Availability: InStock

BL-1773NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

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Product Overview

Description	Recombinant Human Interferon Alpha-2a is produced by our E.coli expression system and the target gene encoding Cys24-Glu188(Arg46Lys) is expressed.
Accession	P01563
Synonym	Interferon Alpha-2; IFN-Alpha-2; Interferon Alpha-A; LeIF A; IFNA2
Gene Background	At least 23 different variants of IFN-α are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-α subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-α subtypes only differ in their sequences by one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end.
Molecular Mass	19.24 KDa
Apmol Mass	16 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.2.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Produced by macrophages, IFN-alpha have antiviral activities.
Subcellular Location	Secreted.
Protein Families	Alpha/beta interferon family
Database References	HGNC: 5423 OMIM: 147562 KEGG: hsa:3440 STRING: 9606.ENSP00000369554 UniGene: PMID: 28958921 Increased protein aggregation and decreased function of IFNA2a upon oxidation correlated with the site of modification identified by proteolysis-coupled mass spectrometry and local structural changes in the protein detected by 2D NMR. PMID: 30324266 These experimental data establish the retromer complex as a key spatiotemporal regulator of IFNAR endosomal sorting and a new factor in type-I IFN-induced JAK/STAT signalling and gene transcription. PMID: 27917878 PVT1 interacts with STAT1 to inhibit IFN-alpha signaling and tumor cells proliferation. PMID: 29715456 Here, we investigated the molecular signals induced by ARI(azacytidine (A) and romidepsin (R), with IFNalpha2 ) treatment and found that this drug combination increased the accessibility to regulatory sequences of IFN-stimulated genes and IFN transcription regulatory factors that were epigenetically silenced in both colorectal cancer cells and Dendritic Cells. PMID: 28615266 All the tested TLRAs induced greater infant IFN-alpha2 production compared to newborn and adult blood. In contrast, CpG induced greater IFN-gamma, IL-1beta, IL-4, IL-12p40, IL-10 and CXCL8 in newborn than in infant and adult blood. PMID: 27081760 Interferon-alpha-induced CD100 expression on naive CD8(+) T cells enhances antiviral responses to hepatitis C infection through CD72 signal transduction. PMID: 28222623 Tumor-associated M2 macrophages in mycosis fungoides acquire immunomodulatory function on exposure to IFN-alpha2a and IFN-gamma. PMID: 27342040 The variant models of the hIFNalpha-2b displayed structural and conformational changes that signified that changes to hIFNalpha-2b may be a risk factor in addition to other known factors associated with onset/progression of female breast carcinoma. PMID: 27403569 Increase in serum IFNA2 is associated with adenoma. PMID: 25793917 Data suggest IFNA2 binding to extracellular domain of IFN receptors IFNAR1 or IFNAR2 promotes proximity between intracellular domains; signaling depends on duration of activation and affinity of binding rather than specific conformational changes. PMID: 26679999 Report biased expression of human interferon alpha-2b and Escherichia coli methionine amino peptidase genes under control of single promoter in E. coli. PMID: 27087087 interferon alpha-2b gene mutations were identified among brain tumor patients; highest percentage of frameshift mutations was identified; patients were found to be under environmental stress from contaminated drinking water and from local gamma radiations PMID: 25837663 PPARalpha activation by an agonist WY-14643 could potentiate IFN-alpha responses, reverse IFN-alpha refractoriness, and enhance viral eradication in hepatocytes. PMID: 25734487 modulates transitional B cell signaling and function in Systemic Lupus Erythematosus patients PMID: 25678471 The chronic use of low dose of radiations by occupational workers has a significant correlation with mutational effects on interferon alpha 2b gene, further evident by depressed interferon alpha levels in serum. PMID: 25768396 IFN-beta was significantly more effective than IFNA2 in protecting human head and neck squamous cell carcinoma lines from oncolysis by vesicular stomatitis. PMID: 25995245 The structure, mechanism of action and biological activities of IFNalpha2. [Review] PMID: 25982860 Therefore, this study associated, for the first time, in a large panel of pancreatic cancer cell lines the effects of IFN-alpha/-beta with the expression of type-I IFN receptors. PMID: 24460759 IFN-1ant may be a therapeutic candidate for the treatment of specific viral infections without inducing the immunomodulatory and antiproliferative functions of wild-type IFN. PMID: 24866020 IFNalpha serum marker could be used to identify a group of rheumatoid Arthritis patients with increased disease activity, endothelial progenitor cell imbalance, enhanced proinflammatory profile and higher cardiovascular risk. PMID: 24465874 these findings establish critical and essential roles for SKAR in the regulation of mRNA translation of IFN-sensitive