Haptoglobin

Haptoglobin Human Recombinant
Cat. No.
BT13721
Source
Escherichia Coli.
Synonyms
Haptoglobin, HP, BP, HPA1S, MGC111141, HP2-ALPHA-2.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity

Greater than 90.0% as determined by SDS-PAGE.

Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

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).

Product Specs

Introduction
Haptoglobin, a glycoprotein primarily synthesized by the liver, plays a crucial role in binding free hemoglobin within the bloodstream. This binding process prevents kidney damage and iron loss, particularly after hemolysis. The haptoglobin-hemoglobin complex is then eliminated by the reticuloendothelial system, primarily the spleen. Consequently, haptoglobin levels decrease during hemolytic anemias. Furthermore, haptoglobin prevents iron-dependent bacteria from utilizing iron released from hemoglobin breakdown. Composed of two A- and two B-chains linked by disulfide bonds, haptoglobin exhibits three primary phenotypes: Hp 1-1, Hp 2-1, and Hp 2-2, with varying effectiveness in binding hemoglobin and modulating inflammation. Ranging in molecular mass from 8-200 kDa, haptoglobin levels serve as a marker for various health conditions, including hemolysis, liver dysfunction, and inflammation. Genetic mutations can lead to ahaptoglobinemia or hypohaptoglobinemia. Research also links haptoglobin to conditions like diabetic nephropathy, coronary artery disease in type 1 diabetes, Crohn's disease, and others.
Description

Recombinant Human Haptoglobin, produced in E.Coli, is a single, non-glycosylated polypeptide chain. It includes a His tag fused to the protein, resulting in a total molecular weight of 33 kDa (including a 4 kDa His-tag).

Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation

Each mg of lyophilized Haptoglobin is supplied in a buffer containing 1xPBS, 0.4% SDS, and 4mM DTT.

Solubility
To reconstitute lyophilized Haptoglobin, it is recommended to dissolve it in sterile 18MΩ-cm H2O to a concentration of at least 100µg/ml. This solution can then be further diluted into other aqueous solutions as needed.
Stability
Lyophilized Haptoglobin remains stable at room temperature for up to 3 weeks. However, for long-term storage, it should be stored desiccated at temperatures below -18°C. After reconstitution, Haptoglobin should be stored at 4°C for 2-7 days. For extended storage, freezing at -18°C is recommended. To preserve protein stability during storage, it is advisable to add a carrier protein (0.1% HSA or BSA) and avoid repeated freeze-thaw cycles.
Purity

The purity of this product is greater than 90.0% as determined by SDS-PAGE analysis.

Synonyms
Haptoglobin, HP, BP, HPA1S, MGC111141, HP2-ALPHA-2.
Source
Escherichia Coli.
Amino Acid Sequence

L ILGGHLDAKG SFPWQAKMVS HHNLTTGATL INEQWLLTTA KNLFLNHSEN ATAKDIAPTL TLYVGKKQLV EIEKVVLHPN YSQVDIGLIK LKQKVSVNER VMPICLPSKD YAEVGRVGYV SGWGRNANFK FTDHLKYVML PVADQDQCIR HYEGSTVPEK KTPKSPVGVQ PILNEHTFCA GMSKYQEDTC YGDAGSAFAV HDLEEDTWYA TGILSFDKSC AVAEYGVYVK VTSIQDWVQK TIAEN

Product Science Overview

Introduction

Haptoglobin (Hp) is an abundant plasma glycoprotein primarily synthesized in the liver. It plays a crucial role in binding free hemoglobin (Hb) released during hemolysis, thereby preventing the toxic effects of free Hb in the kidney, vasculature, and surrounding tissues . The complex formed between haptoglobin and hemoglobin (Hb:Hp complex) provides protective activities that mitigate the harmful impact of free Hb .

Structure and Function

Haptoglobin is a member of the peptidase S1 family of serine proteases . It captures and combines with free plasma hemoglobin to facilitate hepatic recycling of heme iron and prevent kidney damage . Additionally, haptoglobin acts as an antioxidant, has antibacterial activity, and modulates various aspects of the acute phase response .

Genetic Variants

There are two main allelic variants of haptoglobin: HP1 and HP2 . The HP2 variant is considered the ancestral form and is characterized by an α2-chain containing an extra cysteine residue, which pairs with additional α-chains to generate multimers with molecular weights ranging from 200 to 900 kDa . The two human HP1 alleles (HP1F and HP1S) differ by a two-amino-acid substitution polymorphism within the α-chain and are derived from HP2 by recurring exon deletions .

Recombinant Haptoglobin Production

Recombinant haptoglobin (human) is produced using mammalian cell lines, such as FS293F cells . The production process involves co-expression of active complement C1r subcomponent-like protein (C1r-LP) to ensure efficient expression of mature and fully functional haptoglobin . This recombinant approach allows for the production of phenotype-specific haptoglobin polymers, which can be used as therapeutic proteins to attenuate the toxic effects of cell-free hemoglobin in conditions such as sickle cell disease and other hemolytic disorders .

Therapeutic Applications

Haptoglobin has been evaluated as a therapeutic protein in preclinical studies to mitigate the toxic effects of cell-free hemoglobin . Proof-of-concept studies have demonstrated its efficacy in hemolysis associated with transfusion and sickle cell anemia . The recombinant production of phenotype-specific haptoglobin polymers offers opportunities for developing optimized hemoglobin-binding therapeutics .

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