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Hemoglobin subunit zeta (HBZ) is part of the globin family. Hemoglobin Zeta is alpha-like hemoglobin. The HBZ polypeptide is synthesized in the yolk sac of the early embryo, while alpha-globin is produced throughout fetal and adult life.

SRGN is identified as a hematopoietic cell granule proteoglycan. Proteoglycans stored in the secretory granules of various hematopoietic cells also hold a protease-resistant peptide core, and is vital for neutralizing hydrolytic enzymes. SRGN is related to the macromolecular complex of granzymes and perforin that acts as a intermediary of granule-mediated apoptosis.

Secreted frizzled-related protein 2 (SFRP2) belongs to the SFRP family which contains a cysteine-rich domain homologous to the putative Wnt-binding site of Frizzled proteins. SFRP2 function as soluble modulators of Wnt signaling. Methylation of SFRP2 is a possible marker for the existence of colorectal cancer.

Secreted frizzled-related protein 4 (SFRP4) belongs to the SFRP family which contains a cysteine-rich domain homologous to the putative Wnt-binding site of Frizzled proteins. SFRPs serve as soluble modulators of Wnt signaling. SFRP4 may serve as a regulator of adult uterine morphology and function. SFRP4 increases apoptosis during ovulation possibly via modulation of FZ1/FZ4/WNT4 signaling. SFRP4 also has phosphaturic effects by specifically inhibiting sodium-dependent phosphate uptake. SFRP4 is expressed in proliferative endometrium and several types of ovarian, endometrial and Brest tumors. SFRP4 is expressed in mesenchymal cells and in cardiomyocytes. SFRP4 expression in ventricular myocardium correlates with apoptosis related gene expression. SFRP4 is up-regulated in failing myocardium.

The gamma globin genes which are HBG1 and HBG2, usually expressed in the fetal liver, spleen and bone marrow. 2 gamma chains together along with 2 alpha chains comprise fetal hemoglobin (HbF) which is normally replaced by mature hemoglobin (HbA) at birth. Gamma chain production continues into adulthood in several beta-thalassemias and linked situations. The two types of gamma chains differ at residue 136 where glycine is found in the G-gamma product (HBG2) and alanine is found in the A-gamma product (HBG1). The former is predominant at birth.

Neuroglobin, 151 amino acid residue protein, mainly expressed in vertebrate brain and retina, is a recently identified member of the globin superfamily. Augmenting O (2) supply, neuroglobin promotes survival of neurons upon hypoxic injury, potentially limiting brain damage. Moreover, neuroglobin may be a novel oxidative stress-responsive sensor for signal transduction in the brain. Neuroglobin expression is increased by neuronal hypoxia in vitro and focal cerebral ischemia in vivo, and neuronal survival after hypoxia is reduced by inhibiting neuroglobin expression with an antisense oligodeoxynucleotide and enhanced by neuroglobin overexpression.

Alpha-hemoglobin stabilizing protein (AHSP) is an erythroid-specific protein that acts as a chaperone to prevent the aggregation of A-hemoglobin during normal erythroid cell development. AHSP specifically protects free A-hemoglobin from precipitation in live cells and in solution. AHSP is expected to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia. Furthermore, AHSP promotes alpha globin chain stability in human erythropoiesis. In addition, the AHSP stabilizes the alpha-Hb chain, thus avoiding its precipitation and its ability to generate ROS, which is implicated in cell death. AHSP is expressed in blood and bone marrow. AHSP subunit is a monomer, it forms a heterodimer with free alpha-hemoglobin. On the other hand, AHSP does not bind beta-hemoglobin nor alpha2beta2 hemoglobin A. AHSP is downregulated in TSEs (transmissible spongiform encephalopathies).

The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.

Hemoglobin subunit gamma-2 (HBG2), is a member of the globin family. HBG2 belongs to the fetal hemoglobin subunit, which comprised of two alpha chains organized with 2 gamma chains. HBG2 Amplified fetal hemoglobin production in adults and improve the clinical severity of sickle cell disease and beta-thalassemia major.

Hemoglobin Subunit Zeta (Hbz) or Hba-x is a alpha-like hemoglobin and part of the globin family. The protein is expressed and produced in the the yolk sac in early stages of embryonic development. Hemoglobin subunit zeta has 2 pseudogenes and 5 functional genes.

Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is widely used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.

Cytoglobin is a globin protein found in the brain and is mainly utilized in marine mammals. CYGB acts a a protector under conditions of hypoxia. The suggested function of CYGB is the modulation of oxygen and nitric oxide metabolism or scavenging free radicals within a cell.

Aprotinin inhibits the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin and trypsin. Aprotinin is present in blood and in most tissues, with a high concentration in lung. Aprotinin inhibits pro-inflammatory cytokine release and maintains glycoprotein homeostasis. In platelets, aprotinin reduces glycoprotein loss (e.g., GpIb, GpIIb/IIIa), while in granulocytes it prevents the expression of pro-inflammatory adhesive glycoproteins (e.g., CD11b).

