TEST
REF | DESCRIPTION | SAMPLES FOR GEL | TEST FOR KIT |
---|---|---|---|
SRE600K | KIT FOR SERUM PROTEINS AND CONCENTRATED URINES | 13 | 130 |
SRE601K | 26 | 260 | |
SRE636K | 39 | 390 | |
SRE602K | KIT FOR β1-β2 SERUM PROTEINS AND CONCENTRATED URINES | 13 | 130 |
SRE603K | 26 | 260 | |
SRE637K | 39 | 390 | |
SRE627K | KIT FOR ACID VIOLET IMMUNOFIXATION | 2 | 20 |
SRE628K | 4 | 40 | |
SRE639K | 6 | 60 | |
SRE623K | KIT FOR ACID BLUE IMMUNOFIXATION | 2 | 20 |
SRE624K | 4 | 40 | |
SRE643K | 6 | 60 | |
SRE629K | KIT FOR PENTAVALENT IMMUNOFIXATION KIT | 6 | 60 |
SRE630K | 12 | 120 | |
SRE625K | KIT FOR BENCE-JONES IMMUNOFIXATION | 2 | 20 |
SRE626K | 4 | 40 | |
SRE640K | 6 | 60 | |
SRE607K | KIT FOR HIGH RESOLUTION PROTEINS | 13 | 130 |
SRE604K | KIT FOR ALKALINE HAEMOGLOBINS | 13 | 130 |
SRE605K | KIT FOR ACID HAEMOGLOBINS | 13 | 130 |
SRE606K | KIT FOR LIPOPROTEINS | 13 | 130 |
SRE621K | 26 | 260 | |
SRE612K | KIT FOR LDH ISOENZYMES | 13 | 130 |
SRE610K | KIT FOR ALP ISOENZYMES | 13 | 130 |
SRE611K | KIT FOR CK ISOENZYMES | 13 | 130 |
SRE622K | KIT FOR CSF ISOELECTRIC FOCUSING | 6 | 60 |
CODE | DESCRIPTION | SAMPLES FOR GEL | TEST FOR KIT |
---|---|---|---|
SRE600K | KIT FOR SERUM PROTEINS AND CONCENTRATED URINES | 13 | 130 |
SRE601K | 26 | 260 | |
SRE636K | 39 | 390 |
Intended Use
The kits for Serum Protein Electrophoresis and concentrated urines are intended for the separation of proteins in human serum and concentrated urines by electrophoresis on agarose gel plates.
Human body fluids contain a varied mixture of proteins and protein complexes. Each of these protein entities fulfils a specific function within the life process. It is well known that the levels of various proteins in blood serum bear a close relationship to the state of health and disease. The concentration and compositions of the proteins more than one hundred contained in the serum may vary due to physiological and pathological conditions.
Among the laboratory methods available for the separation of proteins, electrophoresis is a well-established and versatile technique widely used in clinical chemistry. Serum Protein Electrophoresis (SPE) on agarose gel at alkaline pH, performed with these kits, yields five bands: albumin and four globulins called alpha 1 (α1), alpha 2 (α2), beta (β) and gamma (γ). Each globulin fraction contains different proteins. Evaluation of single bands by visual inspection and densitometry provides valuable diagnostic support offering a display of the major proteins involved in functional and pathological processes.
Serum protein electrophoresis is a rapid screening technique useful for the initial identification of monoclonal bands and it is often used to identify monoclonal gammopathies.
Electrophoresis of urinary proteins allows assessment of the type of renal damage according to the qualitative composition and the positions of the bands in the pattern. Comparison between the positions of the bands in the urine protein pattern with those in the serum proteins pattern, enclosed in the analysis as a reference, allows identification of glomerular, tubular and mixed proteinuria and proteinuria caused by presence of Bence-Jones proteins.
Electrophoresis separates serum proteins and concentrated urine proteins according to their specific mobility when subjected to an electric field. Each molecule has an electrical charge due to the presence of positive and negative charged groups. The net charge defines the electrophoretic migration characteristics of each protein species at a given pH. With the Interlab SPE procedure, proteins are separated at alkaline pH by zone electrophoresis on agarose gel plates. When the electrophoretic separation of the bands is complete, the agarose gel plate is denatured, stained with Acid Blue, destained and dried. The patterns are then scanned and densitometric results are shown together with the graph.
