Haptoglobin (19-347) Human

Haptoglobin (19-347 a.a) Human Recombinant
Cat. No.
BT13806
Source
Escherichia Coli.
Synonyms
Haptoglobin, Zonulin, Haptoglobin alpha chain, Haptoglobin beta chain, Haptoglobin isoform 2 preproprotein, BP, HP2ALPHA2, HPA1S.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Usage
THE BioTek'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 polypeptide chain containing 352 amino acids (19-347) and having a molecular mass of 39.0 kDa. Haptoglobin is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Haptoglobin is a protein that plays a crucial role in regulating immune responses and maintaining intestinal integrity. It facilitates the disassembly of tight junctions between cells in the intestine, influencing the passage of substances. This protein exhibits antibacterial properties and contributes to the body's defense against infections. Additionally, it modulates various aspects of the acute phase response, a systemic reaction to inflammation or injury. Haptoglobin is synthesized as two separate chains, alpha and beta, which subsequently assemble into a tetrameric structure. Its primary function is to bind free hemoglobin released from red blood cells with high affinity. This binding prevents the oxidative damage that free hemoglobin can cause and facilitates its removal from circulation by the reticuloendothelial system.
Description
This recombinant human Haptoglobin, spanning amino acids 19 to 347, is produced in E. coli. It exists as a single polypeptide chain with a molecular weight of 39.0 kDa. For purification purposes, a 23-amino acid His-tag is attached to the N-terminus. The protein is further purified using proprietary chromatographic methods.
Physical Appearance
The product appears as a clear, colorless solution that has been sterilized by filtration.
Formulation
The Haptoglobin solution is provided at a concentration of 0.5 mg/mL in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 10% glycerol, and 0.4 M Urea.
Stability
For short-term storage (2-4 weeks), the product should be kept at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is advisable for long-term storage. To maintain product integrity, repeated freezing and thawing cycles should be avoided.
Purity
The purity of this Haptoglobin product exceeds 80%, as determined by SDS-PAGE analysis.
Synonyms
Haptoglobin, Zonulin, Haptoglobin alpha chain, Haptoglobin beta chain, Haptoglobin isoform 2 preproprotein, BP, HP2ALPHA2, HPA1S.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSVDSGNDV TDIADDGCPK PPEIAHGYVE HSVRYQCKNY YKLRTEGDGV YTLNNEKQWI NKAVGDKLPE CEAVCGKPKN PANPVQRILG GHLDAKGSFP WQAKMVSHHN LTTGATLINE QWLLTTAKNL FLNHSENATA KDIAPTLTLY VGKKQLVEIE KVVLHPNYSQ VDIGLIKLKQ KVSVNERVMP ICLPSKDYAE VGRVGYVSGW GRNANFKFTD HLKYVMLPVA DQDQCIRHYE GSTVPEKKTP KSPVGVQPIL NEHTFCAGMS KYQEDTCYGD AGSAFAVHDL EEDTWYATGI LSFDKSCAVA EYGVYVKVTS IQDWVQKTIA EN.

Product Science Overview

Structure and Function

Haptoglobin is a glycoprotein composed of two alpha and two beta chains, forming a tetramer. The recombinant human haptoglobin (19-347 a.a) refers to a specific segment of the haptoglobin protein, spanning amino acids 19 to 347. This recombinant form is typically expressed in Escherichia coli (E. coli) and is often fused to a His-tag at the N-terminus to facilitate purification .

The primary function of haptoglobin is to bind free hemoglobin released during hemolysis. This binding prevents the loss of iron through the kidneys and protects the kidneys from damage by free hemoglobin. The haptoglobin-hemoglobin complex is then removed by the reticuloendothelial system, primarily in the liver and spleen.

Clinical Significance

Haptoglobin levels are measured in clinical settings to assess hemolytic anemia. Low levels of haptoglobin in the blood can indicate increased red blood cell destruction. Additionally, haptoglobin is an acute-phase protein, meaning its levels can increase in response to inflammation, infection, or trauma.

Recombinant Production

The recombinant form of haptoglobin (19-347 a.a) is produced using genetic engineering techniques. The gene encoding the desired segment of haptoglobin is inserted into an expression vector, which is then introduced into E. coli cells. These cells are cultured, and the recombinant protein is expressed and subsequently purified using chromatographic techniques .

Recombinant haptoglobin is used in various research applications, including studies on hemolysis, inflammation, and the acute-phase response. It is also utilized in the development of diagnostic assays and therapeutic interventions.

Applications in Research and Medicine
  1. Research: Recombinant haptoglobin is used to study the mechanisms of hemolysis and the body’s response to free hemoglobin. It helps in understanding the role of haptoglobin in various diseases and conditions.
  2. Diagnostics: Haptoglobin levels are measured in blood tests to diagnose and monitor hemolytic anemia and other conditions associated with red blood cell destruction.
  3. Therapeutics: Research is ongoing to explore the potential therapeutic uses of haptoglobin, particularly in conditions involving excessive hemolysis or inflammation.

In summary, recombinant human haptoglobin (19-347 a.a) is a valuable tool in both research and clinical settings. Its ability to bind free hemoglobin and its role in the acute-phase response make it an important protein for studying and managing various medical conditions.

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