hras-1

HRas, also known as HRAS, belongs to the small GTPase superfamily, Ras family, and is widely expressed. It functions in signal transduction pathways. HRas can bind GTP and GDP, and they have intrinsic GTPase activity. It undergoes a continuous cycle of de- and re-palmitoylation, which regulates its rapid exchange between the plasma membrane and the Golgi apparatus. Defects in HRAS are the cause of faciocutaneoskeletal syndrome (FCSS). FCSS is a rare condition characterized by prenatally increased growth, postnatal growth deficiency, mental retardation, distinctive facial appearance, cardiovascular abnormalities, tumor predisposition, skin, and musculoskeletal abnormalities. Defects in HRAS also can cause congenital myopathy with excess of muscle spindles. HRAS deficiency may be a cause of susceptibility to Hurthle cell thyroid carcinoma. It has been shown that defects in HRAS can cause susceptibility to bladder cancer which is a malignancy originating in tissues of the urinary bladder. It often presents with multiple tumors appearing at different times and different sites in the bladder. Most bladder cancers are transitional cell carcinomas. They begin in cells that normally make up the inner lining of the bladder. Other types of bladder cancer include squamous cell carcinoma (cancer that begins in thin, flat cells) and adenocarcinoma (cancer that begins in cells that make and release mucus and other fluids). Bladder cancer is a complex disorder with both genetic and environmental influences. Defects in HRAS are the cause of oral squamous cell carcinoma.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy

HRAS Protein, Rat, Recombinant (His) is expressed in E. coli. The accession number is P20171.

Expression system: E. coli
Length: 1-186, Full Length of Mature Protein
Activity: Not Tested

Lysophospholipase II (LYPLA2, LPL-II, or LysoPLA II), also known as Acyl-protein thioesterase 2 (APT-2), belongs to the AB hydrolase 2 family. This enzyme has lysophospholipase activity and may hydrolyze fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Acyl-protein thioesterase 1 (APT-1) and Acyl-protein thioesterase 2 (APT-2) are cytosolic lysophospholipids hydrolyzing enzymes. The serum activity of APT-1 may play an important role in the determination of the concentration of des-acyl ghrelin in circulation, especially under septic inflammation. APT-2 LYPLA2 is expressed both in CHO-K1 and HeLa cells and its overexpression increased the deacylation rate of single acylated GAP-43 and affected the steady-state localization of diacylated GAP-43 and H-Ras. Thus, the results demonstrate that APT-2 LYPLA2 is the protein thioesterase involved in the acylation deacylation cycle operating in GAP-43 subcellular distribution.

Acyl-Protein Thioesterase 1 (APT-1) is lysophospholipase that belongs to the AB hydrolase 2 family. Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. APT-1 performs on biological membranes to regulate the multifunctional lysophospholipids. It hydrolyzes lysophosphatidylcholine in both monomeric and micellar forms. It hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS; in addition, it also has depalmitoylating activity and low lysophospholipase activity.

Group XVI Phospholipase A1 A2 (PLA2G16) belongs to the H-rev 107 family. PLA2G16 is expressed in a number of human tumors including ovarian carcinomas, lung carcinomas. PLA2G16 is involved in the regulation of differentiation and survival. PLA2G16 regulates adipocyte lipolysis and release of fatty acids through a G-protein coupled pathway involving prostaglandin and EP3. It has also been reported to play a crucial role in the development of obesity in mouse models.