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TMPH-01432
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HMOX1 Protein, Human, Recombinant (His)
HMOX1,Heme oxygenase 1
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Human
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E. coli
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Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis. HMOX1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHi... |
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TMPH-00793
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FtnA Protein, Helicobacter pylori, Recombinant (E. coli, His)
Bacterial non-heme ferritin,ftnA
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Helicobacter pylori
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E. coli
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Iron-storage protein. |
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TMPH-00792
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FtnA Protein, Helicobacter pylori, Recombinant (His)
Bacterial non-heme ferritin,ftnA
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Helicobacter pylori
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Baculovirus Insect Cells
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Iron-storage protein. |
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TMPH-02702
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HEBP1 Protein, Mouse, Recombinant (His)
Hebp1,Heme-binding protein 1,p22HBP
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Mouse
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E. coli
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HEBP1 Protein, Mouse, Recombinant (His) is expressed in E. coli. |
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TMPH-02703
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HEBP1 Protein, Mouse, Recombinant (hFc)
Hebp1,p22HBP,Heme-binding protein 1
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Mouse
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HEK293 Cells
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HEBP1 Protein, Mouse, Recombinant (hFc) is expressed in HEK293. |
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TMPJ-00817
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HO-1 Protein, Human, Recombinant
HO,HMOX1,HO-1,Heme Oxygenase 1,HO1
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Human
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E. coli
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Heme Oxygenase 1 (HO-1) is an enzyme in endoplasmic reticulum that belongs to the heme oxygenase family. HO-1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is subsequently converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HO-1 is found in the spleen, where senescent erythrocytes are sequestrated and destroyed. HO-1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy me... |
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TMPH-00265
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Ferrochelatase, mitochondrial Protein, Bovine, Recombinant (His & Myc & SUMO)
Ferrochelatase, mitochondrial,Protoheme ferro-lyase...
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Bovine
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E. coli
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Catalyzes the ferrous insertion into protoporphyrin IX. Ferrochelatase, mitochondrial Protein, Bovine, Recombinant (His & Myc & SUMO) is expressed in E. coli expression system with N-10xHis-SUMO and C-Mycd tag. The predicted molecular weight is 58.1 kDa and the accession number is P22600. |
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TMPH-01332
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Ferrochelatase Protein, Human, Recombinant (His & Myc)
Ferrochelatase, mitochondrial,Heme synthase,Proto
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Human
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E. coli
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Catalyzes the ferrous insertion into protoporphyrin IX. Ferrochelatase Protein, Human, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 49.6 kDa and the accession number is P22830. |
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TMPJ-00801
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UQCRH Protein, Human, Recombinant (GST)
Complex III subunit 6,Ubiquinol-cytochrome c reductase compl...
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Human
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E. coli
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Cytochrome b-c1 complex subunit 6, mitochondrial (UQCRH) belongs to the UQCRH/QCR6 family, it is a subunit of the respiratory chain protein Ubiquinol Cytochrome c Reductase. This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. UQCRH may mediate formation of the complex between cytochromes c and c1. It may mediate formation of the complex between cytochromes c and c1. |
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TMPH-03751
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CYBB Protein, Human, Recombinant (His)
NADPH oxidase 2,Heme-binding membrane glycoprotein ...
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Human
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E. coli
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Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes. It participates in the regulation of cellular pH and is blocked by zinc. |
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TMPH-03364
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RBCK1 Protein, Rat, Recombinant (His & Myc)
Heme-oxidized IRP2 ubiquitin ligase 1 homolog,RING-...
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Rat
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E. coli
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RBCK1 Protein, Rat, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 65.1 kDa and the accession number is Q62921. |
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TMPY-00367
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Chemerin/RARRES2 Protein, Mouse, Recombinant (His)
AI303516,retinoic acid receptor responder (tazarotene induce...
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Mouse
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HEK293 Cells
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Chemerin/RARRES2 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 17.4 kDa and the accession number is Q9DD06. |
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TMPJ-01292
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Chemerin/RARRES2 Protein, Human, Recombinant (His)
RAR-responsive protein TIG2,RARRES2,Chemerin,Tazaro...
