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Humoral Immunity and Accute Phase Proteins

K271            K275            K277            K276            K272   

K274            K278            K279K          K279L           K250

K271 Total IgG EIA

Immunoglobulin G (IgG) is the main part of serum γ – globulin fraction. IgG is secreted during secondary immune response and plays a key role in humoral immunity. Decrease of serum IgG concentration below 5 g/l is a marker of severe life-threatening immunodeficiency. Determination of serum IgG concentration and IgG/IgA/IgM ratios can be used for monitoring of humoral immune status. Marked elevation of serum IgG may be observed in chronic inflammation, autoimmune diseases and myeloma.
 

Sample type: Serum, plasma, urine,                     Sensitivity: 0.12 g/l                     Control sample: 1
                   saliva, cerebrospinal fluid                 Incubation: 30’/30’/15’, 370С        Shelf life: 12 months
Sample predilution: 1:50-1:200                            Calibrators: 5 (0-25 g/l)               Normal range, g/l: - serum 9.0-20.0
Sample volume: 5-100 μl                                                                                                          

 

K275 Total IgA EIA

Immunoglobulin A (IgA) is a main factor of mucosal immune response to bacteria and viruses. Selective IgA deficiency is one of the most frequent hereditary disorders causing chronic infections, inflammation in gastrointestinal, urinary and respiratory systems. Determination of IgA concentration in serum and other biological fluids can be used as screening for selective IgA deficiency and other immunodeficiency syndromes. Marked elevation of serum IgA is observed in some autoimmune diseases and IgA myeloma.

Sample type: Serum, plasma, urine,                     Sensitivity: 0.12 g/l                     Control sample: 1
                    saliva, cerebrospinal fluid                Incubation: 30’/30’/15’, 370С        Shelf life: 12 months
Sample predilution: 1:100-1:200                          Calibrators: 5 (0-5 g/l)                 Normal range, g/l: - serum 0.9-3.1
Sample volume: 5-50 μl                                                                                                         

 

K277 Total IgM EIA

Immunoglobulin M (IgM) is secreted during primary immune response and exists in monomeric and pentameric forms. Elevated serum IgM is observed in chronic inflammation, macroglobulinemia and IgM myeloma. Decreased IgM level may occur in some immunodeficiency syndromes.

 
Sample type: Serum, plasma, urine,                     Sensitivity: 0.25 g/l                     Control sample: 1
                   saliva, cerebrospinal fluid                 Incubation: 30’/30’/15’, 370С        Shelf life: 12 months
Sample predilution: 1:200                                   Calibrators: 5 (0-10 g/l)               Normal range, g/l: - serum 0.7-3.7
Sample volume: 5-50 μl                                                                                                        

K276 Secretory IgA EIA (in saliva)

Secretory IgA (sIgA) is the main immunoglobulin present on mucosal surfaces. Ca. 90% of sIgA is produced locally and does not penetrate into blood circulation. sIgA is considerably different from serum IgA, as this complex protein consists of 3 completely different molecules. Two or four molecules of immunoglobulin A with molecular weight 160 kDa are joined by J-chain (16 kDa) and attached to the secretory component (80kDa); the formation of this complex occurs during transepithelial transport of polymeric IgA. sIgA plays a pivotal role in local immunity by blocking bacterial and viral adhesion and invasion through epithelial tissues. Determination of sIgA concentration allows to evaluate the local immunity status in stomatology, ophthalmology, respiratory diseases, gastroenterology, gynaecology. The sIgA in saliva can be also used as noninvasive mass screening for selective IgA deficiency. Elevation of sIgA in serum is occasionally observed in some autoimmune diseases and several tumors.

 
Sample type: Saliva, serum, urine etc.                  Sensitivity: 0.5 μg/ml                  Control sample: 1
Sample predilution: 1:50-1:200                            Incubation: 90’/30’/15’, 370С        Shelf life: 12 months
Sample volume: 5-100 μl                                    Calibrators: 6 (0-400 μg/ml)          Normal range, g/l:- serum 1.6-3.8
                                                                                                                                                - saliva 57-260
                                                                                                                                                - urine 0.5-2.7
 

K272 IgG2 EIA

 IgG2 subclass plays a pivotal role in immune response to polysaccharide antigens of incapsulated bacteries. Selective IgG2 deficiency is characterized by low or absent serum IgG2 and may lead to higher probability of infections caused by Meningococcus, Pneumococcus, Haemophilus and related pathogens. In this case the risk of chronical infectious diseases of respiratory system is increased. Low serum IgG2 is also observed in common variable immunodeficiency (CVID). IgG2 serum content comprises 20% of total serum IgG. Serum IgG2 determination may be used for monitoring of humoral immune status. 

Sample type: Serum                         Sensitivity: 0.12 g/l                         Control sample: 1
Sample predilution: 1:5000                Incubation: 30’/30’/15’, 370С            Shelf life: 12 months
Sample volume: 100 μl                     Calibrators: 6 (0-15 g/l)                    Normal range, g/l: 1.0-7.5

 

K274 IgG4 EIA

IgG4 subclass represents ca. 3% of total serum IgG.
IgG4-antibodies are developed after long term antigen stimulation, eg in chronic fungal infections,
parasitic invasions and autoimmunity.
IgG4 plays a special role in atopic allergy. Elevated serum total and venom specific IgG4 is observed
in honey bee keepers. The development of IgG4 response is suggested to correlate with successful
treatment of allergy patients by modified allergens (immunotherapy). Serum IgG4 is also elevated
in atopic diseases (atopic asthma, atopic dermatitis) even in the patients showing normal serum IgE.
IgG4 deficiency is frequently associated with IgG2 deficiency and lead to decreased immune response
to bacterial antigens.

