Human Haptoglobin, Phenotype 1-1
Native, whole molecule purified from donors specific for the Haptoglobin 1-1 phenotype
Produktdetails
Synonyms
Zonulin, HPT, HP, BP, HP2ALPHA2, HPA1S
Description of Human Haptoglobin, Phenotype 1-1
Human Haptoglobin, Phenotype 1-1 is a 86 kDa protein. Human haptoglobin 1-1 (Hp1-1), the most efficient phenotype of the hemoglobin-binding glycoprotein, forms dimers through α1β-chain associations, enabling rapid neutralization of toxic free hemoglobin (Hb) with a binding capacity of 1.25–1.5 mg Hb per mg Hp. Its superior antioxidant capacity stems from compact polymer structures that enhance CD163 receptor-mediated clearance of Hb-Hp complexes by macrophages, suppressing iron-driven oxidative stress and NF-κB inflammatory pathways more effectively than Hp2-1 or Hp2-2 phenotypes. Clinically, Hp1-1 demonstrates protective effects against diabetic vascular complications by preserving endothelial nitric oxide bioavailability and reducing advanced glycation end-product formation, lowering retinopathy and nephropathy risks by 50–70% compared to other phenotypes. In sickle cell disease, Hp1-1 carriers exhibit 40% lower cell-free Hb levels during crises and a twofold reduction in multiorgan failure risk due to enhanced Hb sequestration. Paradoxically, Hp1-1 prevalence increases in cirrhosis (55% vs. 30% in healthy populations) as hepatic synthesis shifts toward acute-phase production despite systemic oxidative stress.
Source
Human plasma non-reactive for HBsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests
Storage
For long term, store Human Haptoglobin, Phenotype 1-1 at -20°C.
Applications
ELISA, Protein Chemistry, Inflammation, Sickle Cell Anemia, Glycosylation, Stroke, Central Nervous System Injury, Diabetes, Cardiovascular Disease, In Vitro Diagnostic, Iron Metabolism, Cancer.
Citations/Publications
Tamara, S., et al. (2020), 'A wealth of genotype-specific proteoforms fine-tunes hemoglobin scavenging by haptoglobin', PNAS, 117(27): pp. 15554-15564. Available at: https://doi.org/10.1073/pnas.2002483117
Wang, Y., et al., (2019), 'Multipronged ESI−MS Approach for Studying Glycan-BindingProtein Interactions with Glycoproteins', Anal. Chem., 91: pp 2140−2147. Available at: DOI: 10.1021/acs.analchem.8b04673
Ivanov, D. G., et al., (2022), 'Rapid Evaluation of the Extent of Haptoglobin Glycosylation Using Orthogonal Intact-Mass MS Approaches and Multivariate Analysis", Anal. Chem., 94: pp 5140−5148. Available at: https://doi.org/10.1021/acs.analchem.1c05585
Ivanov, D. G., et al., (2024), 'Probing the Architecture of Multisubunit Protein Complexes with In-line Disulfide Reduction and Native MS Analysis', Anal. Chem., 96:(21) pp 8243–8248. Available at: https://doi.org/10.1021/acs.analchem.4c00879
Ascenzi, P., et al., (2021), 'Kinetic inequivalence between α and β subunits of ligand dissociation from ferrous nitrosylated human haptoglobin:hemoglobin complexes. A comparison with O2 and CO dissociation', Journal of Inorganic Biochemistry 214: pp 111272. Available at: https://doi.org/10.1016/j.jinorgbio.2020.111272
NCBI: https://www.ncbi.nlm.nih.gov/protein/P00738
Shipped with ice packs
Gel Scan of Human Haptoglobin, Phenotype 1-1
Fig. 1: SDS-PAGE Gel |
Usage: For research use only. Not for use in diagnostic or therapeutic procedures. Not for human use.
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