CODE | DESCRIPTION | SAMPLES FOR GEL | TEST FOR KIT |
---|---|---|---|
SRE602K | KIT FOR β1-β2 SERUM PROTEINS AND CONCENTRATED URINES | 13 | 130 |
SRE603K | 26 | 260 | |
SRE637K | 39 | 390 |
Intended Use
The kits for Serum Protein Electrophoresis and concentrated urines are intended for the separation of proteins in human serum and concentrated urines by electrophoresis on agarose gel plates. Human body fluids contain a varied mixture of proteins and protein complexes. Each of these protein entities fulfills a specific function within the life process. It is well known that the levels of various proteins in blood serum bear a close relationship to the state of health and disease. The concentration and compositions of the proteins more than one hundred contained in the serum may vary due to physiological and pathological conditions.
Among the laboratory methods available for the separation of proteins, electrophoresis is a well-established and versatile technique widely used in clinical chemistry. Serum Protein Electrophoresis (SPE) on agarose gel at alkaline pH, performed with these kits, yields six bands: albumin and five globulins called alpha 1(α1), alpha 2 (α2), beta1 (β1), beta2 (β2) and gamma (γ). Each globulin fraction contains different proteins. Evaluation of single bands by visual inspection provides valuable diagnostic support offering a display of the major proteins involved in functional and pathological processes.
Serum protein electrophoresis is a rapid screening technique useful for the initial identification of monoclonal bands and it is often used to identify monoclonal gammopathies.
Electrophoresis of urinary proteins allows assessment of the type of renal damage according to the qualitative composition and the positions of the bands in the pattern. Comparison between the positions of the bands in the urine protein pattern with those in the serum proteins pattern, enclosed in the analysis as a reference, allows identification of proteinuria of glomerular, tubular and mixed origin and proteinuria caused by the presence of Bence-Jones.
Electrophoresis separates serum proteins and concentrated urine proteins according to their specific mobility when subjected to an electric field. Every molecule has an electrical charge due to the presence of positive and negative charged groups. The net charge defines the electrophoretic migration characteristics of each protein species at a given pH. With the Interlab SPE procedure, proteins are separated at alkaline pH by zone electrophoresis on agarose gel plates. When the migration is complete, the gel plate is stained with Acid Blue to identify proteins. The gel plate is then destained to a clear background, dried and scanned to give a pattern graph and the densitometric values of the main fractions. When the electrophoretic separation of the bands is complete, the agarose gel plate is denatured, stained with Acid Blue, destained and dried. The patterns are then scanned and densitometric results are shown together with the graph.
CODE | DESCRIPTION | SAMPLES FOR GEL | TEST FOR KIT |
---|---|---|---|
SRE627K | KIT FOR ACID VIOLET IMMUNOFIXATION | 2 | 20 |
SRE628K | 4 | 40 | |
SRE639K | 6 | 60 |
Intended Use
The Immunofixation electrophoresis kits are intended to be used for qualitative immunological detection of monoclonal proteins in human serum. The Immunofixation technique is a useful diagnostic tool used as an aid in identifying monoclonal gammopathies.
Monoclonal proteins (paraproteins, M-proteins, monoclonal immunoglobulins) resulted in protein electrophoregram as abnormal bands, primarily located in gamma globulin and beta globulin fractions. When qualitative abnormalities that suggest a monoclonal immunoglobulin are observed the Immunofixation electrophoresis kits are used to confirm the presence of monoclonal bands and to identify the type of paraprotein.
Protein electrophoresis most often involves the separation of serum proteins by passing an electric current through an appropriate electrolytic solution and a solid support medium such as agarose.
The Immunofixation electrophoresis incorporates the use of specific antisera to heavy and light chains to precipitate immunoglobulins following electrophoresis and is a highly sensitive and specific method to detect and classify monoclonal immunoglobulins.
