Journal of Immunological Methods (J IMMUNOL METHODS)

Publisher: Association of Medical Laboratory Immunologists, Elsevier

Journal description

The Journal of Immunological Methods is devoted to covering techniques for: (1) Quantitating and detecting antibodies and/or antigens and haptens based on antigen-antibody interactions. (2) Fractionating and purifying immunoglobulins, lymphokines and other molecules of the immune system. (3) Isolating antigens and other substances important in immunological processes. (4) Labelling antigens and antibodies with radioactive and other markers. (5) Localizing antigens and/or antibodies in tissues and cells, in vivo or in vitro. (6) Detecting, enumerating and fractionating immunocompetent cells. (7) Assaying for cellular immunity. (8) Detecting cell-surface antigens by cell-cell interactions. (9) Initiating immunity and unresponsiveness. (10) Transplanting tissues. (11) Studying items closely related to immunity such as complement, reticuloendothelial system and others. In addition the journal will publish articles on novel methods for analysing the organization, structure and expression of genes for immunologically important molecules such as immunoglobulins, T cell receptors and accessory molecules involved in antigen recognition, processing and presentation. Submitted full length manuscripts should describe new methods of broad applicability to immunology and not simply the application of an established method to a particular substance - although papers describing such applications may be considered for publication as a short Technical Note The Recombinant Technology section will contain articles relating to modification by recombinant techniques of molecules of immunological interest; isolation of novel binding proteins by phage display; gene therapy; transfection; and expression. Immunology Protocols is a section providing detailed, step-by-step descriptions of new and established techniques in immunology. Articles on the molecular biological analysis of immunologically relevant receptor binding sites are also invited.

Current impact factor: 1.82

Impact Factor Rankings

2015 Impact Factor Available summer 2016
2014 Impact Factor 1.82
2013 Impact Factor 2.005
2012 Impact Factor 2.225
2011 Impact Factor 2.203
2010 Impact Factor 2.34
2009 Impact Factor 2.347
2008 Impact Factor 2.12
2007 Impact Factor 1.947
2006 Impact Factor 2.402
2005 Impact Factor 2.572
2004 Impact Factor 2.464
2003 Impact Factor 2.744
2002 Impact Factor 2.598
2001 Impact Factor 2.283
2000 Impact Factor 1.995
1999 Impact Factor 1.95
1998 Impact Factor 1.855
1997 Impact Factor 2.043
1996 Impact Factor 1.883
1995 Impact Factor 1.901
1994 Impact Factor 2.029
1993 Impact Factor 2.104
1992 Impact Factor 1.79

Impact factor over time

Impact factor

Additional details

5-year impact 2.25
Cited half-life >10.0
Immediacy index 0.56
Eigenfactor 0.01
Article influence 0.82
Website Journal of Immunological Methods website
Other titles Journal of immunological methods, Immunological methods, JIM
ISSN 0022-1759
OCLC 1783876
Material type Periodical, Internet resource
Document type Journal / Magazine / Newspaper, Internet Resource

Publisher details


  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author can archive a post-print version
  • Conditions
    • Authors pre-print on any website, including arXiv and RePEC
    • Author's post-print on author's personal website immediately
    • Author's post-print on open access repository after an embargo period of between 12 months and 48 months
    • Permitted deposit due to Funding Body, Institutional and Governmental policy or mandate, may be required to comply with embargo periods of 12 months to 48 months
    • Author's post-print may be used to update arXiv and RepEC
    • Publisher's version/PDF cannot be used
    • Must link to publisher version with DOI
    • Author's post-print must be released with a Creative Commons Attribution Non-Commercial No Derivatives License
    • Publisher last reviewed on 03/06/2015
  • Classification
    ​ green

