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Haptoglobin Human ELISA

  • Regulatory status:RUO
  • Type:Sandwich ELISA, HRP-labelled antibody
  • Other names:Hp
  • Species:Human
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Cat. No. Size Price


RD191407100R 96 wells (1 kit)
PubMed Product Details
Technical Data

Type

Sandwich ELISA, HRP-labelled antibody

Applications

Serum, Plasma-EDTA, Plasma-Heparin, Plasma-Citrate, Urine, Cerebrospinal fluid

Sample Requirements

10 µl/well

Storage/Expiration

Store the complete kit at 2–8°C. Under these conditions, the kit is stable until the expiration date (see label on the box).

Calibration Curve

Calibration Range

3.13–200 ng/ml

Limit of Detection

0.385 ng/ml

Intra-assay (Within-Run)

n = 8; CV = 5.9 %

Inter-assay (Run-to-Run)

n = 6; CV = 6.9 %

Spiking Recovery

Serum: 100.1 %
CSF: 99.3 %
Urine: 100.5 %

Dilutation Linearity

Serum: 100.9 %
CSF: 101.3 %
Urine: 105.4 %

Summary

Features

  • It is intended for research use only
  • The total assay time is less than 3 hours
  • The kit measures haptoglobin in human serum, plasma (EDTA, citrate, heparin), cerebrospinal fluid (CSF) and urine
  • Assay format is 96 wells
  • Standard is purified human native protein (Hp1-1, Hp2-1, Hp2-2 phenotypes)
  • Components of the kit are provided ready to use, concentrated or lyophilized

Research topic

Aneurysmal subarachnoid hemorrhage, Cardiovascular disease, Diabetology - Other Relevant Products, Immune Response, Infection and Inflammation, Neural tissue markers, Oxidative stress, Renal disease

Summary

Haptoglobin (Hp), is a prominent plasma glycoprotein involved in the scavenging of free hemoglobin. Hp is composed of two α-chains and two identical β-chains. The α-chains are linked together by a disulphide bond, and each β-chain is similarly bonded to an α-chain giving the simple chain formula of (αβ)2. The human gene for Hp, located on chromosome 16q22, consists of three structural alleles: Hp1F, Hp1S and Hp2. The Hp2 allele, is the result of a fusion of the Hp1F and Hp1S alleles, and is present only in humans. The presence of the Hp1 and Hp2 alleles gives rise to three major phenotypes: Hp1-1 phenotype is a single α1β homodimer with a molecular weight of 86 kDa; homozygous Hp2-2 individuals express the Hp2-2 phenotype, which consists of cyclic Hp polymers containing 3 or more α2β subunits (170–900 kDa); Hp2-1 heterozygous people have Hp which are assembled into linear homodimers and multimers from various numbers of α2β subunits joined with α1β subunit at each terminus (86–300 kDa). The prevalence of the three Hp genotypes varies dramatically across populations, with the highest frequency of the Hp1 allele found in Africa and South America and the lowest in Southeast Asia. The distribution of the Hp1-1, 2-2 and 2-1 genotypes in most western countries is 16%, 36% and 48% respectively.

Most Hp is produced by the liver, although the skin, lungs, kidney and adipose tissue are additional sources of Hp production. The function of haptoglobin is primarily to bind hemoglobin (Hb) released from red blood cells after either intravascular or extravascular hemolysis. The Hp-Hb complex is removed from the circulation by binding to a receptor CD163 found on the cell surface of monocytes and macrophages (mainly macrophage-like
Kupffer cells in the liver). Although the half-life of Hp is approximately 3–5 days, when bound to hemoglobin the complex is removed from the circulation within 20 min. The normal level of plasma Hp varies considerably ranging from 0.3 to 3 mg/ml, but in any given individual the Hp level remains fairly constant and therefore the observation of marked concentration changes has clinical significance.

The Haptoglobin protein (especially Hp1-1 phenotype) protects against heme- and iron-driven oxidative damage to the vascular system and kidney, and secondly, it plays a role as the bacteriostatic agent by restricting access of bacteria to Hb-derived iron that is critical for their growth.

The level of Hp increases dramatically upon acute stress and inflammation, so it is considered an acute-phase plasma protein. Its synthesis can be stimulated by IL-6. The binding of the Hp-Hb complex by macrophage CD163 leads to secretion of the anti-inflammatory cytokine IL-10 and the breakdown products of hem which also have potent anti-inflammatory activity. Hp also stimulates angiogenesis in vitro and in vivo. It was found that such proangiogenic activity is strongest for Hp2-2 phenotype.

Haptoglobin may affect the interpretation of the glycosylated hemoglobin levels in the estimation of glucose controls in diabetes patients, since haptoglobin is involved in hemoglobin turnover. Hp has been implicated in both type 2 diabetes (T2D) and T2D associated cardiovascular diseases (CVD). It has been reported that Hp (mostly Hp2-2) binds to apolipoprotein A1 (ApoA1) in the same location as lecithin-cholesterol acyltransferase (LCAT), subsequently decreasing LCAT activity and therefore limiting high density lipoprotein (HDL) maturation. This inhibits reverse cholesterol transport causing HDL to become proatherogenic. Moreover the interaction of Hb with HDL through HP-ApoA1 allows the oxidation of HDL and its acquisition of proatherogenic and proinflammatory properties. Such processes can be accentuated when hemoglobin which is complexed with Hp is glycosylated.

Besides CVD, Hp level may be useful to predict patients with type T2D at risk of nephropathy before the development of macroalbuminuria or reduced glomerular filtration rate.