In immunofixation, electrophoresis of one specimen from a patient suspected of monoclonal gammopathy is performed using six separate lanes on the agarose gel plate. The major protein groups are separated by electrophoresis at alkaline pH. When migration is complete, one lane is treated with a fixative solution to fix all proteins in order to provide a reference pattern, the other lanes are overlaid with different polyclonal antibodies displaying different binding specificities to protein domains of human immunoglobulins: anti-γ (to detect γ heavy chain [Ig G]), anti-μ (to detect μ heavy chain [Ig M]), anti-α (to detect α heavy chain [Ig A]), anti-κ (to detect κ light chain), and anti-λ (to detect λ light chain). The interaction between antigen (the immunoglobulin in the sample) and the antisera antibody will result in the formation of an insoluble complex that produces a band of precipitate, provided that the proportion of antibodies and antigens is appropriate. The precipitation rate depends on temperature, pH and ionic strength of the solution. Then, the agarose gel is denaturated, washed (to remove any excess of proteins that have not precipitated), stained, destained and dried. The comparison of the positions of immunofixed bands and that of the suspected monoclonal band in the reference pattern allows assessment of the biochemical identity of the protein.
CODE | DESCRIPTION | SAMPLES FOR GEL | TEST FOR KIT |
---|---|---|---|
SRE623K | KIT FOR ACID BLUE IMMUNOFIXATION | 2 | 20 |
SRE624K | 4 | 40 | |
SRE643K | 6 | 60 |
Intended Use
The Immunofixation electrophoresis kits are intended to be used for qualitative immunological detection of monoclonal proteins in human serum. The Immunofixation technique is a useful diagnostic tool used as an aid in identifying monoclonal gammopathies.
Monoclonal proteins (paraproteins, M-proteins, monoclonal immunoglobulins) resulted in protein electropherogram as abnormal bands, primarily located in gamma globulin and beta globulin fractions. When qualitative abnormalities that suggest a monoclonal immunoglobulin are observed, the Immunofixation electrophoresis kits are used to confirm the presence of monoclonal bands and to identify the type of paraprotein.
Principle
Protein electrophoresis most often involves the separation of serum proteins by passing an electric current through an appropriate electrolytic solution and a solid support medium such as agarose.
The Immunofixation electrophoresis (IFE) incorporates the use of specific antisera to heavy and light chains to precipitate immunoglobulins following electrophoresis and is a highly sensitive and specific method to detect and classify monoclonal immunoglobulins.
In immunofixation, electrophoresis of one specimen from a patient suspected of monoclonal gammopathy is performed using six separate lanes on the agarose gel plate. The major protein groups are separated by electrophoresis at alkaline pH. When migration is complete, one lane is treated with a fixative solution to fix all proteins in order to provide a reference pattern, the other lanes are overlaid with different polyclonal antibodies displaying different binding specificities to protein domains of human immunoglobulins: anti-γ (to detect γ heavy chain [Ig G]), anti-μ (to detect μ heavy chain [Ig M]), anti-α (to detect α heavy chain [Ig A]), anti-κ (to detect κ light chain), and anti-λ (to detect λ light chain). The interaction between antigen (the immunoglobulin in the sample) and the antisera antibody will result in the formation of an insoluble complex that produces a band of precipitate, provided that the proportion of antibodies and antigens is appropriate. The precipitation rate depends on temperature, pH and ionic strength of the solution. Then, the agarose gel is denaturated, washed (to remove any excess of proteins that have not precipitated), stained, destained and dried. The comparison of the positions of immunofixed bands and that of the suspected monoclonal band in the reference pattern allows assessment of the biochemical identity of the protein.
CODE | DESCRIPTION | SAMPLES FOR GEL | TEST FOR KIT |
---|---|---|---|
SRE629K | KIT FOR PENTAVALENT IMMUNOFIXATION KIT | 6 | 60 |
SRE630K | 12 | 120 |
Intended Use
The Pentavalent Immunofixation electrophoresis kits are intended to be used for qualitative immunological detection of monoclonal proteins in human serum. The Immunofixation technique is a useful diagnostic tool used as an aid in identifying monoclonal gammopathies.
Monoclonal proteins (paraproteins, M-proteins, monoclonal immunoglobulins) resulted in protein electrophoregram as abnormal bands, primarily located in gamma globulin and beta globulin fractions. When qualitative abnormalities that suggest a monoclonal immunoglobulin are observed, the Pentavalent Immunofixation electrophoresis kits are used to confirm the presence of monoclonal bands and to identify monoclonal bands that could be hidden by regular serum proteins.
Protein electrophoresis most often involves the separation of serum proteins by passing an electric current through an appropriate electrolytic solution and a solid support medium such as agarose.
