Haptoglobin, Phenotype 1-1 [9087-69-8]
16-16-080116-1/1
Protein IDP00738
Product group Proteins / Signaling Molecules
Overview
- SupplierAthens Research
- Product NameHaptoglobin, Phenotype 1-1 [9087-69-8]
- Delivery Days Customer9
- Applications SupplierELISA, Protein Chemistry, Inflammation, Sickle Cell Anemia, Glycosylation, Stroke, Central Nervous System Injury, Diabetes, Cardiovascular Disease, In Vitro Diagnostic, Iron Metabolism, Cancer
- CertificationResearch Use Only
- Estimated Purity≥95% by SDS-PAGE, no visible alpha-2 light chain by SDS-PAGE
- Protein IDP00738
- Protein NameHaptoglobin
- Scientific DescriptionHuman haptoglobin 1-1 (Hp1-1), the most efficient phenotype of the hemoglobin-binding glycoprotein, forms dimers through alfa1bèta-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-kappaB 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.
- Shelf life instructionmore then 1 year
- SourceSource human plasma non-reactive for HBsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.
- Storage Instruction-20C
- UNSPSC41116100
References
- Tamara, S., et al. (2020), 'A wealth of genotype-specific proteoforms fine-tunes hemoglobin scavenging by haptoglobin', PNAS, 117(27): pp. 15554-15564Read this paper
- Wang, Y., et al., (2019), 'Multipronged ESI−MS Approach for Studying Glycan-BindingProtein Interactions with Glycoproteins', Anal. Chem., 91: pp 2140−2147Read this paper
- 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.Read this paper
- Ascenzi, P., et al., (2021), 'Kinetic inequivalence between alfa and bèta 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.Read this paper