Sample type: Serum                         Sensitivity: 0.03 g/l                         Control sample: 1
Sample predilution: 1:5000                Incubation: 30’/30’/15’, 370С            Shelf life: 12 months
Sample volume: 5 μl                         Calibrators: 5 (0-2.5 g/l)                  Normal range, g/l: 0.1 – 1.2

K278 IgD EIA                                                                                                         New kit!

Immunoglobulin D (IgD) was first described in 1905. IgD is localized on membranes of B-lymphocyres
and, similarly to membrane IgM, serves as a receptor to various antigens.
IgD function is not completely clear yet. IgD deficiency occurs rather frequently – in some populations,
its prevalence comes to 10%. Nevertheless, selective IgD deficiency is not associated with any clinical
pathology. Elevated IgD level is characteristic for the hyper-IgD-syndrome which is associated with
intermittent fever of unknown etiology and arthropathy. Besides, elevated serum IgD was also found
in IgD myeloma (in this case, it is usually accompanied by a marked proteinuria and Bence-Jones
protein in urine), in chronic infections (tuberculosis, lepra, aspergillosis, AIDS), and in patients with
rheumatoid arthritis, lymphogranulematosis, liver cirrhosis and diabetes. A slightly elevated serum IgD
was also seen in pregnancy and in smokers.

Sample type: Serum                         Sensitivity: 7.5 μg/ml                      Control sample: 1
Sample predilution: 1:101                 Incubation: 60’/60’/15’, 370С            Shelf life: 12 months
Sample volume: 20 μl                       Calibrators: 5 (0-360 μg/ml)             Normal range, μg/ml: < 150
 

K279K Ig K (free kappa light chains) EIA                                                                    New kit!

Along with native immunoglobulin molecules consisting of two heavy and two light chains, free kappa
and lambda light chains are also found in blood, spinal fluid and urine. Normally, free light chains in small
quantities are produced by B-cells and generated by proteolytic cleavage of immunoglobulins. Recently,
some evidence was reported regarding proteolytic and anti-angiogenic activity of free light chains,
as well as their ability to specifically interact with mast cells to induce hypersensitivity reactions.
Markedly elevated levels of free light chains are found in patients with multiple sclerosis, myeloma,
rheumatoid arthritis, systemic lupus erythematosus, acute nephritis.
As half-life period of free light chains is much less than that of native immunoglobulin molecules,
determination of free light chains concentration is recommended to estimate effectiveness of treatment
of myeloma, amiloidosis and other relevant pathology.

Sample type: Serum, plasma, urine,         Sensitivity: 1.0 μg/ml                  Control sample: 1
                   cerebrospinal fluid               Incubation: 30’/30’/15’, 370С       Shelf life: 12 months
Sample predilution: 1:101                       Calibrators: 6 (0-150 μg/ml)         Normal range, μg/ml: 6 – 13
Sample volume: 10-100 μl

K279L Ig L (free lambda light chains) EIA                                                                   New kit!

Along with native immunoglobulin molecules consisting of two heavy and two light chains, free kappa
and lambda light chains are also found in blood, spinal fluid and urine. Normally, free light chains in small
quantities are produced by B-cells and generated by proteolytic cleavage of immunoglobulins. Recently,
some evidence was reported regarding proteolytic and anti-angiogenic activity of free light chains,
as well as their ability to specifically interact with mast cells to induce hypersensitivity reactions.
Markedly elevated levels of free light chains are found in patients with multiple sclerosis, myeloma,
rheumatoid arthritis, systemic lupus erythematosus, acute nephritis.
As half-life period of free light chains is much less than that of native immunoglobulin molecules,
determination of free light chains concentration is recommended to estimate effectiveness of treatment
of myeloma, amiloidosis and other relevant pathology.

Sample type: Serum, plasma, urine,     Sensitivity: 1.0 μg/ml                      Control sample: 1
                   cerebrospinal fluid          Incubation: 30’/30’/15’, 370С            Shelf life: 12 months
Sample predilution: 1:101                   Calibrators: 6 (0-15 μg/ml)               Normal range, μg/ml: 0.2 – 1.3
Sample volume: 10-100 μl

K250 CRP ultra EIA

С–reactive protein (CRP) is a pentamerous protein with a MM ca. 100 kDa. CRP is one of the most
ancient factors of humoral immunity. CRP has high affinity to a number of internal antigens –
phosphoethanolamine, phosphorilcholine, histones, fibronectin, laminine and poly-cationic compounds.
CRP may bind to cell wall polysaccarides of streptococci and staphylococci, takes part in plasma clearance
from apoptotic and necrotic detrite by promoting their phagocytosis. CRP may activate classical
complement cascade and stimulate phagocytic activity of macrophages. A sharp rise (up to 1000-
fold) of circulating CRP level is a sensitive but not specific marker of acute inflammation induced by
interleukin 6. Recently it has been found that a long-term elevation of plasma CRP level (3–10 mg/l) is
associated with a high risk of coronary disease. Elevated basal plasma CRP level is found in menopausal
women treated by replacing hormonal therapy as well as in smokers.

Sample type: serum, plasma                 Sensitivity: 0.2 mg/l                      Control sample: 1
Sample predilution: 1:101                     Incubation: 30’/30’/15’, 370С          Shelf life: 12 months
Sample volume: 25 μl                           Calibrators: 6 (0-25 mg/l)              Normal range, mg/l: 0-5.0

 

Copyright © 2002 GENTAUR Molecular Products
Last modified: 05/29/09