Changes in Haptoglobin levels were found also in other pathologies. Decrease of Hp occurs during hemolysis (hemolytic anemia), ineffective erythropoiesis and liver disease. Moreover, Hp levels are decreased in people with allergy reactions. Several studies have associated haptoglobin concentration in serum with many types of cancer. The anti-inflammatory role of Hp may play a role in failure of the host immune system to recognize the tumor by impairing the tumor surveillance system. Increased Hp was found in cerebrospinal fluid (CSF) from patients with CNS disorders. Increases of Hp in traumatic brain injury likely are related to high levels of IL-6 and IL-8.

References to Summary

References to Haptoglobin

  • Adams JN, Cox AJ, Freedman BI, Langefeld CD, Carr JJ, Bowden DW. Genetic analysis of haptoglobin polymorphisms with cardiovascular disease and type 2 diabetes in the Diabetes Heart Study. Cardiovasc Diabetol. 2013;12:31
  • Bhensdadia NM, Hunt KJ, Lopes-Virella MF, Michael Tucker J, Mataria MR, Alge JL, Neely BA, Janech MG, Arthur JM. Urine haptoglobin levels predict early renal functional decline in patients with type 2 diabetes. Kidney Int. 2013 Jun;83 (6):1136-43
  • Cahill LE, Levy AP, Chiuve SE, Jensen MK, Wang H, Shara NM, Blum S, Howard BV, Pai JK, Mukamal KJ, Rexrode KM, Rimm EB. Haptoglobin genotype is a consistent marker of coronary heart disease risk among individuals with elevated glycosylated hemoglobin. J Am Coll Cardiol. 2013 Feb 19;61 (7):728-37
  • Carter K, Worwood M. Haptoglobin: a review of the major allele frequencies worldwide and their association with diseases. Int J Lab Hematol. 2007 Apr;29 (2):92-110
  • Chen YC, Lee CC, Huang CY, Huang HB, Yu CC, Ho YC, Su YC. Haptoglobin polymorphism as a risk factor for chronic kidney disease: a case-control study. Am J Nephrol. 2011;33 (6):510-4
  • Costacou T, Levy AP. Haptoglobin genotype and its role in diabetic cardiovascular disease. J Cardiovasc Transl Res. 2012 Aug;5 (4):423-35
  • Goldenstein H, Levy NS, Levy AP. Involvement of haptoglobin in prevention of oxidative stress cause by hemoglobin in preeclampsia. Adv Biosci Biotechnol. 2012;3:1037-1042
  • Ko DH, Chang HE, Kim TS, Song EY, Park KU, Song J, Han KS. A review of haptoglobin typing methods for disease association study and preventing anaphylactic transfusion reaction. Biomed Res Int. 2013;2013:390630
  • Leclerc JL, Blackburn S, Neal D, Mendez NV, Wharton JA, Waters MF, Dore S. Haptoglobin phenotype predicts the development of focal and global cerebral vasospasm and may influence outcomes after aneurysmal subarachnoid hemorrhage. Proc Natl Acad Sci U S A. 2015 Jan 27;112 (4):1155-60
  • Levy AP, Asleh R, Blum S, Levy NS, Miller-Lotan R, Kalet-Litman S, Anbinder Y, Lache O, Nakhoul FM, Asaf R, Farbstein D, Pollak M, Soloveichik YZ, Strauss M, Alshiek J, Livshits A, Schwartz A, Awad H, Jad K, Goldenstein H. Haptoglobin: basic and clinical aspects. Antioxid Redox Signal. 2010 Feb;12 (2):293-304
  • Levy NS, Levy AP. Changing the face of diabetic care with haptoglobin genotype selection and vitamin e. Rambam Maimonides Med J. 2011 Apr;2 (2):e0047
  • Papp M, Foldi I, Nemes E, Udvardy M, Harsfalvi J, Altorjay I, Mate I, Dinya T, Varvolgyi C, Barta Z, Veres G, Lakatos PL, Tumpek J, Toth L, Szathmari E, Kapitany A, Gyetvai A, Korponay-Szabo IR. Haptoglobin polymorphism: a novel genetic risk factor for celiac disease development and its clinical manifestations. Clin Chem. 2008 Apr;54 (4):697-704
  • Pirincci N, Gecit I, Gunes M, Kemik AS, Yuksel MB, Kaba M, Ceylan K, Aslan M. Haptoglobin levels in Turkish patients with bladder cancer and its association with clinicopathological features. Asian Pac J Cancer Prev. 2012;13 (12):6063-6
  • Polticelli F, Bocedi A, Minervini G, Ascenzi P. Human haptoglobin structure and function--a molecular modelling study. FEBS J. 2008 Nov;275 (22):5648-56
  • Pompach P, Novakova J, Kavan D, Benada O, Ruzicka V, Volny M, Novak P. Planar Functionalized Surfaces for Direct Immunoaffinity Desorption/Ionization Mass Spectrometry. Clin Chem. 2016 Jan;62 (1):270-8
  • Speeckaert R, Brochez L, Lambert J, van Geel N, Speeckaert MM, Claeys L, Langlois M, Van Laer C, Peeters P, Delanghe JR. The haptoglobin phenotype influences the risk of cutaneous squamous cell carcinoma in kidney transplant patients. J Eur Acad Dermatol Venereol. 2012 May;26 (5):566-71
  • Suzuki K, Yagi K, Oka R, Saiki Y, Kubota M, Sugihara M, Ito N, Kawashiri MA, Nohara A, Horita H, Takeda Y, Yamagishi M, Kobayashi J. Relationships of serum haptoglobin concentration with HbA1c and glycated albumin concentrations in Japanese type 2 diabetic patients. Clin Chem Lab Med. 2009;47 (1):70-4
  • Weissgerber TL, Roberts JM, Jeyabalan A,
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