light

Expression system: Baculovirus Insect Cells
Length: 72-239, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 89-240, Partial
Activity: ELISA

LIGHT TNFSF14 Protein, Human, Recombinant (rFc) is expressed in HEK293 mammalian cells with rFc tag. The predicted molecular weight is 45.7 kDa and the accession number is AAK26160.1.

Expression system: HEK293 Cells
Length: 74-240, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 74-240, Partial
Activity: ELISA

Expression system: Baculovirus Insect Cells
Length: 72-239, Partial
Activity: Not Tested

LIGHT TNFSF14 Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 44.9 kDa and the accession number is AAK26160.1.

LIGHT TNFSF14 Protein, Human, Recombinant is expressed in HEK293 Cells. The accession number is O43557.

Expression system: E. coli
Length: 1-175, Full Length
Activity: Not Tested

GPR37 (cathepsin Z) is an orphan receptor that belongs to the G-protein coupled receptor 1 family. G protein-coupled receptors are a large protein family comprised of transmembrane receptors that sense molecules outside the cell and activate inside signal transduction pathways and, ultimately, cellular responses. They only exist in eukaryotes, including yeast, choanoflagellates, and animals. These receptors are bonded and activated by light-sensitive compounds, odors, pheromones, hormones, and neurotransmitters. These ligands vary in size from small molecules to peptides to large proteins. G protein-coupled receptors are involved in many diseases and are also the target of approximately 40% of all modern medicinal drugs. GPR37 is expressed in the brain and spinal cord, and at lower levels in the testis, placenta, and liver, but no detectable expression is observed in any other tissue. GPR37 may have a unique functional role in the central nervous system.

Factor XI (plasma thromboplastin antecedent) is a plasma glycoprotein, and a zymogen acting as a serine protease which participates in blood coagulation as a catalyst in the conversion of factor IX to factor IXa in the presence of calcium ions. It is an unusual dimeric protease, with structural features that distinguish it from vitamin K-dependent coagulation proteases. The factor XI is synthesized in the liver as a single polypeptide chain with a molecular weight estimated between 125 ~160 kDa and then is processed into a disulfide-bond linked homodimer. FXI is a homodimer, with each subunit containing four apple domains and a protease domain. The apple domains form a disk structure with binding sites for platelets, high molecular weight kininogen, and the substrate factor IX (FIX). FXI is converted to the active protease FXIa by cleavage of the Arg369-Ile370 bond on each subunit. After the activation reaction, Factor XIa is composed of two heavy and two light chains held together by three disulfide bonds. The heavy chains are derived from the amino termini of the zymogen and responsible for the binding of factor XI to high molecular weight kininogen and for the activation of factor IX, while the light chain contains the catalytic portion of the enzyme and is homologous to the trypsin family of serine proteases. FXI deficiency is a disorder characterized by a mild or no bleeding tendency. Severe FXI deficiency is an injury-related bleeding disorder common in Ashkenazi Jews and rare worldwide.

Immunoglobulin Kappa is constant region of immunoglobulin light chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.

Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, alpha (IkB alpha, NFKBIA, or IKBA), is a member of the NF-kappa-B inhibitor family that function to inhibit the NF-kB transcription factor. NFKBIA inhibits NF-kB by masking the nuclear localization signals (NLS) of NF-kB proteins and keeping them sequestered in an inactive state in the cytoplasm. Also, NFKBIA blocks the ability of NF-κB transcription factors to bind to DNA, which is required for NF-kB's proper functioning. Signal-induced degradation of I kappa B alpha exposes the nuclear localization signal of NF-kappa B, thus allowing it to translocate into the nucleus and activate transcription from responsive genes. An autoregulatory loop is established when NF-kappa B induces expression of the I kappa B alpha gene and newly synthesized I kappa B alpha accumulates in the nucleus where it negatively regulates NF-kappa B-dependent transcription. As part of this post-induction repression, the nuclear export signal on I kappa B alpha mediates the transport of NF-kappa B-I kappa B alpha complexes from the nucleus to the cytoplasm. Deletion of NFKBIA has an effect that is similar to the effect of EGFR amplification in the pathogenesis of glioblastoma and is associated with comparatively short survival. Polymorphisms in NFKBIA may be important in pre-disposition to and outcome after treatment, of multiple myeloma (MM). The NFKBIA gene product, IkappaBalpha, binds to NF-kappaB preventing its activation and is important in mediating resistance to apoptosis in B-cell lymphoproliferative diseases.

Enterokinase (EK) is a serine protease produced in the duodenum and involved in mammalian digestion. It activates trypsinogen to trypsin, thereby indirectly initiating the activation of pancreatic digestive enzymes. EK specifically cleaves after the recognition sequence Asp-Asp-Asp-Asp-Lys, but is inactive if a proline follows the cleavage site. This recombinant bovine enterokinase is the light chain catalytic subunit, comprising a single glycosylated polypeptide chain corresponding to residues Ile801–His1035 of the native protein (Accession # P98072). Expressed in Pichia pastoris under animal-free conditions, the enzyme is highly active and suitable for applications in drug and vaccine development. A C-terminal 6×His tag is included to allow efficient removal by Ni²⁺ affinity chromatography following cleavage reactions.

Expression system: E. coli
Length: 1-89, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-89, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-195, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-126, Full Length of Mature Protein
Activity: Not Tested

Enterokinase is a member of the trypsin family of serine proteases. The precursor protein is cleaved into two chains which then forms a heterodimer linked by a disulfide bond. The heavy chain anchors enterokinase in the intestinal brush border membrane and the light chain is the catalytic subunit, which initiates conversion activation of a subset of pancreatic proteolytic proenzymes. Enterokinase is the physiological activator of trypsinogen and has a specificity for the sequence (Asp)4-Lys-Ile. The mature trypsin in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases. In addition, Enterokinase is a tool protease widely utilized in the cleavage of recombinant fusion proteins.

Expression system: E. coli
Length: 1-36, Partial
Activity: Not Tested

Expression system: Baculovirus Insect Cells
Length: 1-494, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-364, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 2-484, Full Length of Mature Protein
Activity: Not Tested

Expression system: P. pastoris (Yeast)
Length: 2-172, Full Length of Mature Protein
Activity: ELISA