The Immunofixation electrophoresis (IFE) incorporates the use of specific antisera to heavy and light chains to precipitate immunoglobulins following electrophoresis and is a highly sensitive and specific method to detect and classify monoclonal immunoglobulins.
In immunofixation, electrophoresis of one specimen from a patient suspected of monoclonal gammopathy is performed using two separate lanes on the agarose gel plate. The major protein groups are separated by electrophoresis at alkaline pH. When migration is complete, one lane is treated with a fixative solution to fix all proteins in order to provide a reference pattern (ELP), the other lane is overlaid with pentavalent antibody displaying binding specificities to the following protein domains of human immunoglobulins: anti-γ (to detect γ heavy chain [Ig G]), anti-μ (to detect μ heavy chain [Ig M]), anti-α (to detect α heavy chain [Ig A]), anti-κ (to detect κ light chain bound and free), and anti-λ (to detect λ light chain bound and free). The interaction between antigen (the immunoglobulin in the sample) and the antisera antibody will result in the formation of an insoluble complex that produces a band of precipitate, provided that the proportion of antibodies and antigens is appropriate. The precipitation rate depends on temperature, pH and ionic strength of the solution. Then, the agarose gel is denaturated, washed (to remove any excess of proteins that have not precipitated), stained, destained and dried. The comparison of the positions of immunofixed bands and that of the suspected monoclonal band in the reference pattern allows assessment of the biochemical identity of the protein and confirms the actual presence or absence of monoclonal protein.
CODE | DESCRIPTION | SAMPLES FOR GEL | TEST FOR KIT |
---|---|---|---|
SRE625K | KIT FOR BENCE-JONES IMMUNOFIXATION | 2 | 20 |
SRE626K | 4 | 40 | |
SRE640K | 6 | 60 |
Intended Use
The Bence-Jones Immunofixation Electrophoresis kits are intended to be used for qualitative immunological identification of Bence-Jones proteins in human neat urines. The Immunofixation Bence-Jones technique is a useful diagnostic tool used as an aid in identifying monoclonal gammopathies and for the characterization of urinary proteinuria.
Urine is formed by plasma ultrafiltration through the glomerular capillary wall that works as a filter for plasma proteins depending on their molecular size, configuration and electrical charge. Only molecules with a molecular mass less than 50 kDa can pass through the glomerular barrier, but they are reabsorbed by the proximal tubule cells and digested by enzymes that convert them into amino acids which can passed back into the bloodstream.
The Bence-Jones proteins are free monoclonal light chains that can pass the glomerular barrier due to their low molecular mass. Once the mechanism of tubular reabsorption becomes saturated, this protein excess is excreted in urine. Immunoelectrophoretic techniques allow the characterization of the two pathognomonic features of light chains: monoclonality and absence of heavy chains. When qualitative abnormalities are observed in gamma globulin and beta globulin zones using Urine Electrophoresis, the Bence-Jones Immunofixation kits are used to identify the possible presence of Bence-Jones proteins.
The Interlab kits SRE625K, SRE626K and SRE640K for Bence-Jones Immunofixation have been designed for use in conjunction with:
- SCE280M: B-J Antisera and Fixative Kit
- SCE639M: Total Urine Profile Antisera and Fixative kit
Protein electrophoresis most often involves the separation of urine proteins by passing an electric current through an appropriate electrolytic solution and a solid support medium such as agarose.
The Bence-Jones Immunofixation electrophoresis incorporates the use of specific antisera to heavy and light chains to precipitate immunoglobulins following electrophoresis.
In immunofixation, electrophoresis of one specimen from a patient suspected of monoclonal gammopathy is performed using six separate lanes on the agarose gel plate. The major protein groups are separated by electrophoresis at alkaline pH. When migration is complete, one lane is treated with a fixative solution to fix all proteins in order to provide a reference pattern, the other lanes are overlaid with different polyclonal antibodies displaying different binding specificities to protein domains of human immunoglobulins.
About IFE BJ Kits SRE625K, SRE626K, SRE640K used in conjunction with SCE280M, the polyclonal antibodies overlaid are the following: anti-Trivalent (to detect γ, μ and α heavy chains [GAM]), anti-κ (to detect κ light chains free and bound [k tot]), anti-λ (to detect λ light chains free and bound [λ tot]), anti-κ free (to detect κ light chains free), and anti-λ free (to detect λ light chains free).
