Recombinant Human Interferon Alpha-1/13 (IFNA1), Active

Name: Recombinant Human Interferon Alpha-1/13 (IFNA1), Active
Brand: Beta LifeScience
SKU: BLC-06070P
Price: 744.8 USD
Availability: InStock

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Cytokines, Cytokines and growth factors, Interferons and receptors (ifn), Recombinant proteins

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Product Overview

Description	Recombinant Human Interferon Alpha-1/13 (IFNA1), Active is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 97% 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 specific activity determined by an anti-viral assay is no less than 1.0x10 8 IU/mg.
Uniprotkb	P01562
Target Symbol	IFNA1
Synonyms	IFN-alpha-1/13, LeIF D
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	Tag-Free
Complete Sequence	M+CDLPETHSL DNRRTLMLLA QMSRISPSSC LMDRHDFGFP QEEFDGNQFQ KAPAISVLHE LIQQIFNLFT TKDSSAAWDE DLLDKFCTEL YQQLNDLEAC VMQEERVGET PLMNADSILA VKKYFRRITL YLTEKKYSPC AWEVVRAEIM RSLSLSTNLQ ERLRRKE
Expression Range	24-189aa
Protein Length	Full Length of Mature Protein
Mol. Weight	19.5 kDa
Research Area	Immunology
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 µm filtered PBS, pH 7.4, containing 3 Mannitol, 5 Trehalose, 0.05 Tween-80
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	Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
Subcellular Location	Secreted.
Protein Families	Alpha/beta interferon family
Database References	HGNC: 5417 OMIM: 147578 KEGG: hsa:3439 STRING: 9606.ENSP00000276927 UniGene: Hs.37026