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: Severely immunodeficient mice such as the NOD/SCID/IL2rγ(null) (NSG) strain can be engrafted with human hematopoietic stem cells (HSCs), resulting in chimeric mice containing many components of the human immune system (Human Immune System mice or HIS mice). HIS mice can both support the replication of and recapitulate much of the immunological response to a variety of pathogens, including ones with strict human tropism, such as HIV-1. In an effort to develop a better mouse model for human infectious pathogen infection and possible immune resolution, we compared the human immune system reconstitution of NSG mice following injection with human CD34+ HSCs purified from either fetal liver (FL) or umbilical cord blood (UCB). We analyzed reconstitution in standard NSG mice as well as a derivative of these mice containing an HLA.A2 encoding transgene (NSG.A2). HSCs from both sources effectively reconstituted hematopoietic lineages when injected into NSG mice. In marked contrast, total CD45(+) human hematopoietic cells in NSG.A2 mice were well reconstituted by HSCs from UCB but very poorly by HSCs purified from FL. Moreover, the reconstitution of T cell lineages in NSG.A2 mice by HSCs from UCB was inferior to that obtained using NSG mice. We also found that FL CD34(+) HSCs contain a much higher percentage of cells with a phenotype consistent with primitive progenitors than UCB HSCs. We discuss possible explanations for the influence of the HLA.A2 transgene on hematopoietic reconstitution using the two sources of HSCs. Copyright © 2015. Published by Elsevier B.V.
    Journal of Immunological Methods 03/2015; 422. DOI:10.1016/j.jim.2015.02.007
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    ABSTRACT: A rabbit monoclonal antibody (Abcam ab124797), with high affinity for a synthetic peptide corresponding to the C-terminal region of the receptor activator of nuclear factor (NF)-κB ligand (RANKL), specifically recognizes a 37 kDa protein by immunoblotting, in good agreement with the molecular mass of RANKL. However, our mass spectroscopy analysis revealed that the protein recognized by the antibody is the α-subunit of NAD(+)-dependent isocitrate dehydrogenase (ICDH), a key Krebs cycle enzyme in mitochondria. Consistently, immunocytochemical staining with the antibody revealed a network organization characteristic of mitochondria, which overlapped with staining by MitoTracker and was lost after the siRNA-mediated downregulation of ICDH. The C-terminal peptide of ICDH contains similar chemical characteristics to that of the RANKL peptide and interacts with the antibody, although the affinity is a hundred times weaker. The present study provides an example of the preferential recognition of a surrogate protein by a rabbit monoclonal antibody. Copyright © 2015. Published by Elsevier B.V.
    Journal of Immunological Methods 03/2015; 420. DOI:10.1016/j.jim.2015.03.006
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    ABSTRACT: The study aimed to evaluate cell surface mobilisation of CD107a as a general activation marker on chicken cytotoxic T cells (CTL). Experiments comprised establishment of an in vitro model for activation induced CD107a mobilisation and design of a marker panel for detection of CD107a mobilisation on chicken CTL isolated from different tissues. Moreover, CD107a mobilisation was analysed on CTL isolated from airways of infectious bronchitis virus (IBV) infected birds direct ex vivo and upon in vitro stimulation. Results showed that phorbol 12-myristate 13-acetate (PMA) in combination with ionomycin was a consistent inducer of CD107a cell surface mobilisation on chicken CTL in a 4h cell culture model. In chickens experimentally infected with IBV, a higher frequency of CTL isolated from respiratory tissues were positive for CD107a on the cell surface compared to those from uninfected control chickens indicating in vivo activation. Moreover, upon in vitro PMA+ionomycin stimulation higher proportions of CTL isolated from the airways of IBV infected chickens showed CD107a mobilisation compared to those from uninfected control chickens. Monitoring of CD107a cell surface mobilisation may thus be a useful tool for studies of chicken CTL cytolytic potential both in vivo and in vitro. Copyright © 2015. Published by Elsevier B.V.