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Human
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HEK293 Cells
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Retinoic acid receptor responder protein 2(RARRES2) is a secreted protein that in humans is encoded by the RARRES2 gene. It is highly expressed in skin, also found in pancreas, liver, spleen, prostate, ovary, small intestine and colon. It is a chemoattractant protein that acts as a ligand for the G protein-coupled receptor CMKLR1. RARRES2 is secreted in an inactive form as prochemerin and is activated through cleavage of the C-terminus by inflammatory and coagulation serine proteases. It is thou... |
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TMPY-04143
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Chemerin/RARRES2 Protein, Mouse, Recombinant (hFc)
0610007L05Rik,retinoic acid receptor responder (tazarotene i...
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Mouse
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HEK293 Cells
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Chemerin/RARRES2 Protein, Mouse, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 42.6 kDa and the accession number is Q9DD06. |
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TMPY-02707
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PAH Protein, Human, Recombinant (415 Asn/Asp, His)
phenylalanine hydroxylase,PH,PKU1,PKU
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Human
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Baculovirus Insect Cells
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PAH (phenylalanine hydroxylase), also known as PH, belongs to the biopterin-dependent aromatic amino acid hydroxylase family. It contains 1 ACT domain, N-terminal region of PAH is thought to contain allosteric binding sites for phenylalanine and to constitute an "inhibitory" domain that regulates the activity of a catalytic domain in the C-terminal portion of the molecule. In humans, PAH is expressed both in the liver and the kidney, and there is some indication that it may be differentially reg... |
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TMPK-00545
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HPX Protein, Cynomolgus, Recombinant (His)
Hemopexin,Hpx,Hpxn
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Cynomolgus
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HEK293 Cells
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Hemopexin (HPX) serves as scavenger and transporter of toxic plasma heme to the liver. HPX is formed by two four-bladed beta-propeller domains, resembling two thick disks that lock together at a 90 degrees angle. The heme is bound between the two beta-propeller domains in a pocket formed by the interdomain linker peptide.HPX, acting not only as a heme carrier but also displaying transient heme-based ligand binding and (pseudo-)enzymatic properties, could be considered a 'chronosteric' heme-prote... |
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TMPH-03561
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lsdB Protein, S. aureus, Recombinant (His & SUMO)
Fur-regulated protein B,Iron-regulated surface determinant p...
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Staphylococcus aureus
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E. coli
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Cell wall-anchored surface receptor that extracts heme from oxidized metHb to enable growth on hemoglobin as a sole iron source. Rapidly extracts heme from hemoglobin and transfers it to IsdA or IsdC, which then relays it to the membrane transporter/IsdEF for internalization. Promotes also resistance to hydrogen peroxide and killing by neutrophils. lsdB Protein, S. aureus, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is ... |
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TMPJ-00806
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HMBS Protein, Human, Recombinant (His)
Pre-Uroporphyrinogen Synthase,PBG-D,Hydroxymethylbilane Synt...