Gene Functions References

SOCS2 impairs IFN/JAK/STAT signaling through reducing the stability of tyrosine kinase 2 (TYK2), downregulating the expression of type I and III IFN receptors, attenuating the phosphorylation and nucleus translocation of STAT1. PMID: 28496097
Significant associations were observed for 4 variants in IFNAR2, IFNLR1 with hepatitis B virus infection, and IFNLR1-rs4649203 was associated with hepatitis B recovery. Moreover, the authors demonstrated the clear relevance of 5 polymorphisms in IFNA1, IFNA2, IFNL4 with hepatocellular carcinoma. PMID: 29080269
HIV-1 IIIB infection of myeloid ThP-1 cells also reduced the IFN-alpha-mediated induction of the anti-viral gene, ISG15, but not MxA, revealing a functional consequence of this HIV-1-mediated immune evasion strategy. PMID: 29580840
Therefore, these results demonstrate the importance of MxB in alpha interferon-mediated inhibition of HIV-1 infection. PMID: 29925663
Our results illustrate a novel regulatory role of TWEAK, in which its activity positively regulates type I IFN pathway in lupus nephritis (LN) based on preclinical models. Our findings suggest TWEAK could act as a critical target in preventing renal damage in patients with LN. PMID: 29333443
Myeloid cells contribute more to the whole blood interferon signature in systemic lupus erythematosus than their lymphocytic counterpart. Very similar leukocyte subsets reveal distinctive IFN signatures. IFN alpha mixes up composition of blood and leads to a preferential neutropenia, yielding relative lymphocytosis. PMID: 28357476
the polymorphic variant of IFNA1 (-2) gene is associated with chronic HBV infection PMID: 27101083
Cerebrospinal fluid interferon alpha levels correlate with neurocognitive impairment in ambulatory HIV-Infected individuals. PMID: 27400930
Data suggest a central role of XBP1 in TLR7-induced IFNalpha production and identify XBP1 as a potential novel therapeutic target in IFNalpha-driven autoimmune and inflammatory diseases. PMID: 28408069
Study shows IFN-alpha rapidly induces a profound shift in whole brain network structure, impairing global functional connectivity and the efficiency of parallel information exchange. PMID: 26697999
The review focuses on the value of the type I and III interferon subtypes (alphas, beta and lambdas) as therapeutics for prevention and treatment of viral infections (influenza, herpes, human immunodeficiency virus and hepatitis viruses). PMID: 27544015
MiR-181a is an important mediator for interferons-induced SAMHD1 expression in astrocytes and microglia, but not for inhibition of HIV-1 infection induced by IFN-alpha. PMID: 27219130
the expression of certain TAM components was reduced as a result of prolonged degradation of MYD88 by Porphyromonas gingivalis infection. PMID: 28076786
Type I interferons (IFNs) signature is seen in a significant proportion of anti-nuclear antibody-positive (ANA(+) individuals and appears to be associated with ANA titre and type of autoantibodies, rather than with the presence or development of clinical systemic autoimmune rheumatic diseases (SARDs) symptoms. PMID: 28245862
study found that endogenous IFNalpha autocrinally promotes the expression of Interferon-Stimulated Gene (ISG) mRNAs in IL-3-, but not in IFNlambda3 plus IL-3-, treated plasmacytoid dendritic cells (pDCs); production of IFNalpha by IFNlambda3 plus IL-3-treated pDCs is mostly dependent on endogenously produced TNFalpha PMID: 27513213
results demonstrate that Sphingosine 1-phosphate lyase (SPL) is a host factor that augments type I IFN responses during influenza A virus infection; study delineates the relationship between IKKepsilon and SPL, which provides a mechanistic understanding of the pro-IFN activity of SPL PMID: 28600291
These data suggest that plasmacytoid dendritic cells producing IFN-alpha and IL-33 play a pivotal role in the chronic fibro-inflammatory responses underlying murine autoimmune pancreatitis and human IgG4-related autoimmune pancreatitis. PMID: 28373582
These findings also identify STAT3 as a therapeutic target against viral infection and highlight it as an essential pathway component for endogenous and therapeutic IFN-alpha responsiveness. PMID: 27988795
Mothers of children affected by autoimmune congenital heart block had a significantly higher expression IFN-alpha. PMID: 28501799
Suppression of the exogenous Type I IFN-induced Jak/STAT signaling by NSs might be one of the mechanisms of Severe fever with thrombocytopenia syndrome (SFTS) to evade host immune surveillance. PMID: 28234991
the paper shows the data on the role of interferons -alpha and -beta in infections - not only commonly known viral infections, but also bacterial, fungal and parasitic. PMID: 28388697
High Type I Interferon expression due to hypomethylation is associated with Systemic Lupus Erythematosus. PMID: 28085900
these studies identify phosphorylation of S734-STAT2 as a new regulatory mechanism that negatively controls the type I IFN-antiviral response. PMID: 27802159
The synthetic IFNP molecule exerted its antitumor activity by upregulating the downstream genes involved in the STAT1 pathway and in apoptosis. Using a cell receptor binding assay, we showed that this Jurkat-binding peptide facilitated the binding affinity of IFNalpha to the cell surface type I IFN receptor PMID: 28578326
KSHV-encoded viral IRF4 interacts with the host IRF7 and inhibits interferon-alpha production. PMID: 28342865
Data indicate ARID3a(+) B cells as a type of effector B cell, and link ARID3a expression in B lymphocytes to interferon alpha (IFNa)-associated inflammatory responses in systemic lupus erythematosus (SLE). PMID: 27522115
On one hand, hepatitis B virus activates MMP-9 in infected patients and leukocytes. On the other hand, MMP-9 facilitates hepatitis B virus replication through repressing IFN/JAK/STAT signaling, IFNAR1 function, and IFN-alpha action. PMID: 28122987
Interferon-alpha Induces the apoptosis of Hela cells by activating both the intrinsic mitochondrial pathway and endoplasmic reticulum stress-induced pathway. PMID: 27827850
Decreased interferon alpha (IFN-alpha) secretion induced by Toll-like receptor 7 and Toll-like receptor 8 (TLR7/TLR8) activation was observed in common variable immunodeficiency (CVID), which was recovered with Toll-like receptor 9 (TLR9) signaling. PMID: 27392462
Plasmacytoid dendritic cells (pDCs) and type 1 interferon (FNalpha/beta)frequently accompanied plasmablast/plasma cells (PB/PCs). PMID: 27102764
These results establish that activation of STAT pathway is essential for anti-hepatitis c virus efficacy of IFN-alpha. PMID: 27855377
IL-2 therapy should be used as a first- or second-line therapy following IFN-a therapy. IL-2 may have a lower response if it is used after molecular-targeted therapy or other treatments PMID: 27630356
results show that IFNA1 rs1332190 and IFNA17 rs9298814 SNPs may play an important role in Crimean-Congo hemorrhagic fever susceptibility PMID: 26694082
Interferon-alpha-induced TRIM22 interrupts hepatitis c virus replication by ubiquitinating NS5A. PMID: 25683609
our data indicate that by targeting PTP1B, miR-744 plays a feed-forward role in regulating type I IFN signaling pathway. PMID: 26259828
the findings demonstrate that treatment with anti-CD20-hIFNalpha reverses resistance of B-NHL PMID: 26398317
NS of severe fever with thrombocytopenia syndrome virus inhibited the activity of IFN-alpha1, IFN-beta, IFN-lambda1 and IFN-lambda2 through inhibition of STAT1 phosphorylation. PMID: 26353965
interferon (IFN)-alpha, weakens activation of the anti-bacterial interleukin (IL)-1/IL-22 axis in human peripheral blood mononuclear cells exposed to viable B. burgdorferi PMID: 26152778
Shp-2 contributes to the control of respiratory syncytial virus replication and progeny production in pulmonary alveolar epithelial cells by interfering with IFN-alpha-induced Jak/Stat1 pathway activation PMID: 26119280
Interferon alfa induces high response rates with low toxicity in patients with polycythemia vera. PMID: 26261238
This study suggests that suppression of miR-122 induced by hepatitis B virus infection, leads to the inactivation of interferon expression, which in turn enhances hepatitis B virus replication. PMID: 25766860
Data suggest that Viral microRNA hcmv-miR-UL112 subverts innate immunity by downregulating type I interferons IFN-alpha and IFN-beta signaling to inhibit natural killer (NK) cell cytotoxicity. PMID: 25530545
Interferon-alpha and interferon-beta are at the crossroads of allergy and viral infections. (Review) PMID: 26026068
The interaction between AIP and IRF7 is enhanced upon virus infection, and AIP potently inhibits IRF7-induced type I IFN (IFN-alpha/beta) production. PMID: 25911105
Interferon-alpha inhibits CD4 T cell responses to interleukin-7 and interleukin-2 and selectively interferes with Akt signaling. PMID: 25784743
Data show that chemokine CXCL13 production by monocytes required toll-like receptor 7 activation and secretion of interferon-alpha. PMID: 25667414
Studies indicate that type I interfereon signaling cascade is initiated by the binding of the cytokines to the high-affinity interferon alpha receotor. PMID: 25747907
Results show that histone-lysine N-methyltransferase Set7 facilitates hepatitis C virus (HCV) replication through the attenuation of interferon-alpha (IFN-alpha) signaling pathways and IFN-related effectors. PMID: 25681344
Domain 2 of the hepatitis C virus core protein critically affected the magnitude of host IFN-alpha responses. PMID: 25552725
Hepatitis C virus NS3-4A similarly diminished both human and mouse MAVS-dependent signaling in human and mouse cells and MAVS induces both type I and type III interferons, which together control the hepatitis C virus replication. PMID: 25609814

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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.