    Journal of Immunological Methods 03/2015; 419(1). DOI:10.1016/j.jim.2015.02.011
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    ABSTRACT: Bioanalytical data from early human studies conducted in normal volunteers are often used for building pharmacokinetic/pharmacodynamic models that can predict outcomes of future studies in diseased patients. Thus, it's important to develop and validate reliable and accurate bioanalytical assays that instill confidence that the intended therapeutic species (total or free) are being measured. Assays quantifying the free therapeutic species, the partially bound (for multivalent therapeutics) and unbound species, require much more characterization than assays that quantify the total therapeutic species. We have developed an immunoassay to measure free BMS-962476, an Adnectin protein therapeutic against soluble proprotein convertase subtilisin kexin (PCSK)-9, and performed an in-depth characterization of the accuracy of this assay with the assistance of modeling. The experimental data correlates with modeled data within 15% at all clinically relevant levels of PCSK9 in normal and diseased populations. Copyright © 2015. Published by Elsevier B.V.
    Journal of Immunological Methods 02/2015; 419(1). DOI:10.1016/j.jim.2015.02.009
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    ABSTRACT: Citrobacter rodentium is a natural mouse pathogen which reproducibly infects mice and causes intestinal disease. The C. rodentium model of infection is very useful for investigating host-pathogen immune interactions in the gut, and can also be used to understand the pathogenesis of several important human intestinal disorders, including Crohn's disease, ulcerative colitis, dysbiosis and colon tumorigenesis. Both innate and adaptive immune responses play a critical role in protection against C. rodentium. Here, we summarize the role of immune components in protection against C. rodentium and describe techniques for the analysis of innate and adaptive mucosal immune responses, including setting up the infection, analysis of colonic hyperplasia and bacterial dissemination, evaluation of antibody responses, and purification and analysis of intestinal epithelial and lymphoid cells. Copyright © 2015. Published by Elsevier B.V.
    Journal of Immunological Methods 02/2015; 421. DOI:10.1016/j.jim.2015.02.003
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    ABSTRACT: Immunoconjugates that deliver cytotoxic payloads to cancer cells represent a promising class of therapeutic agents which are intensively investigated in various clinical applications. Prerequisites for the generation of effective immunoconjugates are antibodies which efficiently deliver the respective cytotoxic payload. To facilitate the selection of human or mouse antibodies that display favorable characteristics as immunotoxins, we developed a novel Pseudomonas exotoxin A (ETA)-based screening protein. The α-Fc-ETA' consists of a multispecies-specific Fc-binding domain antibody genetically fused to a truncated ETA version (ETA'). α-Fc-ETA' non-covalently bound to human and mouse antibodies but did not form immune complexes with bovine immunoglobulins. In combination with antibodies harboring human or mouse Fc domains α-Fc-ETA' inhibited proliferation of antigen-expressing tumor cells. The cytotoxic effects were strictly antibody dependent and were observed with low α-Fc-ETA' concentrations. Mouse antibodies directed against CD7 and CD317/HM1.24 that previously had been used for the generation of functional recombinant immunotoxins, also showed activity in combination with α-Fc-ETA' by inhibiting growth of antigen-positive myeloma and leukemia cell lines. In contrast, α-kappa-ETA', a similarly designed human kappa light chain-specific fusion protein, was only specifically active in combination with antibodies containing a human kappa light chain. Thus, the novel α-Fc-ETA' fusion protein is broadly applicable in screening antibodies and Fc-containing antibody derivatives from different species to select for candidates with favorable characteristics for immunotoxin development. Copyright © 2015. Published by Elsevier B.V.
    Journal of Immunological Methods 02/2015; DOI:10.1016/j.jim.2015.02.002