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Human
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HEK293 Cells
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Porphobilinogen Deaminase (HMBS) is a member of the HMBS family. PBGD is the third enzyme of the heme biosynthetic pathway and catalyzes the head to tail condensation of four porphobilinogen molecules into the linear hydroxymethylbilane. HMBS is involved in the production of heme, which is important for all of the body's organs, although it is most abundant in the blood, bone marrow, and liver. In addition, Heme is an essential component of iron-containing proteins called hemoproteins, including... |
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TMPJ-00788
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UROD Protein, Human, Recombinant (His)
UPD,UROD,Uroporphyrinogen Decarboxylase,URO-D
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Human
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E. coli
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Uroporphyrinogen decarboxylase (UROD), is an enzyme of the heme biosynthetic pathway which belongs to the uroporphyrinogen decarboxylase family. This enzyme is responsible for catalyzing the conversion of uroporphyrinogen to coproporphyrinogen through the removal of four carboxymethyl side chains. UROD is a homodimeric enzyme that catalyzes the fifth step in heme biosynthesis: the elimination of carboxyl groups from the four acetate side chains of uroporphyrinogen III to yield coproporphyrinogen... |
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TMPJ-01147
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Cld Protein, Dechloromonas aromatica, Recombinant (His)
Daro_2580,Chlorite O(2)-lyase,Chlorite dismutase,Cld
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Dechloromonas aromatica
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E. coli
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Chlorite dismutase (Cld) found in prokaryotic organisms, also known as Chlorite O2-lyase, is a b-type heme containing enzyme that catalyzes the reduction of chlorite into chloride plus dioxygen. The subunit of chlorite dismutase consists of a heme free N-terminal and a heme b containing C-terminal ferredoxin-like fold with high structural homology to the dye-decolorizing peroxidases (DyPs). The physiological role of Cld in prokaryote has been shown that some microorganisms can use perchlorate or... |
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TMPH-01748
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CYPOR Protein, Human, Recombinant (GST)
NADPH--cytochrome P450 reductase,P450R,CPR,POR,CYPOR
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Human
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E. coli
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This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. CYPOR Protein, Human, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 102.9 kDa and the accession number is P16435. |
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TMPJ-00723
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CYB5A Protein, Human, Recombinant (His)
CYB5,Cytochrome b5,Microsomal Cytochrome b5 Type A,CYB5A,MCB...
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Human
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E. coli
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Cytochrome b5 (CYB5A) is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. CYB5A contains one cytochrome b5 heme-binding domain and has two isoforms produced by alternative splicing. Isoform 1 is a sngle-pass membrane protein. Isoform 2 is located in cytoplasm. The defects in CYB5A can result in type IV hereditary methemoglobinemia. |
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TMPY-02519
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BLVRB Protein, Human, Recombinant (His)
HEL-S-10,biliverdin reductase B,FLR,BVRB,SDR43U1
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Human
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E. coli
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Biliverdin reductase (hBVR) is a serine/threonine kinase that catalyzes reduction of the heme oxygenase (HO) activity product, biliverdin, to bilirubin. BVR consists of an N-terminal dinucleotide-binding domain (Rossmann-fold) and a C-terminal domain that contains a six-stranded β-sheet that is flanked on one face by several α-helices. The C-terminal and N-terminal domains interact extensively, forming the active site cleft at their interface. Biliverdin reductase (BVR) catalyzes the last step i... |
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TMPH-02617
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COX5A Protein, Mouse, Recombinant (His & SUMO)
Cytochrome c oxidase subunit 5A, mitochondrial,COX5A,Cytochr...
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Mouse
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E. coli
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Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over t... |
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TMPH-03128
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TSPO Protein, Pig, Recombinant (His & Myc & SUMO)
TSPO,Peripheral-type benzodiazepine receptor,Translocator pr...
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Sus scrofa (Pig)
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E. coli
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Promotes the transport of cholesterol across mitochondrial membranes and may play a role in lipid metabolism, but its precise physiological role is controversial. It is apparently not required for steroid hormone biosynthesis. Can bind protoporphyrin IX and may play a role in the transport of porphyrins and heme. Was initially identified as peripheral-type benzodiazepine receptor; can also bind isoquinoline carboxamides. TSPO Protein, Pig, Recombinant (His & Myc & SUMO) is expressed in E. coli e... |
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TMPJ-00470
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CYB5B Protein, Human, Recombinant (His)
Cytochrome b5 outer mitochondrial membrane isoform,OMB5
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Human
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HEK293 Cells
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Cytochrome b5 type B (CYB5B) is a membrane of the cytochrome b5 family. It contains 1 cytochrome b5 heme-binding domain. Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. In the mitochondrion of eukaryotes and in aerobic prokaryotes, cytochrome b is a component of respiratory chain complex III also known as the bc1 complex or ubiquinol-cytochrome c reductase. |
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TMPH-02661
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Frataxin/FXN Protein, Mouse, Recombinant (E. coli, His)
Fxn,Frataxin, mitochondrial
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Mouse
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E. coli
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Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization. Modulates the RNA-binding activit... |
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TMPH-02660
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Frataxin/FXN Protein, Mouse, Recombinant (His)
Fxn,Frataxin, mitochondrial
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Mouse
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P. pastoris (Yeast)
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Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization. Modulates the RNA-binding activit... |
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TMPH-03371
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Transferrin Protein, Rat, Recombinant (His & KSI)
Tf,Beta-1 metal-binding globulin,Liver regeneration-related ...
