at-6

Expression system: E. coli
Length: 2-95, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 29-151, Full Length of Mature Protein
Activity: Not Tested

LY6D (Lymphocyte Antigen 6 Family Member D) is a Protein Coding gene. It may act as a specification marker at the earliest stage specification of lymphocytes between B- and T-cell development. Marks the earliest stage of B-cell specification. The expression of LY6D is induced in MCF10A cells by X-ray irradiation. The induction of LY6D expression is triggered through a pathway regulated by ATM, CHK2, and p53. This method is a new Ab-directed proteomic strategy for the analysis of membrane proteins and applies to various biological phenomena in situations in which both target molecule-expressing cells and nonexpressing cells are available. Diseases associated with LY6D include Alzheimer's Disease 16 and Inferior Myocardial Infarction.

Fatty Acid-Binding Protein 6 (FABP6) is cytoplasmic protein that binds long-chain fatty acids and other hydrophobic ligands which belongs to the calycin superfamily. FABP6 expression is restricted in the small intestine to the ileum where it is involved in the enterohepatic circulation of bile acids. FABP6 forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior. Isoform 2 is expressed in colorectal adenocarcinomas and their adjacent normal mucosa (at protein level). Isoform 1 is expressed in the jejunum, ileum, cecum and ascending colon intestine. FABP6 plays a role in fatty acid uptake, transport, and metabolism. FABP6 stimulates gastric acid and pepsinogen secretion. It seems to be able to bind to bile salts and bilirubins.

Glucokinase belongs to the bacterial glucokinase family. Hexokinases phosphorylate glucose to produce glucose-6-phosphate, the first step in most glucose metabolism pathways. Alternative splicing of this gene results in three tissue-specific forms of glucokinase, one found in pancreatic islet beta cells and two found in liver. The protein localizes to the outer membrane of mitochondria. In contrast to other forms of hexokinase, this enzyme is not inhibited by its product glucose-6-phosphate but remains active while glucose is abundant. Mutations in this gene have been associated with non-insulin dependent diabetes mellitus (NIDDM), maturity onset diabetes of the young, type 2 (MODY2) and persistent hyperinsulinemic hypoglycemia of infancy (PHHI). It can Catalyzes the initial step in utilization of glucose by the beta-cell and liver at physiological glucose concentration. Glucokinase has a high Km for glucose, and so it is effective only when glucose is abundant. The role of GCK is to provide G6P for the synthesis of glycogen. Pancreatic glucokinase plays an important role in modulating insulin secretion. Hepatic glucokinase helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage. It has a pivotal role as glucose sensor of the pancreatic beta-cells. Glucokinase explains the capacity, hexose specificity, affinities, sigmoidicity, and anomeric preference of pancreatic islet glycolysis, and because stimulation of glucose metabolism is a prerequisite of glucose stimulation of insulin release, glucokinase also explains many characteristics of this beta-cell function. Glucokinase of the beta-cell is induced or activated by glucose in contrast to liver glucokinase, which is regulated by insulin. Tissue-specific regulation corresponds with observations that liver and pancreatic beta-cell glucokinase are structurally distinct. Glucokinase could play a glucose-sensor role in hepatocytes as well, and certain forms of diabetes mellitus might be due to glucokinase deficiencies in pancreatic beta-cells, hepatocytes, or both.

Insulin-like growth factor 2 (IGF-2 IGF-II) is a member of the insulin family of polypeptide growth factors, which are involved in development and growth. It is an imprinted gene, expressed only from the paternal allele, and epigenetic changes at this locus are associated with Wilms tumor, Beckwith-Wiedemann syndrome, rhabdomyosarcoma, and Silver-Russell syndrome. IGF-2 IGF-II is a mediator of prolactin-induced alveologenesis; prolactin, IGF-2, and cyclin D1, all of which are overexpressed in breast cancers, are components of a developmental pathway in the mammary gland. IGF-2 and exhibited statistically significant, positive associations with colorectal cancer risk when cases were confined to those diagnosed within a relatively short period after enrolment. Circulating IGF-2 and IGFBP-3 can serve as early indicators of impending colorectal cancer. IGF-2 IGF-II appears to be involved in the progression of many tumors. It binds to at least two different types of receptors: IGF type 1 (IGF 1R) and mannose 6-phosphate IGF type 2 (M6-P IGF 2R). Ligand binding to IGF 1R provokes mitogenic and anti-apoptotic effects. M6-P IGF 2R has a tumor suppressor function—it mediates IGF 2 degradation. Mutation of M6-P IGF 2R causes both diminished growth suppression and augmented growth stimulation. This study aimed to investigate the role of IGF 2 and its receptors (IGF 1R and IGF 2R) in human gastric cancer.

KSP-Cadherin Cadherin-16 is a member of the cadherin superfamily, calcium-dependent, membrane-associated glycoproteins. The protein consists of an extracellular domain containing 6 cadherin domains, a transmembrane region and a truncated cytoplasmic domain but lacks the prosequence and tripeptide HAV adhesion recognition sequence typical of most classical cadherins. Expression is exclusively in kidney, where the protein functions as the principal mediator of homotypic cellular recognition, playing a role in the morphogenic direction of tissue development. KSP-Cadherin Cadherin-16 can be detected at later stages of tubulogenesis during human renal development and in the distal tubules of adult kidneys, no expression was found by immunohistochemistry or Western blot analysis in RCC tumour tissues and several RCC cell lines. However, despite the lack of protein expression, mRNA synthesis of KSP-Cadherin Cadherin-16 could be detected by reverse transcriptase-polymerase chain reaction analysis in all RCC tissues and most of the RCC cell lines studied, although at a reduced level. The loss of KSP-Cadherin Cadherin-16 protein was only observed in the malignant part of the tumour kidneys, whereas in the normal part of the affected kidneys KSP-Cadherin Cadherin-16 expression was clearly detected. These results indicate a downregulation of Ksp-cadherin in RCC and suggest a role for this cell adhesion molecule in tumour suppression.

