HAPTOGLOBIN, HUMAN Chemical Properties

storage temp. 

-20°C

solubility 

H₂O: 10 mg/mL, clear to faintly turbid, colorless to almost colorless

form 

powder

color 

off-white

biological source

human plasma (pooled)

Water Solubility 

water: 1mg/mL

Safety Information

Hazard Codes 

B

WGK Germany 

3

RTECS 

MG8575500

HS Code 

3504009000

Storage Class

11 - Combustible Solids

MSDS

• Language:English Provider:SigmaAldrich

HAPTOGLOBIN, HUMAN Usage And Synthesis

Uses

Haptoglobin was used to study induction of the acrosome reaction in sperm. Exposure to low temperature increases their rate of fusion with zona-free hamster oocytes.

General Description

Haptoglobin is an α₂-globulin found in normal plasma at a concentration of 82-236 mg/dl and accounts for 0.4-2.6% of the total plasma proteins.The monomeric form of this acute phase plasma protein is composed of four polypeptide chains: two α chains and two β chains.

Biochem/physiol Actions

Functions by binding to plasma hemoglobin (from hemolysis). The complex is removed from the circulation, by binding to CD163 receptors on macrophages, to salvage iron and prevent oxidative damage.

Description

Haptoglobin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing fusion protein with His tag and having a total Mw of 33 kDa (4 kDa His-tag).

Source

Escherichia Coli

Background

Haptoglobin is a glycoprotein which is synthesized in the liver and circulates in the blood. Haptoglobin is produced typically by hepatocytes but also by other tissues: e.g. skin, lung, and kidney. It is a positive acute phase protein that binds free hemoglobin and removes it from the circulation to prevent kidney injury, and iron loss following hemolysis. The haptoglobin-hemoglobin complex is subsequently removed by the reticuloendothelial system (generally the spleen). As the reticuloendothelial system removes the haptoglobin-hemoglobin complex from the body, haptoglobin levels are reduced in hemolytic anaemias. In the course of binding hemoglobin, haptoglobin sequesters the iron inside hemoglobin, preventing iron-utilizing bacteria from benefitting from hemolysis.
Haptoglobin consists of two A- and two B-chains, connected by disulfide bonds. Three major haptoglobin phenotypes are known to exist (Hp 1-1, Hp 2-1, and Hp 2-2). Hp 1-1 is biologically the most effective in binding free hemoglobin and suppressing inflammatory responses associated with free hemoglobin. Hp 2-2 is biologically the least active, and Hp 2-1 is moderately active. Haptoglobin’s molecular mass ranges from 8-200 kDa.
Reduced levels can be seen in haemolysis and impaired liver function. High levels are a marker for acute or chronic inflammation. Ahaptoglobinemia or hypohaptoglobinemia are caused by mutations in the haptoglobin gene and/or its regulatory regions. Haptoglobin is also linked to diabetic nephropathy, the incidence of coronary artery disease in type 1 diabetes, Crohn's disease, inflammatory disease behavior, primary sclerosing cholangitis, susceptibility to idiopathic Parkinson's disease, and a reduced incidence of Plasmodium falciparum malaria.

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