About IFE BJ Kits SRE625K, SRE626K, SRE640K used in conjunction with SCE639M, the polyclonal antibodies overlaid are the following: anti-Mid Low MW Proteins (to detect tubular proteins), anti-Mid High MW Proteins (to detect glomerular proteins), anti-Bivalent (to detect K and λ light chains free and bound), anti-k free chains (to detect κ light chains free), and anti-λ free (to detect λ light chains free).
The interaction between antigen (the immunoglobulin in the sample) and the antisera antibody will result in the formation of an insoluble complex that produces a band of precipitate, provided that the proportion of antibodies and antigens is appropriate. The precipitation rate depends on temperature, pH and ionic strength of the solution. Then, the agarose gel is denaturated, washed (to remove any excess of proteins that have not precipitated), stained with Acid Violet, destained and dried.The comparison of the positions of immunofixed bands and that of the suspected monoclonal band in the reference pattern allows assessment of the biochemical identity of the protein, either complete immunoglobulin and/or free light chains.
CODE | DESCRIPTION | SAMPLES FOR GEL | TEST FOR KIT |
---|---|---|---|
SRE607K | KIT FOR HIGH RESOLUTION PROTEINS | 13 | 130 |
Intended Use
The High Resolution Proteins Electrophoresis kit is intended for the separation of proteins in human serum and urine by electrophoresis on agarose gel plates. Proteins are resolved into discrete bands to give an electrophoretic pattern that is examined visually for the detection of abnormal profiles, including both qualitative variations of the bands and appearance of additional bands.
The high-resolution technique applied to the analysis of proteins in serum, allows to further improve the separation of those protein components for whom a more in-depth study is required.
The characterization of the alpha 2 macroglobulin, that is the anodic component of the alpha 2, the characterization of the transferrin variants and the detection of the oligoclonal bands of very low concentration are some examples of the application of this analysis method on serum.
Urinary proteins are derived primarily from plasma proteins that filter through the kidney. Normally, a sieving system exists that prevents efficiently the passage of large molecular mass proteins through the glomerulus, namely the basic filtration unit in the kidney. Proteins of low molecular weight can pass freely and most of them are reabsorbed in the tubulus.
The appearance of increased protein concentration in urine, also called proteinuria, or the appearance of abnormal plasma proteins in the electrophoretic pattern of the urine is very important for the evaluation of renal function or for identification of other pathological conditions. Proteinuria is often associated with poor tubular reabsorption, but most frequently results from problems associated with the impaired permeability of the glomerulus.
Electrophoresis of urine on agarose gel is an effective method to detect abnormal proteins in urines. Normal and abnormal bands in urine are identified by comparing their position to that of the bands of a serum protein pattern, used as a reference.
Electrophoresis separates proteins according to their specific mobility when subjected to an electric field. Every molecule has an electrical charge due to the presence of positively and negatively charged groups. The net charge defines the electrophoretic migration characteristics of each protein species at a given pH. With the Interlab H. R. procedure, proteins are separated at alkaline pH by zone electrophoresis on agarose gel plates. When the electrophoretic separation of the bands is complete, the agarose gel plate is denaturated, stained with Acid Violet, destained and dried. Visual inspection of the patterns is performed to detect, as in the case of urine analysis, the presence of proteins of glomerular, tubular, or mixed origin and monoclonal bands, including intact immunoglobulins and free light chains.
CODE | DESCRIPTION | SAMPLES FOR GEL | TEST FOR KIT |
---|---|---|---|
SRE604K | KIT FOR ALKALINE HAEMOGLOBINS | 13 | 130 |
Intended Use
The Alkaline Hemoglobin Electrophoresis kit is intended for the qualitative and semiquantitative analysis of normal and abnormal hemoglobins using electrophoretic separation on agarose gel plates. The electrophoretic test is performed at alkaline pH and provides a valuable screening method for hemoglobin patterns. Densitometry of the pattern allows the relative quantification of hemoglobin bands.
Hemoglobin (Hb) is a protein found in red blood cells that plays a key role as a carrier for oxygen that is bound in the lungs and delivered to organs and tissues to maintain cell viability.
