This is a 2S seed storage protein.; binds to mammalian chromatin, preventing the normal formation of the kinetochore complex in the centromere and leading to the disruption of mitosis.

This is a 2S seed storage protein.; binds to mammalian chromatin, preventing the normal formation of the kinetochore complex in the centromere and leading to the disruption of mitosis. 2S albumin Protein, Glycine max, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 32.2 kDa and the accession number is P19594.

Weak inhibitor of trypsin. Conglutin-7 Protein, Arachis hypogaea, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 22.0 kDa and the accession number is Q6PSU2.

Lysosome-Associated Membrane Glycoprotein 1 (LAMP1) is a single-pass type I membrane protein belonging to the LAMP family. LAMP1 is expressed largely in the endosome-lysosome membranes of cells.It shuttles between lysosomes, endosomes, and the plasma membrane. LAMP1 functions to present carbohydrate ligands to selectins and it has also been implicated in tumor cell metastasis. It has been proposed LAMP1 can be used as a therapeutic agent for certain cancers, as well as a marker for lysosomal storage disorders and degranulation on lymphocytes such as CD8+ and NK cells. Cell surface LAMP1 and LAMP2 have been shown to promote adhesion of human peripheral blood mononuclear cells(PBMC) to vascular endothelium, therefore they are possibly involved in the adhesion of PBMCs to the site of inflammation.

NCKIPSD is localized exclusively in the cell nucleus. It plays a role in signal transduction and may function in the maintenance of sarcomeres and the assembly of myofibrils into sarcomeres. NCKIPSD also plays an important role in stress fiber formation. NCKIPSD gene is involved in therapy-related leukemia by a chromosomal translocation t(3;11)(p21;q23) that involves this gene and the myeloid/lymphoid leukemia gene. Alternative splicing occurs in this locus and two transcript variants encoding distinct isoforms have been identified. NCKIPSD is an SH3 domain protein. Fas ligand is a cytotoxic effector molecule of T and NK cells which is characterized by an intracellular N-terminal polyproline region that serves as a docking site for SH3 and WW domain proteins. Several previously described Fas ligand-interacting SH3 domain proteins turned out to be crucial for the regulation of storage, expression, and function of the death factor. Recent observations, however, indicate that Fas ligand is also subject to posttranslational modifications including shedding and intramembrane proteolysis.

Iron-storage protein.

Facilitates the accumulation of zinc from the cytoplasm into intracellular vesicles, being a zinc-efflux transporter. May be a major component for providing zinc to insulin maturation and/or storage processes in insulin-secreting pancreatic beta-cells. SLC30A8 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-10xHis tag. The predicted molecular weight is 43.6 kDa and the accession number is Q8IWU4.

FTH1 (ferritin, heavy polypeptide 1) is the heavy subunit of ferritin which is the major intracellular iron storage protein in prokaryotes and eukaryotes. It is composed of 24 subunits of the heavy and light ferritin chains. Variation in ferritin subunit composition may affect the rates of iron uptake and release in different tissues. A major function of ferritin is the storage of iron in a soluble and nontoxic state. Defects in ferritin proteins are associated with several neurodegenerative diseases. FTH1 gene has multiple pseudogenes. Several alternatively spliced transcript variants have been observed, but their biological validity has not been determined. FTH1 stores iron in a soluble, non-toxic, readily available form. It is important for iron homeostasis. It has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. It also plays a role in delivery of iron to cells. FTH1 mediates iron uptake in capsule cells of the developing kidney.

Copper homeostasis protein cutC homolog, also known as CGI-32 and CUTC, is a cytoplasm and nucleus protein which belongs to theCutC family. CUTC may play a role in copper homeostasis. It can bind one Cu1+per subunit. Copper is an essential trace element to life and particularly plays a pivotal role in the physiology of aerobic organisms. Copper is a micronutrient that is required for proper metabolic functioning of most prokaryotic and eukaryotic organisms. To sustain an adequate supply of copper, a cell requires molecular mechanisms that control the metal content to avoid copper toxicity. This toxicity comes primarily from the reactivity of copper, which can lead to the generation of free radicals. In bacteria, two independent systems are responsible for maintaining the balance of copper within the cells ( Cop and Cut family proteins ). The Cut protein family is associated with copper homeostasis and involved in uptake, storage, delivery, and efflux of copper. CutC is a member of the Cut family and is suggested to be involved in efflux trafficking of cuprous ion. CutC is able to respond transcriptionally to copper and to participate in the control of copper homeostasis in E. faecalis.