Gastrotropin, also known as Fatty acid-binding protein 6, Ileal lipid-binding protein, ILBP, Intestinal 15 kDa protein, Intestinal bile acid-binding protein, I-BABP and FABP6, is a cytoplasm protein which belongs to thecalycin superfamily and Fatty-acid binding protein (FABP) family. Isoform2 of FABP6 is expressed in colorectal adenocarcinomas and their adjacent normal mucosa (at protein level). Isoform1of FABP6 is expressed in the jejunum, ileum, cecum and ascending colon intestine. Isoform2is expressed in the gallbladder, duodenum, jejunum, ileum, cecum, ascending, transverse and descending colon, sigmoid colon and rectum. FABP6 I-BABP is a cancer-related protein that acts as an intracellular transporter of bile acid in the ileal epithelium. FABP6 I-BABP may also play an important role in early carcinogenesis.

Recombinant PreScission Protease (rPSP) is a highly purified, restriction-grade 6×His-tagged protease derived from human rhinovirus 3C (HRV 3C). It specifically cleaves at the recognition sequence Leu-Glu-Val-Leu-Phe-Gln↓Gly-Pro (LEVLFQ↓GP), with the cleavage occurring between the Gln and Gly residues. This protease is commonly used to remove affinity tags from fusion proteins. rPSP functions optimally at 30 °C, but retains activity at temperatures as low as 4 °C. Cleavage efficiency may vary with different fusion proteins, so optimization of enzyme amount, incubation time, and temperature is recommended. The His-tag allows easy removal of the protease after digestion using Ni²⁺ affinity chromatography. The recombinant enzyme consists of 217 amino acids, has a molecular mass of approximately 24 kDa, and is produced through proprietary purification methods. It is fully biologically active.

MGMT belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. MGMT involved in the cellular defense against the biological effects of O6-methylguanine in DNA. Repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme. MGMT catalyzes the chemical reaction: DNA (containing 6-O-methylguanine) and proteinL-cysteine into DNA (without 6-O-methylguanine) and protein S-methyl-L-cysteine.

Expression system: HEK293 Cells
Length: 17-363, Extracellular Domain
Activity: Not Tested

Expression system: HEK293 Cells
Length: 29-409, Partial
Activity: Not Tested

Expression system: E. coli
Length: 24-297, Extracellular Domain
Activity: Not Tested

Interleukin-17 is a potent pro-inflammatory cytokine produced by activated memory T cells. There are at least six members of the IL-17 family in humans and in mice. As IL-17 shares properties with IL-1 and TNF-alpha, it may induce joint inflammation and bone and cartilage destruction. This cytokine is found in synovial fluids of patients with rheumatoid arthritis, and produced by rheumatoid arthritis synovium. It increases IL-6 production, induces collagen degradation and decreases collagen synthesis by synovium and cartilage and proteoglycan synthesis in cartilage. IL-17 is also able to increase bone destruction and reduce its formation. Blocking of interleukin-17 with specific inhibitors provides a protective inhibition of cartilage and bone degradation.

TMEM25 is a novel member of the immunoglobulin superfamily. Immunoglobulin superfamily members are implicated in immune responses, growth factor signaling, and cell adhesion. TMEM25 contains 1 Ig-like (immunoglobulin-like) domain and is a target of pharmacogenomics in the field of oncology and regenerative medicine. TMEM25 isoform 1, consisting of exons 1-9, encoded a 366-aa transmembrane protein. TMEM25 isoform 2, consisting of exons 1-4 and 6-9, encoded a 322-aa secreted protein. TMEM25 mRNA was expressed in brain, including cerebellar cortex and hippocampus, as well as in neuroblastoma, brain tumors, and gastric cancer. Human TMEM25 gene was located at the 11q23.3 oncogenomic recombination hotspot around the MLL amplicon and the neuroblastoma deleted region.

PSME3, also known as PA28-gamma, is a subunit of proteasome. The 26S proteasome multicatalytic proteinase complex has a highly ordered structure composed of 2 complexes, a 2S core and a 19S regulator. The 2S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 1 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. PSME3 gene encodes the gamma subunit of the 11S regulator. Six gamma subunits combine to form a homohexameric ring.

Tryptase beta-2(Tpsb2), also known as Mast cell protease 6(mMCP-6), belongs to the peptidase S1 family and Tryptase subfamily. Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. It plays a role in innate immunity. Tpsb2 can be detected primarily in skin during embryogenesis. Tpsb2 can not be detected at early embryonic stages but is abundantly expressed in later stages with a peak at E17.5-E18.5. Tryptase is a homotetramer. The active tetramer is converted to inactive monomers at neutral and acidic pH in the absence of heparin. Low concentrations of inactive monomers become active monomers at pH 6.0 in the presence of heparin. When the concentration of active monomers is higher, they convert to active monomers and then to active tetramers. These monomers are active and functionally distinct from the tetrameric enzyme. In contrast to the hidden active sites in the tetrameric form, the active site of the monomeric form is accessible for macromolecular proteins and inhibitors eg: fibrinogen which is a substrate for the monomeric but not for the tetrameric form. The monomeric form forms a complex with SERPINB6.

Expression system: P. pastoris (Yeast)
Length: 247-454, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 21-189, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 18-202, Partial
Activity: Not Tested

Expression system: E. coli
Length: 1-153, Full Length
Activity: Not Tested

Expression system: Baculovirus Insect Cells
Length: 1-663, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-249, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1820-2590, Partial
Activity: Not Tested