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Rat
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E. coli
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Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. Transferrin Protein, Rat, Recombinant (His & KSI) is expressed in E. coli expression system with N-6xHis-KSI tag. The predicted molecular weight ... |
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TMPJ-01142
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CDO1 Protein, Human, Recombinant (His)
CDO-I,CDO,Cysteine Dioxygenase Type I,CDO1,Cysteine Dioxygen...
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Human
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E. coli
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Cysteine Dioxygenase Type 1 (CDO1) is a mammalian non-heme iron enzyme that belongs to the cysteine dioxygenase family. CDO1 is highly expressed in the liver and placenta, and has a low expression in heart, brain and pancreas. CDO1 can also be detected in hepatoblastoma HepG2 cells. CDO1 catalyzes the conversion of L-cysteine to cysteine sulfinic acid by incorporation of dioxygen. CDO1 is a vital regulator of cellular cysteine concentrations and has an essential role in maintaining the hepatic c... |
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TMPJ-00830
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UROIIIS Protein, Human, Recombinant (His)
Hydroxymethylbilane Hydrolyase [Cyclizing],Uroporphyrinogen-...
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Human
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E. coli
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Uroporphyrinogen-III Synthase is an enzyme which belongs to the uroporphyrinogen-III synthase family. Uroporphyrinogen-III Synthase is ubiquitous and it is involved in Porphyrin metabolism. Porphyrins act as cofactors for a multitude of enzymes that perform a variety of processes within the cell such as Methionine synthesis (Vitamin B12) or oxygen transport (Heme). Uroporphyrinogen-III Synthase can catalyze cyclization of the linear Tetrapyrrole, Hydroxymethylbilane, to the Macrocyclic Uroporphy... |
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TMPJ-01066
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CYCS Protein, Human, Recombinant (His)
CYC,Cytochrome C,CYCS
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Human
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E. coli
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Cytochrome C (CYCS) is a small heme protein that belongs to the cytochrome c family. It is found loosely associated with the inner membrane of the mitochondrion. Cytochrome C is a highly soluble protein that functions as a central component of the electron transport chain in mitochondria. CYCS transfers electrons between Complexes III (Coenzyme Q - Cyt C reductase) and IV (Cyt C oxidase). CYCS plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic... |
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TMPJ-01055
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HBA1 Protein, Human, Recombinant (His)
α-globin,Hemoglobin subunit alpha,HBH,HBA-T3,Alpha-globin,He...
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Human
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E. coli
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Hemoglobin subunit alpha 1 (HBA1), also known as α2β2, is a hetero-tetramer consisting of two α and two β subunits held together by non-covalent interactions. Each subunit contains a heme group with an iron atom in the Fe2+ state. Cooperativity of Hemoglobin (Hb) in binding with O2 and allosteric regulatory binding properties with CO2, H+, Cl−, and 2,3-DPG (2,3-bisphosphoglycerate) are based on subunit interactions. HBA1 is the most common type of Hb in adult humans, which mediates the transport... |
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TMPY-02464
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Catalase/CAT Protein, Human, Recombinant (His)
catalase
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Human
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Baculovirus Insect Cells
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Catalase is a ubiquitously expressed enzyme that catalyzes the decomposition of hydrogen peroxide to water and oxygen. It is a tetramer of four polypeptides chains containing four porphyrin heme groups that allow the enzyme to react with the hydrogen peroxide. The optimum PH of human catalase is approximately 7 and the optimum temperature is at 37 degree. Both the PH optimum and temperature for other catalases varies depending on the species. Catalase can be inhibited by a flux of O2-generated i... |
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