Phosphorylase b kinase gamma catalytic chain, skeletal muscle isoform, also known as Phosphorylase kinase subunit gamma-1 and PHKG1, is a member of the protein kinase superfamily and CAMK Ser/Thr protein kinase family. PHKG1 is the catalytic member of a 16 subunit protein kinase complex that contains equimolar ratios of 4 subunit types. The complex is a crucial glycogenolytic regulatory enzyme. Muscle glycogenosis caused by phosphorylase kinase (Phk) deficiency may lead to exercise intolerance, weakness and musculatur atrophy. The gene encoding the muscle isoform of the Phk gamma subunit (gamma M) is one of the candidate genes in which mutations responsible for this condition should be sought. Muscle-specific deficiency of Phk causes glycogen storage disease, clinically manifesting in exercise intolerance with early fatiguability, pain, cramps and occasionally myoglobinuria.

Hormone that acts as a blood lipid regulator by regulating serum triglyceride levels. May be involved in the metabolic transition between fasting and refeeding: required to direct fatty acids to adipose tissue for storage in the fed state. According to a report, may act by promoting ANGPTL3 cleavage. According to another study, not required for cleavage of ANGPTL3. ANGPTL8 Protein, Mouse, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 22.5 kDa and the accession number is Q8R1L8.

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.

Nesfatin-1 is a metabolic polypeptide encoded in the N-terminal region of the precursor protein, Nucleobindin2 (NUCB2). Nesfatin-1 is a neuropeptide produced in the hypothalamus of mammals. It participates in the regulation of hunger and fat storage. Nesfatin-1 is also expressed in other areas of the brain, and in pancreatic islets β-cells, gastric endocrine cells and adipocytes. Nesfatin-1 suppresses food intake and can regulate energy metabolism in a Leptin independent manner. Nesfatin-1 may also exert hypertensive roles and modulate blood pressure through directly acting on peripheral arterial resistance.

ANGPTL3 is a secreted glycoprotein that is structurally related to the angiopoietins. Mature human ANGPTL3 contains an N-terminal coiled coil domain and a C‑terminal fibrinogen-like domain. ANGPTL3 is expressed in the liver from early in development through adulthood. Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism. Proposed to play a role in the trafficking of energy substrates to either storage or oxidative tissues in response to food intake. ANGPTL3 Protein, Human, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 26.6 kDa and the accession number is Q9Y5C1.

Hepcidin（HAMP）is a secreted protein that belongs to the hepcidin family.It is expressed in liver, heart and brain. It is involved in the maintenance of iron homeostasis, and it is necessary for the regulation of iron storage in macrophages, and for intestinal iron absorption. The preproprotein is post-translationally cleaved into mature peptides of 20, 22 and 25 amino acids, and these active peptides are rich in cysteines, which form intramolecular bonds that stabilize their beta sheet structures.

Niemann-Pick C1 (NPC1), a host receptor involved in the envelope glycoprotein (GP)-mediated entry of filoviruses into cells, is believed to be a major determinant of cell susceptibility to filovirus infection. Niemann-Pick C1 (NPC1), a membrane protein of lysosomes, is required for the export of cholesterol derived from receptor-mediated endocytosis of LDL. The NPC1 protein is a multipass transmembrane protein whose deficiency causes the autosomal recessive lipid storage disorder Niemann-Pick type C1. NPC1 localizes predominantly to late endosomes and has a dileucine motif located within a small cytoplasmic tail thought to target the protein to this location. Niemann-Pick disease type C1 (NPC1) is a rare progressive neurodegenerative disorder caused by mutations in the NPC1 gene. On the cellular level, NPC1 mutations lead to an accumulation of cholesterol and gangliosides.

Ferritin, light polypeptide (FTL) is the light subunit of the ferritin protein. Ferritin is the major intracellular iron storage protein in prokaryotes and eukaryotes. It is composed of 24 subunits of the heavy and light ferritin chains. Storage of iron in the tissues occurs in the form of ferritin and hemosiderin. The latter originates from ferritin that has undergone intracellular digestion of its protein shell, leaving the iron core. Ferritin and hemosiderin are components of a continuum. Ferritin has been identified in all types of living organisms: animals, plants, molds, and bacteria. Whithin the protein shell of ferritin, iron is first oxidized to the ferric state for storage as ferric oxyhdroxide. Thus, ferritin removes excess iron from the cell sap where it could otherwise participate in peroxidation mechanisms.

Seed storage protein. Canavalin Protein, Canavalia gladiata, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 55.0 kDa and the accession number is P10562.

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May also function as a storage protein or ligandin for parasitotoxic ferriprotoporphyrin IX (hemin). GST Protein, Plasmodium falciparum, Recombinant (His) is expressed in yeast with N-10xHis tag. The predicted molecular weight is 27.3 kDa and the accession number is Q8MU52.

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 is 89.9 kDa and the accession number is P12346.

Involved in vitamin D transport and storage, scavenging of extracellular G-actin, enhancement of the chemotactic activity of C5 alpha for neutrophils in inflammation and macrophage activation. VDB Protein, Mouse, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 53.9 kDa and the accession number is P21614.