The molecule of hemoglobin is a tetramer that contains two different types of proteins called globins that are assembled in pairs. Alpha type globin is always present in the normal hemoglobin; the other type of globin (named β, δ, γ etc.) defines different hemoglobin molecules and determine their biological function. In each globin chain a small heme group is included that contains an iron (Fe) atom.
In the red blood cells of a normal adult three different types of hemoglobin are present. HbA is the predominant type with small amounts of HbA2 and HbF.
Mutations in the genes involved in hemoglobin synthesis cause the production of variant hemoglobins, with qualitative variations in their molecular structure, that may eventually cause pathological conditions that are grouped as hemoglobinopathies.
The variant hemoglobins most found are HbS and HbC. Other variants like Hb Lepore, HbE, HbG-Philadelphia, HbD-Los Angeles, and HbO-Arab can be detected. Decreased or modified rate of synthesis of one of the hemoglobin chains leads to quantitative variations of hemoglobin blood concentration, causing diseases called thalassemias.
About a quarter of the six hundred human hemoglobin variants currently identified have a net charge on the protein that allows them to be separated by electrophoresis on agarose gel at alkaline pH.
Normal hemoglobins and most variants have different electrophoretic mobility and can be resolved according to their net charge by electrophoresis on agarose gel plate in an alkaline buffer. When the electrophoretic separation of the bands is complete, the agarose gel plate is denaturated, stained with Acid Blue, destained and dried. The patterns are then scanned and the densitometric results are shown together with the graph.
CODE | DESCRIPTION | SAMPLES FOR GEL | TEST FOR KIT |
---|---|---|---|
SRE605K | KIT FOR ACID HAEMOGLOBINS | 13 | 130 |
Intended Use
The Acid Hemoglobin Electrophoresis kit is a qualitative analysis for the identification of both normal and abnormal hemoglobins, using electrophoretic separation on agarose gel plates. The electrophoretic test is carried out at an acidic pH and is based on the effect of the interactions between the agarose and the hemoglobin molecules.
Hemoglobin (Hb) is a protein found in red blood cells that plays a key role as a carrier for oxygen that is bound in the lungs and delivered to organs and tissues to maintain cell viability.
The molecule of hemoglobin is a tetramer that contains two different types of proteins called globins that are assembled in pairs. Alpha type globin is always present in the normal hemoglobin; the other type of globin (named β, δ, γ etc.) defines different hemoglobin molecules and determine their biological function. In each globin chain a small heme group is included that contains an iron (Fe) atom.
In the red blood cells of a normal adult three different types of hemoglobin are present. HbA is the predominant type with small amounts of HbA2 and HbF.
Mutations in the genes involved in hemoglobin synthesis cause the production of variant hemoglobins, with qualitative variations in their molecular structure, that may eventually cause pathological conditions that are grouped as hemoglobinopathies.
Over six hundred structural hemoglobin variants are known, whose identity can be demonstrated by electrophoretic methods (e.g. HbS, HbC, HbE, HbD, HbG, HbH, HbI, Hb Lepore).
The screening of hemoglobin patterns is generally performed by electrophoresis at alkaline pH. Variant hemoglobins often occupy positions in the pattern that are clearly distinct from normal ones, making their identification very easy. Sometimes the occurrence of overlapping of variant hemoglobins with normal fractions poses the problem to assess if an increased band concentration is due to a true increased normal fraction, or to the presence of an abnormal hemoglobin.
Electrophoresis on agarose gel at acid pH provides a method to identify abnormal hemoglobins that are not resolved by alkaline pH electrophoresis.
Hemoglobin electrophoresis at acidic pH is intended as a confirmatory test only and cannot substitute the method at alkaline pH for the evaluation of hemoglobin profiles.
Normal hemoglobins and most variants have different electrophoretic mobility and can be resolved according to their net charge by electrophoresis on agarose gel in acid buffer. This method allows separation of those variant hemoglobins that overlap in the alkaline electrophoretic pattern.
When the electrophoretic separation of the bands is complete, the agarose gel plate is denaturated, stained with Acid Blue, destained and dried. Visual inspection of the patterns is performed to detect both normal and abnormal or variant hemoglobins.
