Hemopexin Human, Sf9

Hemopexin Human Recombinant, Sf9
Cat. No.
BT20480
Source

Sf9, Baculovirus cells.

Synonyms

Hemopexin, Beta-1B-Glycoprotein, HX, Beta-1B-glycoprotein.

Appearance
Sterile filtered colorless solution.
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.
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Description

Hemopexin produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 448 amino acids (24-462a.a.) and having a molecular mass of 50.4kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).
Hemopexin is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Hemopexin, also spelled haemopexin, is a protein found in blood plasma that exhibits an exceptionally high affinity for heme, binding it more strongly than any other known protein. Primarily produced by the liver, hemopexin is classified as an acute phase reactant, meaning its synthesis increases in response to inflammation. Heme, a molecule crucial for oxygen transport, possesses the potential for toxicity due to its ability to penetrate cell membranes and generate harmful free radicals. Hemopexin plays a critical role in safeguarding the body from this potential damage by scavenging free heme released during the natural breakdown and recycling of heme-containing proteins like hemoglobin. Upon binding heme, hemopexin interacts with a specific receptor on liver cells, facilitating the delivery of heme for internalization and degradation. This process not only neutralizes heme's toxicity but also enables the conservation of iron, a valuable component of heme. Consequently, the concentration of hemopexin in the serum serves as an indicator of heme levels in circulation. Low hemopexin levels suggest elevated heme presence, indicating significant heme release and potential tissue damage.
Description
Produced using Sf9 insect cells and baculovirus expression system, our recombinant human Hemopexin is a single polypeptide chain comprising 448 amino acids (specifically, residues 24 to 462). It features a molecular weight of 50.4 kDa, as determined by its amino acid sequence. However, it's important to note that on SDS-PAGE analysis, the protein may appear as a band between 50-70 kDa due to glycosylation. This product is engineered with a 9-amino acid Histidine tag (His-tag) at the C-terminus to facilitate purification and is purified using proprietary chromatographic techniques to ensure high purity.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The Hemopexin protein is supplied in a solution at a concentration of 0.5 mg/ml. The solution is buffered using Phosphate Buffered Saline (PBS) at a pH of 7.4 and contains 10% glycerol as a stabilizing agent.
Stability
For short-term storage (up to 4 weeks), the Hemopexin solution can be stored at refrigerated temperature (4°C). For extended storage, it is highly recommended to store the protein in frozen aliquots at -20°C. To further enhance stability during long-term storage, consider adding a carrier protein such as bovine serum albumin (BSA) or human serum albumin (HSA) to a final concentration of 0.1%. It's crucial to avoid repeated freeze-thaw cycles to maintain protein integrity and activity.
Purity
The purity of our Hemopexin protein is greater than 90%, as determined by SDS-PAGE analysis, indicating a high level of purity.
Synonyms

Hemopexin, Beta-1B-Glycoprotein, HX, Beta-1B-glycoprotein.

Source

Sf9, Baculovirus cells.

Amino Acid Sequence

ADPTPLPPTS AHGNVAEGET KPDPDVTERC SDGWSFDATT LDDNGTMLFF KGEFVWKSHK WDRELISERW KNFPSPVDAA FRQGHNSVFL IKGDKVWVYP PEKKEKGYPK LLQDEFPGIP SPLDAAVECH RGECQAEGVL FFQGDREWFW DLATGTMKER SWPAVGNCSS ALRWLGRYYC FQGNQFLRFD PVRGEVPPRY PRDVRDYFMP CPGRGHGHRN GTGHGNSTHH GPEYMRCSPH LVLSALTSDN HGATYAFSGT HYWRLDTSRD GWHSWPIAHQ WPQGPSAVDA AFSWEEKLYL VQGTQVYVFL TKGGYTLVSG YPKRLEKEVG TPHGIILDSV DAAFICPGSS RLHIMAGRRL WWLDLKSGAQ ATWTELPWPH EKVDGALCME KSLGPNSCSA NGPGLYLIHG PNLYCYSDVE KLNAAKALPQ PQNVTSLLGC THHHHHHH.

Product Science Overview

Introduction

Hemopexin is a plasma glycoprotein known for its high affinity for binding heme, a component of hemoglobin. It plays a crucial role in the body’s defense mechanism against heme-induced oxidative stress and inflammation. The recombinant form of hemopexin, produced in Sf9 insect cells, has garnered significant attention for its potential therapeutic applications.

Structure and Function

Hemopexin is composed of a single 60-kDa peptide chain . It binds heme with exceptional affinity, forming a 1:1 complex at low heme concentrations and a 2:1 complex at higher concentrations . This binding is pivotal in conditions such as malaria, sickle cell disease, thalassemia, hemorrhage, and hemorrhagic stroke .

Recombinant Production

The recombinant production of hemopexin involves the use of Sf9 insect cells, a widely used system for producing recombinant proteins. This method ensures high yield and purity of the protein, making it suitable for therapeutic applications. The recombinant hemopexin produced in Sf9 cells retains the structural and functional characteristics of the native protein, including its high affinity for heme binding .

Therapeutic Potential

Hemopexin’s ability to scavenge free heme makes it a promising candidate for treating conditions associated with hemolysis and heme-induced toxicity. Studies have shown that recombinant hemopexin can effectively bind heme, reducing its pro-inflammatory and oxidative effects . This property is particularly beneficial in managing hemolytic disorders and conditions involving excessive heme release.

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Related Products

Hemopexin Human
Hemopexin Human Recombinant
Cat. No.
BT20413
Source
Escherichia Coli.
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