globin

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.

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.

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

Cytoglobin is a ubiquitously globin protein that belongs to the globin family. The highest expressed in heart, stomach, bladder and small intestine. CYGB acts a protector under conditions of oxidative stress. CYGB may be involved in intracellular oxygen storage or transfer, modulates oxygen and nitric oxide metabolism or scavenging free radicals within a cell.

Myoglobin(MB) is a cytoplasmic protein expressed in myocytes of the heart and skeletal muscle that reversibly binds oxygen. It belongs to the globin family. Functions of myoglobin include oxygen storage and transport, as well as scavenging of NO and reactive oxygen species. MB serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. Myoglobin also serves as a sensitive marker for muscle injury resulting from cardiac infarction. Surprisingly, mice in which myoglobin has been removed by gene targeting are able to perform extensive exercise and respond normally to hypoxic challenge.

Haptoglobin Protein, Human, Recombinant (C-His) is expressed in HEK293 mammalian cells with C-6xHis tag. The predicted molecular weight is 16 and 40-75 KDa and the accession number is P00738.

Mammaglobin-A/SCGB2A2 Protein, Human, Recombinant (GST) is expressed in E. coli.

Neuroglobin Protein, Human, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 32.9 kDa and the accession number is Q9NPG2.

Myoglobin Protein, Mouse, Recombinant (E. coli, His & Myc) is expressed in E. coli.

May have a protective function during conditions of oxidative stress. May be involved in intracellular oxygen storage or transfer. Plays a role in the development of liver fibrosis. Has a peroxidase activity.

Uteroglobin Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 9.2 kDa and the accession number is P11684.

Haptoglobin Protein, Human, Recombinant (N-His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 35 KDa and the accession number is P00738.

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

Uteroglobin Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 9.8 kDa and the accession number is Q06318.

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.

Haptoglobin Protein, Mouse, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 40.9 kDa and the accession number is Q61646.

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.

Haptoglobin Protein, Rat, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 38.1 kDa and the accession number is A6IZ24.

Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. Myoglobin Protein, Mouse, Recombinant (His & Myc) is expressed in HEK293 mammalian cells with N-10xHis and C-Myc tag. The predicted molecular weight is 21.9 kDa and the accession number is P04247.

SCGB2A1 represented a novel, prognostic factor for CRC, and that expression of SCGB2A1 correlated with chemoresistance, radioresistance and cancer cell stemness. SCGB2A1 is a top differentially expressed gene in all major histological types of ovarian cancers and may represent a novel and attractive target for the immunotherapy of patients harbouring recurrent disease resistant to chemotherapy.

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.

DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolytic activity is essential for the survival of cells at elevated temperatures. It can degrade IciA, Ada, casein, globin and PapA. DegP shares specificity with DegQ. DegP is also involved in the biogenesis of partially folded outer-membrane proteins (OMP).