CODE | DESCRIPTION | SAMPLES FOR GEL | TEST FOR KIT |
---|---|---|---|
SRE606K | KIT FOR LIPOPROTEINS | 13 | 130 |
SRE621K | 26 | 260 |
Intended Use
The SRE606K and SRE621K Lipoprotein Electrophoresis Kits are used for the separation of human serum lipoproteins by electrophoresis on agarose gel plates. The tracks are subjected to visual inspection to identify anomalies, such as variations of bands or appearance of new bands. The densitometry of the traces allows the quantitative evaluation of the lipoprotein fractions.
Lipoproteins are circulating macromolecular complexes, that transport lipids to various tissues where they perform their metabolic functions. Lipoproteins have a spherical shape and contain triglycerides and cholesterol esters in the core of the molecule, with phospholipids and free cholesterol on the surface. On the surface are also present specific proteins called apolipoproteins (e. g. Apo A, Apo B, Apo C) that bind lipids.
Lipoproteins have been classified according to their physical and chemical properties. Ultracentrifugation allows to separate lipoproteins in different fractions, according to their density, called chylomicrons, high density lipoproteins (HDL), intermediate density lipoproteins (IDL), low density lipoproteins (LDL), very low-density lipoproteins (VLDL). Except for LDL lipoproteins that contain only one type of apolipoprotein, the other classes of lipoproteins are carried by more than one type of apolipoproteins whose percentage varies according to the class of lipoprotein.
Electrophoresis of lipoproteins fractions, on agarose gel plate at alkaline pH, yields four bands called Alpha (anodal), Pre-Beta, Beta and Chylomicrons that remain at the application point. Each fraction contains a different combination of cholesterol, glycerides, cholesterol esters and proteins.
This lipoprotein distribution reflects the interactions between plasma lipids and lipoproteins. Disorders of lipid metabolism are termed “dislipoproteinemias” and include hypercholesterolemia or increase of plasma triglycerides and/or cholesterol. These alterations are associated with modified lipoprotein electrophoretic pattern and, in some pathological conditions, can provide important clinical information as many lipoproteins disorders result in the same lipid concentration profile.
Electrophoresis separates the different classes of lipoproteins according to their specific mobility when subjected to an electric field. With the Interlab procedure, lipoproteins are separated at alkaline pH by zone electrophoresis on agarose gel plates. When the electrophoretic separation of the bands is complete, the agarose gel plate is denaturated, stained with Sudan Black, destained and dried. The patterns are then scanned and densitometric results are shown together with the graph.
CODE | DESCRIPTION | SAMPLES FOR GEL | TEST FOR KIT |
---|---|---|---|
SRE612K | KIT FOR LDH ISOENZYMES | 13 | 130 |
Intended Use
The electrophoresis of LDH Isoenzymes kit is intended for the qualitative and quantitative determination of the Lactate Dehydrogenase isoenzymes in human serum by electrophoresis on agarose gel and specific enzymatic revelations.
Lactate Dehydrogenase (LDH) is an enzyme that catalyses the reversible oxidation of lactate to pyruvate using NAD+ as a hydrogen acceptor, with the formation of NADH. It is an enzyme present in almost all tissues and cells of the human body, particularly in the liver, heart, skeletal muscles, kidneys, lungs, red blood cells, white blood cells.
The enzyme has a molecular weight of about 134000 Da, it is a tetramer consisting of the association of four polypeptide chains (subunits) of two different types: M (“muscle”) and H (“heart”). The different possible combinations of the two types of subunits in forming the tetramer give rise to five different molecular forms, called isoforms or isoenzymes. Each isoform exhibits a different electrophoretic mobility.
LDH is used as a marker of tissue or cellular damage because it is released from the cells into the bloodstream when they are damaged or destroyed.
The qualitative and/or quantitative variations of electrophoresis of isoenzymes LDH therefore provide useful information in the diagnosis of many pathologies.
LDH isoforms are separated on agarose gel according to their different electrophoretic mobility. After electrophoresis, the isoenzymes are revealed by incubation with a specific enzymatic reaction producing precipitates with a colour proportional to the LDH enzymatic activity.
CODE | DESCRIPTION | SAMPLES FOR GEL | TEST FOR KIT |
---|---|---|---|
SRE610K | KIT FOR ALP ISOENZYMES | 13 | 130 |
Intended Use
The electrophoresis of ALP isoenzymes kit is intended to be used for the qualitative and quantitative identification of the Alkaline Phosphatase isoenzymes in human serum by agarose electrophoresis and specific enzymatic revelations.
