Gamma chains make up the fetal hemoglobin F, in combination with alpha chains. Hemoglobin subunit gamma-1/HBG1 Protein, Human, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 23.0 kDa and the accession number is P69891.

Involved in oxygen transport from the lung to the various peripheral tissues. Hemoglobin subunit delta/HBD Protein, Human, Recombinant (GST & His) is expressed in E. coli expression system with N-6xHis-GST tag. The predicted molecular weight is 47.5 kDa and the accession number is P02042.

AHSP, also known as ERAF, is a conserved mammalian erythroid protein which belongs to the AHSP family. It is expressed in blood and bone marrow. AHSP facilitates the production of Hemoglobin A by stabilizing free α-globin. It rapidly binds to ferrous α with association (k'(AHSP)) and dissociation (k(AHSP)) rate constants of ≈1 μm(-1) s(-1) and .2 s(-1), respectively, at pH 7.4 at 22 ℃. A small slow phase was observed when AHSP binds to excess ferrous αCO. This slow phase appears to be due to cis to trans prolyl isomerization of the Asp(29)-Pro(3) peptide bond in wild-type AHSP because it was absent when αCO was mixed with P3A and P3W AHSP, which are fixed in the trans conformation. This slow phase was also absent when met(Fe(3+))-α reacted with wild-type AHSP, suggesting that met-α is capable of rapidly binding to either Pro(3) conformer. Both wild-type and Pro(3)-substituted AHSPs drive the formation of a met-α hemichrome conformation following binding to either met- or oxy(Fe(2+))-α. The dissociation rate of the met-α·AHSP complex (k(AHSP) ≈ .2 s(-1)) is ～1-fold slower than that for ferrous α·AHSP complexes, resulting in a much higher affinity of AHSP for met-α. Thus, in vivo, AHSP acts as a molecular chaperone by rapidly binding and stabilizing met-α hemichrome folding intermediates. The low rate of met-α dissociation also allows AHSP to have a quality control function by kinetically trapping ferric α and preventing its incorporation into less stable mixed valence Hemoglobin A tetramers. Reduction of AHSP-bound met-α allows more rapid release to β subunits to form stable fully, reduced hemoglobin dimers and tetramers.

HBA1 Protein, Mouse, Recombinant (His) is expressed in E. coli.

Hemoglobin subunit theta-1 is a protein that in humans is encoded by the HBQ1 gene. Theta-globin mRNA is originally found in human fetal erythroid tissue but not in adult erythroid or other nonerythroid tissue. Theta-1 is a member of the human alpha-globin gene cluster that includes five functional genes and two pseudogenes. Research supports a transcriptionally active role for the gene and a functional role for the peptide in specific cells, possibly those of early erythroid tissue. Hemoglobin has a quaternary structure characteristically composed of many multi-subunit globular proteins. Most of the amino acids in hemoglobin form alpha helices, connected by short non-helical segments. Hydrogen bonds stabilize the helical sections inside this protein, causing attractions within the molecule, folding each polypeptide chain into a specific shape. Hemoglobin's quaternary structure comes from its four subunits in roughly a tetrahedral arrangement.

Hemoglobin Subunit Zeta (HBZ) is a member of the Globin family. The zeta chain is an alpha-type chain of mammalian embryonic Hemoglobin that is synthesized primarily in the yolk sac of the early embryo, while alpha-globin is produced throughout fetal growth and adult life. The HBZ gene consists of five functional genes and two pseudogenes, the order of genes is 5-zeta-pseudozeta-mu-pseudoalpha-1-alpha-2-alpha-1-theta-1-3.

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 of oxygen and carbon dioxide in the blood. In recent years, Hb α and β chains have been found co-expressed in alveolar cells, mesangial cells of the kidney, retinal ganglion cells, hepatocytes and neurons. Endothelial and peripheral catecholaminergic cells express exclusively the α chain, while macrophages present the β chain only.

Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation. Leghemoglobin A Protein, Phaseolus vulgaris, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 22.9 kDa and the accession number is P02234.

Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation. Leghemoglobin Lb120-8 Protein, Pisum sativum, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 19.9 kDa and the accession number is Q9SAZ1.

Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation.

The hemoglobin (Hb) scavenger receptor, CD163, is a macrophage-specific protein and the upregulated expression of this receptor is one of the major changes in the macrophage switch to alternative activated phenotypes in inflammation. Accordingly, a high CD163 expression in macrophages is a characteristic of tissues responding to inflammation. CD163 Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 111.4 kDa and the accession number is Q86VB7-1.

Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria. Lys-gingipain Protein, Porphyromonas gingivalis, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 56.6 kDa and the accession number is B2RLK2.

Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria. Lys-gingipain 381 Protein, Porphyromonas gingivalis, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 44.8 kDa and the accession number is P72194.

Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria. Lys-gingipain HG66 Protein, Porphyromonas gingivalis, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 46.4 kDa and the accession number is P72197.

During the asexual blood stage, catalyzes the initial cleavage of native host hemoglobin (Hb) resulting in Hb denaturation; specifically cleaves between Phe-33 and Leu-34 of Hb alpha-chain. Digestion of host Hb is an essential step which provides the parasite with amino acids for protein synthesis, and regulates osmolarity (Probable). Plasmepsin-1 Protein, Plasmodium falciparum, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 41.0 kDa and the accession number is P39898.

During the asexual blood stage, participates in initial cleavage of native host hemoglobin (Hb) resulting in Hb denaturation. May cleave preferentially denatured hemoglobin that has been cleaved by PMI. Digestion of host Hb is an essential step which provides the parasite with amino acids for protein synthesis, and regulates osmolarity (Probable). Plasmepsin-2 Protein, Plasmodium falciparum, Recombinant (E. coli, His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 41.9 kDa and the accession number is P46925.

The hemoglobin (Hb) scavenger receptor, CD163, is a macrophage-specific protein and the upregulated expression of this receptor is one of the major changes in the macrophage switch to alternative activated phenotypes in inflammation. Accordingly, a high CD163 expression in macrophages is a characteristic of tissues responding to inflammation. CD163 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 109.53 kDa and the accession number is Q2VLH6-1.

The hemoglobin (Hb) scavenger receptor, CD163, is a macrophage-specific protein and the upregulated expression of this receptor is one of the major changes in the macrophage switch to alternative activated phenotypes in inflammation. Accordingly, a high CD163 expression in macrophages is a characteristic of tissues responding to inflammation. CD163 Protein, Human, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 111.4 kDa and the accession number is Q86VB7-1.

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 41.6 kDa and the accession number is P0C7J5.

Bisphosphoglycerate Mutase (BPGM) is a member of the Phosphoglycerate Mutase family and BPG-Dependent PGAM subfamily. BPGM is a multifunctional enzyme. BPGM catalyzes 2,3-DPG synthesis via its synthetase activity, and 2,3-DPG degradation via its phosphatase activity. It also has phosphoglycerate phosphomutase activity. BPGM plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of 2,3-bisphosphoglycerate (2,3-BPG). Deficiency of BPGM increases the affinity of cells for oxygen and result in hemolytic anemia.

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 hemoglobin. Defects in PBGD are the cause of acute intermittent porphyria.

During the asexual blood stage, participates in initial cleavage of native host hemoglobin (Hb) resulting in Hb denaturation. May cleave preferentially denatured hemoglobin that has been cleaved by PMI. Digestion of host Hb is an essential step which provides the parasite with amino acids for protein synthesis, and regulates osmolarity (Probable). Plasmepsin-2 Protein, Plasmodium falciparum, Recombinant (His & Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag. The predicted molecular weight is 40.8 kDa and the accession number is P46925.