SPARC protein, or secreted protein acidic and rich in cysteine, or osteonectin or basement-membrane protein 40 is a protein that is coded by the SPARC gene in humans. It is a glycoprotein located in bones, that binds to calcium. The osteonectin is secreted from osteoblasts cells when boas are formed, mineralized and promotes the formation and creation of mineral crystals. Asides from calcium, it has been shown that this protein can also bind to collagen.

Secreted Protein Acidic & Rich in Cysteine (SPARC) protein is coded by the SPARC gene in humans. SPARC is a glycoprotein located in bones that binds to calcium. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, mainly in areas of tissue morphogenesis and remodelling. Asides from calcium, SPARC can also bind to collagen.

HBA2 is a member of the globin family. HBA2 takes part in oxygen transport from the lung to the different peripheral tissues. The coding sequences of HBA2 and HBA1 are equal but have a small difference over the 5' untranslated regions and the introns, and a large difference over the 3' untranslated regions. HbA is constituted from two alpha chains and two beta chains which in standard adult life hold about 97% of the total hemoglobin; alpha chains associate with delta chains to create HbA-2 that with HbF (fetal hemoglobin) form the remaining 3% of adult hemoglobin. Alpha thalassemia is caused by removal of each of the alpha genes or removal of both HBA2 and HBA1; nondeletion alpha thalassemias has also been reported.

Myoglobin is a member of the globin superfamily and can be found in skeletal and cardiac muscles. It is a haemoprotein that contributs to intracellular oxygen storage and transcellular facilitated diffusion of oxygen. Myoglobin has a single-chain globular structure of 153 amino acids, containing a heme prosthetic group (iron-containing porphyrin) in the core around which the remaining apoprotein folds. Myoglobin has 8 alpha helices and a hydrophobic core. Myoglobin’s molecular weight is 16.7 kDa, and it is the primary oxygen-carrying pigment of muscle tissues. The binding of oxygen in myoglobin is different from the cooperative oxygen binding in hemoglobin, since positive collaboration is a property of multimeric/oligomeric proteins only. Instead, the binding of oxygen by myoglobin is uninfluenced by the oxygen pressure in the surrounding tissue. Myoglobin is frequently referred to as having an "instant binding tenacity" to oxygen given its hyperbolic oxygen dissociation curve. Different organisms are able to hold their breaths longer due to high concentrations of myoglobin in their muscle cells. Myoglobin is responsible for the pigments that make meat red. The color of the meat is partly determined by the charge of the iron atom in myoglobin and the oxygen attached to it. Myoglobin is found in Type I muscle, Type II A and Type II B, but it is mostly deemed that myoglobin is not found in smooth muscle. Myoglobin is discharged from damaged muscle tissue (rhabdomyolysis), which contains very high concentrations of myoglobin. Even though the released myoglobin is filtered by the kidneys, it is toxic to the renal tubular epithelium and thus may cause acute renal failure.

Frizzled-Related Protein (FRZB) is a secreted protein which is involved in the regulation of bone development. FRZB gene defects cause the female-specific osteoarthritis (OA) susceptibility. sFRPS (Soluble frizzled-related proteins) serve as modulators of Wnt signaling by way of direct interaction with Wnts. sFRPS have a role in regulating cell growth and differentiation in specific cell types. SFRP3/FRZB is involved in limb skeletogenesis. FRZB regulates chondrocyte maturation and long bone development.

Obestatin is a hormone that is produced in the cells lining the stomach and small intestine of several mammals including humans; it drastically reduces appetite in mice and is expected to do the same in humans. Obestatin is a peptide hormone - a relatively small protein. It is encoded by the same gene that also encodes ghrelin, a peptide hormone that increases appetite. The protein produced by that gene breaks into two smaller peptides, ghrelin and obestatin. Ghrelin is an endogenous ligand for the growth hormone secretagogue receptor and is involved in regulating growth hormone release. Ghrelin is derived from a preprohormone called preproghrelin, which also generates a second peptide called obestatin. Ghrelin is an endogenous ligand for the orphan G protein-coupled receptor GPR39 and is involved in satiety and decreased food intake.

SecB, a significant chaperone that takes part in protein export, binds various ligands rapidly with high affinity and low specificity. SecB plays an important role during protein export through the general secretory pathway by modulating the partitioning of precursors between folding or aggregation and delivery to the membrane-bound translocation apparatus. SecB has the potential to take part in functions outside of export acting as a universal nonspecific chaperone to provide buffering capacity of the nonnative state of proteins in the cytosolic pool.

Frizzled-4, also known as FZD4 is a 7 ­transmembrane glycoprotein which belongs to the Frizzled family within the G-protein coupled receptor superfamily. FZD4 acts as a positive regulator of the Wingless type MMTV integration site signaling pathway. These pathways appear to include interactions with G-proteins. FZD4 is implicated in transduction as well as intercellular transmission of polarity information in the course of tissue morphogenesis and differentiated tissues.

Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.