Sialidase-1 belongs to the N-acetyl-a neuraminidase family. Sialidase-1 is expressed in many tissues; it is highly expressed in the pancreas, and weakly expressed in the brain. Sialidase-1 is a lysosomal enzyme, which cleaves terminal sialic acid residues from substrates such as glycoproteins and glycolipids. Deficiencies in the human enzyme Sialidase-1 leads to sialidosis, a rare lysosomal storage disease. Sialidase-1 has been shown to interact with Cathepsin A (protective protein), β-galactosidase and N-acetylgalactosamine-6-sulfate sulfatase in a multienzyme complex.

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.

Serpins are the largest and most diverse family of protease inhibitors. Most serpins control proteolytic cascades, certain serpins do not inhibit enzymes, but instead perform diverse functions such as storage (ovalbumin, in egg white), hormone carriage proteins (thyroxine-binding globulin, cortisol-binding globulin) and tumor suppressor genes (maspin). Most inhibitory serpins target chymotrypsin-like serine proteases. These enzymes are defined by the presence of a nucleophilic serine residue in their catalytic site. Some serpins inhibit other classes of protease. A number of such serpins have been shown to target cysteine proteases. These enzymes differ from serine proteases in that they are defined by the presence of a nucleophilic cysteine residue, rather than a serine residue, in their catalytic site.SerpinA12, also known as OL-64, Visceral adipose tissue-derived serine protease inhibitor, Vaspin, Visceral adipose-specific serpin and SERPINA12, is a secreted protein that belongs to the serpin family. SerpinA12 / Vaspin is expressed in visceral adipose tissues. It may modulate insulin action conceivably only in the presence of its yet undefined target proteases in white adipose tissues. SerpinA12 / Vaspin may be the compensatory molecule in the pathogenesis of metabolic syndrome and SerpinA12 / Vaspin recombinant protein or vaspin-mimicking agents such as vaspin analogs, antibodies or small molecule agents may be the link to drug discovery and development.

Facilitates the accumulation of zinc from the cytoplasm into intracellular vesicles, being a zinc-efflux transporter. May be a major component for providing zinc to insulin maturation and/or storage processes in insulin-secreting pancreatic beta-cells. SLC30A8 Protein, Mouse, Recombinant (His) is expressed in E. coli expression system with N-10xHis tag. The predicted molecular weight is 43.0 kDa and the accession number is Q8BGG0.

Involved in vitamin D transport and storage, scavenging of extracellular G-actin, enhancement of the chemotactic activity of C5 alpha for neutrophils in inflammation and macrophage activation. VDB Protein, Mouse, Recombinant (E. coli, His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 57.4 kDa and the accession number is P21614.

β Galactosidase is a lysosomal β Galactosidase that hydrolyzes the terminal β Galactose from Ganglioside and Keratan sulfate. In lysosome, the mature β Galactosidase protein associates with Cathepsin A and Neuraminidase 1 to form the lysosomal multienzyme complex . An alternative splicing at the RNA level of β Galactosidase results a catalytically inactive β Galactosidase that plays an important role in vascular development. Defects of β-galactosidase (GLB1) are the cause of diseases like GM1-gangliosidosis which is a lysosomal storage disease and Morquio Syndrome B that cause patients to have abnormal elastic fibers. More than 100 mutations have been identified for β Galactosidase, which result in different residual activities of the mutant enzymes and a spectrum of symptoms in the two related diseases.

ANGPTL3 is a secreted glycoprotein that is structurally related to the angiopoietins. Mature human ANGPTL3 contains an N-terminal coiled coil domain and a C‑terminal fibrinogen-like domain. ANGPTL3 is expressed in the liver from early in development through adulthood. Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism. Proposed to play a role in the trafficking of energy substrates to either storage or oxidative tissues in response to food intake. ANGPTL3 Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 26.6 kDa and the accession number is Q9Y5C1.

Protein Z-dependent protease inhibitor, also known as PZ-dependent protease inhibitor, SERPINA1 and ZPI, is a secreted protein that belongs to the serpin family. It is expressed by the liver and secreted in plasma. SERPINA1 / Serpin-A1 inhibits factor Xa activity in the presence of protein Z, calcium and phospholipid. Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases (serine protease inhibitors). Over 1 serpins have now been identified, these include 36 human proteins, as well as molecules in plants, fungi, bacteria, archaea and certain viruses. Serpins are the largest and most diverse family of protease inhibitors. Most serpins control proteolytic cascades, certain serpins do not inhibit enzymes, but instead perform diverse functions such as storage (ovalbumin, in egg white), hormone carriage proteins (thyroxine-binding globulin, cortisol-binding globulin) and tumor suppressor genes (maspin). Most inhibitory serpins target chymotrypsin-like serine proteases. These enzymes are defined by the presence of a nucleophilic serine residue in their catalytic site. Some serpins inhibit other classes of protease. A number of such serpins have been shown to target cysteine proteases. These enzymes differ from serine proteases in that they are defined by the presence of a nucleophilic cysteine residue, rather than a serine residue, in their catalytic site.

Iron-storage protein.