genes and induction of IFN-alpha biological responses. PMID: 25049393 Hepatitis B virus could induce both SOCS-1 and 3 expression regardless of endogenous interferon level. PMID: 24636575 IL6 is an inducer of IRF9 expression in prostate cancer and a sensitizer for the antiproliferative effects of IFNalpha2. PMID: 23913484 IFNA2 inhibits viral protein expression through PKR activation, leading to a decrease of viral protein synthesis. PMID: 24089560 These studies identify IFNalpha derived from lymph nodes, rather than blood leukocytes, as a possible source of the IFN-I signature that contributes to immune activation in HIV-1 infection PMID: 23437155 Pre-treatment waking hypothalamic-pituitary-adrenal (HPA) axis response is greater in subjects switching to major depressive disorder during INFalpha2a treatment and may constitute a vulnerability factor in patients with hepatitis C virus infection. PMID: 22571879 The association with clinical disease and activation of multiple inflammatory cytokines supports a role for IFN-alpha2 in disease perpetuation in a large subset of systemic lupus erythematosis patients. PMID: 23213068 Obese subjects showed a decreased ability to produce IFN-alpha and IFN-beta in response to TLR ligands; this response was associated with increased basal levels of SOCS3 but not SOCS1. PMID: 22951153 analysis of how an N-acetylgalactosamine residue at threonine 106 modifies the dynamics and structure of interferon alpha2a around the glycosylation site PMID: 23184955 The authors concluded that IFN-alpha-induced inhibition of miR-122 may negatively affect the anti-hepatitis B virus function of IFN-alpha. PMID: 23055569 Results showed that missense mutations in transmembrane protein 2 p.Ser1254Asn, interferon alpha 2 p.Ala120Thr, its regulator NLR family member X1 p.Arg707Cys, and complement component 2 p.Glu318Asp were associated with chronic hepatitis B. PMID: 22610944 Successful immunostimulation by IFNalpha2b may help tongue squamous cell carcinoma patients in clinical improvement. PMID: 22885264 Data indicate that the combination of AAV2.IL-4 and AAV2.IFN-alpha was not significantly different as compared to AAV2.IL-4 alone. PMID: 22685550 The crystal structures of two human type I IFN ternary signaling complexes containing IFNalpha2 and IFNomega reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between type I IFNs. PMID: 21854986 Structural AA changes in the C-helix interacting with IFNAlphaR1 may change the signaling dynamics leading to elevated APOBEC3 & lower IDO by an engineered mutant derived from the amino-terminal region of IFNalpha21b and the COOH-terminus from IFNalpha2c. PMID: 21757613 interferon-stimulated genes which exerts its negative feedback action by taking advantage of the weakness of IFNalpha2 binding to the receptor PMID: 22731491 protein kinase, DNA-activated catalytic polypeptide (PRKDC), was confirmed to play a role in MyD88-induced IFNA2 activation and IL-8 secretion PMID: 22332739 variation at IFNA2 -173 and IFNA8 -884 conditions reduced IFN-alpha production, and increased susceptibility to SMA and mortality PMID: 22570109 Data indicate that the production of IFN-alpha in supernatant of transfected cells was about 3.15 ng/mL. PMID: 22482409 IFNalpha rapidly down-regulates BCL-6 mRNA in purified mouse normal germinal center B cells. PMID: 22204827 we have demonstrated that IFNalpha2, a type I interferon, increases the expression of TLR3 on human dermal fibroblasts PMID: 21223583 Interferon alpha 2 regulates MAPK and STAT1 pathways in human hepatoma cells. PMID: 21466707 Degos disease is a distinct vascular injury syndrome whereby a dysregulated interferon-alpha response in concert with membranolytic attack complex deposition may contribute to the unique vascular changes. PMID: 21411783 These findings indicate that the expression of MxA, 2',5'-OAS and PKR are up-regulate by PI3K-AKT signal pathway, and Raf-MEK-ERK signal pathway has a negative regulatory effect on the expression of MxA and no significant effect on 2',5'-OAS and PKR. PMID: 20309637 Studies indicate that it remains unclear whether interruption of IFNalphaA and IL-10 signaling in the absence of CD73 activity results from a deficiency of its product adenosine or an accumulation of its substrate nucleotides. PMID: 21057730 Data show that pDCs and type I IFNs promote inflammatory responses and wound healing in injured skin. PMID: 21115688 The result suggests that hyper-induction of TNF-alpha in human macrophages is not always associated with a highly pathogenic phenotype of avian and human influenza viruses. PMID: 20532927 Strategies are described to maximize expression of rightly processed human INF alpha2b protein in Pichia. PMID: 20159042 Data show that serum concentrations of pegylated interferon alpha-2b increased in a dose-related manner. PMID: 19621225

FAQs

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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.

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Recombinant Human IFN alpha2a Protein

Recombinant Human IFN alpha2a Protein

Product Overview

Target Details

FAQs