Haptoglobin

Haptoglobin (abbreviated as Hp) is the protein that in humans is encoded by the HP gene. In blood plasma, haptoglobin binds with high affinity to free hemoglobin released from erythrocytes, and thereby inhibits its deleterious oxidative activity. Compared to Hp, hemopexin binds to free heme. The haptoglobin-hemoglobin complex will then be removed by the reticuloendothelial system (mostly the spleen).

HP
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesHP, BP, HP2ALPHA2, HPA1S, haptoglobin
External IDsOMIM: 140100 MGI: 96211 HomoloGene: 121756 GeneCards: HP
Orthologs
SpeciesHumanMouse
Entrez

3240

15439

Ensembl

ENSG00000257017

ENSMUSG00000031722

UniProt

P00738

Q61646

RefSeq (mRNA)

NM_001126102
NM_005143
NM_001318138

NM_017370
NM_001329965

RefSeq (protein)

NP_001119574
NP_001305067
NP_005134

NP_001316894
NP_059066

Location (UCSC)Chr 16: 72.05 – 72.06 MbChr 8: 110.3 – 110.31 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

In clinical settings, the haptoglobin assay is used to screen for and monitor intravascular hemolytic anemia. In intravascular hemolysis, free hemoglobin will be released into circulation and hence haptoglobin will bind the hemoglobin. This causes a decline in haptoglobin levels.

The protein was discovered as a "plasma substance" in 1938 by French biochemists Max-Fernand Jayle and Michel Polonovski.

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