compartment

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

Expression system: E. coli
Length: 40-536, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 40-536, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 11-379, Partial
Activity: Not Tested

Expression system: E. coli
Length: 174-272, Partial
Activity: Not Tested

Expression system: E. coli
Length: 55-319, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-54, Partial
Activity: ELISA

Scavenger Receptor Class B Member 2 (SCARB2) is a type III multi-pass membrane glycoprotein that is located primarily in limiting membranes of lysosomes and endosomes on all tissues and cell types so far examined. Earlier studies in mice and rat suggested that this protein may participate in membrane transportation and the reorganization of endosomal lysosomal compartment. The protein deficiency in mice was reported to impair cell membrane transport processes and cause pelvic junction obstruction, deafness, and peripheral neuropathy. Further studies in human showed that this protein is identified as a receptor for EV71 (human enterovirus species A, Enterovirus 71) and CVA16 (coxsackievirus A16) which are most frequently associated with hand, foot and mouth disease (HFMD). Mutations in this gene caused an autosomal recessive progressive myoclonic epilepsy-4 (EPM4), also known as action myoclonus-renal failure syndrome (AMRF). Alternatively spliced transcript variants encoding different isoforms have been found for this gene. In addition, SCARB2 also has been shown to bind thrombospondin-1, may contribute to the pro-adhesive changes of activated platelets during coagulation, and inflammation.

Lysosome membrane protein II (LIMPII),also known as SCARB2, is a type III multi-pass membrane glycoprotein that is located primarily in limiting membranes of lysosomes and endosomes on all tissues and cell types so far examined. Earlier studies in mice and rat suggested that this protein may participate in membrane transportation and the reorganization of endosomal lysosomal compartment. The protein deficiency in mice was reported to impair cell membrane transport processes and cause pelvic junction obstruction, deafness, and peripheral neuropathy. Further studies in human showed that this protein is identified as a receptor for EV71 (human enterovirus species A, Enterovirus 71) and CVA16 (coxsackievirus A16) which are most frequently associated with hand, foot and mouth disease (HFMD). Mutations in this gene caused an autosomal recessive progressive myoclonic epilepsy-4 (EPM4), also known as action myoclonus-renal failure syndrome (AMRF). Alternatively spliced transcript variants encoding different isoforms have been found for this gene. In addition, LIMPII also has been shown to bind thrombospondin-1, may contribute to the pro-adhesive changes of activated platelets during coagulation, and inflammation.

Oncomodulin-1 (OM) is a small, calcium-binding protein and a macrophage-derived growth factor, which can promote axon regeneration in retinal ganglion cells. Oncomodulin-1 is constitutively secreted by activated macrophages in the vitreous and retina in response to inflammatory conditions that promote optic nerve regeneration. Oncomodulin-1 binds RGCs with high affinity in vitro, but only when cAMP is pharmacologically elevated or if the membrane is permeabilized allowing Oncomodulin-1 access to the cytosolic compartment. Oncomodulin-1 is a member of the superfamily of calmodulin proteins and is a high-affinity calcium ion-binding protein and contains 2 EF-hand domains. OM is found in early embryonic cells in the placenta and also in tumors. It has some calmodulin-like activity with respect to enzyme activation and growth regulation.

Expression system: E. coli
Length: 1-251 (mutation), Full Length
Activity: Not Tested

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

The tubby-like protein 1 (tulp1) gene is a member of the tubby multigene family which includes tub, tulp1, tulp2 and tulp3.TULP1 is a cytoplasmic, membrane-associated protein shown to be involved in transportation of newly synthesized proteins destined for the outer segment compartment of photoreceptor cells.

Expression system: HEK293 Cells
Length: 25-209, Partial
Activity: SPR

Expression system: HEK293 Cells
Length: 1-314, Full Length
Activity: Cell Activity

The Secreted frizzled-related protein (SFRP) family consists of five secreted glycoproteins in humans (SFRP1~5) that act as extracellular signaling ligands. Each SFRP is approximately 3 amino acids in length and contains a cysteine-rich domain (CRD) that shares 3-5% sequence homology with the CRD of Frizzled (Fz) receptors, a putative signal sequence, and a conserved hydrophilic carboxy-terminal domain. SFRPs are able to bind Wnt proteins and Fz receptors in the extracellular compartment. The interaction between SFRPs and Wnt proteins prevents the latter from binding the Fz receptors. The Wnt pathway plays a key role in embryonic development, cell differentiation and cell proliferation. sFRP2 is a member of the SFRP family acting as soluble modulators of Wnt signaling and contains a cysteine-rich domain homologous to the putative Wnt-binding site of Frizzled proteins called FZ domain and a NTR domain.sFRP2 inhibites hypoxia induced endothelial cell apoptosis and increases endothelial cell migration. It prevents mesoderm specification and maintains the cells in the undifferentiated state. SFRP2 is also a novel stimulator of angiogenesis that stimulates angiogenesis via a calcineurin NFAT pathway, thus is regarded as a favorable target for the inhibition of angiogenesis in solid tumors. Mouse sFRP2 is highly expressed in the eye and is also detected in heart and lung at low level.

Expression system: HEK293 Cells
Length: 26-269, Partial
Activity: Not Tested

Expression system: E. coli
Length: 1-77, Partial
Activity: Not Tested

STX3, also known as syntaxin 3, belongs to the syntaxin family. STX3 is a target membrane protein (t-SNARE) that is needed for membrane fusion. Membrane fusion requires the formation of a complex between a vesicle protein (v-SNARE) and t-SNAREs. STX3, together with syntaxin 2, are predominantly localized at the plasma membrane. Syntaxin 2 cycles between the plasma membrane and the perinuclear compartment whereas syntaxin 3 cycles between the plasma membrane and the trans-Golgi network. It is possible that this cycling has an important role in the regulation of t-SNARE function.