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    ABSTRACT: Specimen collection method and quality insurance is pivotal in biomarker discovery. Pre-analytical variables concerning blood collection and sample handling might affect analytical results and should be standardised prior application. In this study, we examine pre-analytical characteristics of blood samples using protein microarray. The influences of 1) standby times until centrifugation (1h, 4h, 24h and 48h), 2) four blood collection methods, and 3) IgG purified from those samples on differentially reactive antigens between samples ("DIRAGs") were investigated. Spearman correlation analyses of intra-individual arrays demonstrated remarkable differences (0.75-0.98 vs. 0.5-0.75) of antibody reactivities within and between serum and plasma samples. Class comparison showed that reactive antigen profiles were best preserved using IgG purified samples of serum tubes without separation gel as after 24hours 83% of the 1h baseline DIRAGs were re-found. Testing dilution series with protein microarrays and Luminex xMap® Technology, we found linear correlations (R(2)=0.94-0.99) between IgG concentration and read-out when using purified IgG instead of serum. Therefore, we highly recommend standardising pre-analytics and proposing the use of purified IgG for autoantibody immune-profiling with protein microarrays to reduce potential unspecific binding of matrix proteins abundant in serum and plasma samples. Although purified IgG cannot completely compensate the influence of pre-analytics, in highly parallel immune-profiling IgG enables reduction of unspecific effects, which occur when using serum or plasma for analysis on protein microarrays. Reproducibility problems due to pre-analytical processing of blood samples might explain discrepant results reported in various biomarker studies. Copyright © 2015 Elsevier B.V. All rights reserved.
    Journal of Immunological Methods 02/2015; 418. DOI:10.1016/j.jim.2015.01.009
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    ABSTRACT: Isolation and characterization of anti HIV-1 broadly neutralizing antibodies (bNAbs) has elucidated new epitopes and sites of viral vulnerability. Anti-HIV-1 bNAbs typically show high levels of somatic mutations in their variable region genes. This feature potentially limits antibody identification, since the mutated antibody sequences are no longer complimentary to primers designed based on germline antibody sequences. Here we report a new set of primers for Igλ light chains that aligns to the 5' end of the leader sequence and is highly efficient for the amplification of antibodies that contain mutations and deletions in the 5' end of human Igλ. Copyright © 2015 Elsevier B.V. All rights reserved.
    Journal of Immunological Methods 02/2015; 418. DOI:10.1016/j.jim.2015.01.011
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    ABSTRACT: Soluble Glycoprotein VI (GPVI) is an attractive marker for disorders marked by platelet activation, such as thrombotic microangiopathy, myocardial infarction, and stroke. Several groups have already developed an immunoassay for soluble GPVI; however, there are several discrepancies between the groups' assays. In this study, we prepared the two types of recombinant soluble GPVI, the monomeric form GPVI (GPVI-His) and the dimeric form of GPVI (GPVI-Fc), moreover, we generated four anti-GPVI antibodies, F1232-7-1 (7S1), F1232-10-2 (10S2), F1232-19-1 (19D1), and F1232-21-1 (21D1). The former 2 antibodies (7S1 and 10S2) had a high affinity for both GPVI-His and GPVI-Fc, while the latter 2 antibodies (19D1 and 21D1) showed a high affinity for GPVI-Fc but low affinity for GPVI-His. All of the antibodies comparably recognized surface GPVI on resting platelets. Furthermore, we established two immunoassays for soluble GPVI, 7S1/10S2-HRP and 19D1/21D1-HRP (capture antibody/detection antibody). 7S1/10S2-HRP showed equivalent reactivity with GPVI-His and GPVI-Fc, whereas 19D1/21D1-HRP had high affinity for GPVI-Fc but low reactivity with GPVI-His. In terms of reactivity with platelet-derived soluble GPVI, 7S1/10S2-HRP demonstrated sensitive detection whereas 19D1/21D1-HRP was nonreactive. Taken together, 7S1/10S2-HRP is a suitable candidate for a reliable soluble GPVI immunoassay as it has a high affinity for monomeric GPVI.
    Journal of Immunological Methods 02/2015; 418. DOI:10.1016/j.jim.2015.01.010