Haptoglobin Antibody [B3H20] | Primary Antibodies

Application: Reactivity: Human

Lane 1: Human plasma

Usage Information

Dilution
WB1:1000 IHC1:100-1:200 IF1:100-1:200

Application
WB, IHC, IF, ELISA

Reactivity
Human

Source
Mouse Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
242 kDa

Datasheet & SDS

Biological Description

Specificity
Haptoglobin Antibody [B3H20] detects endogenous levels of total Haptoglobin protein.

Clone
B3H20

Synonym(s)
Haptoglobin; Zonulin; HP

Background
Haptoglobin (Hp) is an acute phase glycoprotein produced mainly in hepatocytes that functions as a key extracellular scavenger of hemoglobin released during intravascular hemolysis, thereby limiting iron driven oxidative damage and protecting renal and vascular tissues. It circulates as dimeric and multimeric assemblies whose structural organization supports high affinity binding to free hemoglobin, forming a stable haptoglobin–hemoglobin (Hp–Hb) complex that masks the pro oxidant heme moiety and prevents its dissociation into ferric iron and globin radicals. This complex is recognized by the hemoglobin–haptoglobin scavenger receptor CD163, which is expressed on monocytes and tissue macrophages in the liver, spleen, and bone marrow, mediating clathrin dependent endocytosis and subsequent lysosomal degradation of Hp–Hb, while the heme component is catabolized and iron is recycled or stored via ferritin. In parallel, haptoglobin modulates inflammatory signaling by regulating the availability of free hemoglobin for CD163 dependent anti inflammatory pathways, since ligation of CD163 promotes secretion of interleukin 10 and suppresses pro inflammatory cytokine production, thus positioning haptoglobin as a molecular interface between hemolysis, oxidative stress, and macrophage polarization. By sequestering toxic hemoglobin and facilitating its receptor mediated clearance, haptoglobin constrains lipid peroxidation, endothelial activation, and renal tubular injury in settings of hemolytic anemia, ischemia–reperfusion, and severe infection, so that its depletion or overload is associated with accentuated oxidative damage and microvascular dysfunction. Polymorphisms in the haptoglobin gene generate distinct isoforms that differ in polymerization state and hemoglobin binding capacity, influencing the efficiency of Hp–Hb complex formation and clearance, and these allelic variants are linked to altered susceptibility to ischemic cardiovascular events and chronic inflammatory states, yet haptoglobin dependent signaling remains dysregulated when hemolytic or inflammatory loads overwhelm the scavenger system and exhaust the CD163 mediated clearance machinery.

Background

Haptoglobin (Hp) is an acute phase glycoprotein produced mainly in hepatocytes that functions as a key extracellular scavenger of hemoglobin released during intravascular hemolysis, thereby limiting iron driven oxidative damage and protecting renal and vascular tissues. It circulates as dimeric and multimeric assemblies whose structural organization supports high affinity binding to free hemoglobin, forming a stable haptoglobin–hemoglobin (Hp–Hb) complex that masks the pro oxidant heme moiety and prevents its dissociation into ferric iron and globin radicals. This complex is recognized by the hemoglobin–haptoglobin scavenger receptor CD163, which is expressed on monocytes and tissue macrophages in the liver, spleen, and bone marrow, mediating clathrin dependent endocytosis and subsequent lysosomal degradation of Hp–Hb, while the heme component is catabolized and iron is recycled or stored via ferritin. In parallel, haptoglobin modulates inflammatory signaling by regulating the availability of free hemoglobin for CD163 dependent anti inflammatory pathways, since ligation of CD163 promotes secretion of interleukin 10 and suppresses pro inflammatory cytokine production, thus positioning haptoglobin as a molecular interface between hemolysis, oxidative stress, and macrophage polarization. By sequestering toxic hemoglobin and facilitating its receptor mediated clearance, haptoglobin constrains lipid peroxidation, endothelial activation, and renal tubular injury in settings of hemolytic anemia, ischemia–reperfusion, and severe infection, so that its depletion or overload is associated with accentuated oxidative damage and microvascular dysfunction. Polymorphisms in the haptoglobin gene generate distinct isoforms that differ in polymerization state and hemoglobin binding capacity, influencing the efficiency of Hp–Hb complex formation and clearance, and these allelic variants are linked to altered susceptibility to ischemic cardiovascular events and chronic inflammatory states, yet haptoglobin dependent signaling remains dysregulated when hemolytic or inflammatory loads overwhelm the scavenger system and exhaust the CD163 mediated clearance machinery.

References
https://pubmed.ncbi.nlm.nih.gov/19620777/ https://pubmed.ncbi.nlm.nih.gov/40644526/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%