Alkaline Phosphatase (ALP) is an enzyme found in all tissues. Tissues with particularly high concentrations of ALP include the liver, bile ducts, placenta and bone. Damaged or diseased tissue releases enzymes into the blood, so serum ALP measurements can be abnormal in many conditions, including bone disease. Serum ALP is also increased in some normal circumstances (for example, during normal bone growth) or in response to a variety of drugs.
There are multiple varieties of ALP, called isoenzymes. Different types of isoenzymes, each different structure, are found in different tissues (for example, liver and bone ALP isoenzymes have different structures) and can be quantified separately in the laboratory. To differentiate the location of damaged or diseased tissue in the body, ALP isoenzyme testing must be done.
The ALP isoenzymes are separated according to their mobility on agarose gel plate. It is known that the presence of sialic acid groups increases the electrophoretic mobility of proteins and that the ALP isoenzymes are sialated to different degree. The treatment with Neuraminidase allows to remove sialic acid residues and therefore to reduce of the electrophoretic mobility of some components of the alkaline phosphatase. Intestinal Alkaline Phosphatase differs from other tissue phosphatases because it lacks sialic acid and will not be affected by treatment with Neuraminidase. After migration, each fraction can be detected with a specific enzymatic reaction producing precipitates with a colour proportional to the ALP enzymatic activity. At the end of the analysis it will be possible to compare the electrophoretic runs of the different ALP isozymes by comparing the electrophoretic mobilities influenced by the treatment with Neuraminidase.
CODE | DESCRIPTION | SAMPLES FOR GEL | TEST FOR KIT |
---|---|---|---|
SRE611K | KIT FOR CK ISOENZYMES | 13 | 130 |
Intended Use
The electrophoresis of CK Isoenzymes kit is intended to be used for the qualitative and quantitative determination of the Creatine-kinase isoenzymes in human serum by electrophoresis on agarose gel and specific enzymatic revelations.
The Creatine-kinase (CK) is an enzyme of intra-cellular transfer of energy. The CK is present in the cytoplasm and mitochondria of muscular cells. The CK is found in several human tissues and particularly in Brain, Myocardial and Skeletal muscles. They are 2 molecular subunits of the CK, called M and B, because they have been isolated respectively from Muscle and Brain.
Each CK isoenzyme is a molecule dimer of these 2 subunits: Brain CK is composed of 2 subunits of B and is called CK-BB. Muscle CK is composed of 2 subunits of M and is called CK-MM. Heart muscle CK is composed of 1 subunit of M and 1 subunit of B and is called CK-MB.
The most important use of CK isoenzymes is in the aid of diagnosis of myocardial damage.
CK isoenzymes are separated based on their different electrophoretic mobility on agarose gel.
After electrophoresis, the isoenzymes are revealed by incubation with a specific enzymatic reaction producing precipitates with a colour proportional to the CK enzymatic activity.
CODE | DESCRIPTION | SAMPLES FOR GEL | TEST FOR KIT |
---|---|---|---|
SRE622K | KIT FOR CSF ISOELECTRIC FOCUSING | 6 | 60 |
Intended use
The Interlab CSF Isoelectric Focusing Kit is intended for identifying oligoclonal banding in paired serum and cerebrospinal fluid (CSF) using isoelectric focusing and immunoblotting.
It is used to allows the chromogenic detection of IgG oligoclonal immunoglobulins.
IgG profiles in serum and CSF are visually compared allowing the identification of oligoclonal bands originating from the intrathecal synthesis of immunoglobulins, with the aim of providing support in the diagnosis of inflammatory diseases of the central nervous system.
The procedure includes isoelectric focusing on agarose gel plate and immunoblotting steps.
Isoelectric focusing on agarose gel has the purpose to separate the proteins depending on their isoelectric point in the CSF and serum samples. The immunoblotting steps have the purpose to transfer proteins on the transfer membrane.
The incubation of transfer membrane with Anti-IgG Fc Human Antibody allows to detect the IgG oligoclonal banding with high sensitivity and to demonstrate the difference or missing in the distribution of IgG in the CSF and serum of the same patient.