up-2

Uroplakin-2 is a single-pass type I membrane protein that belongs to the uroplakin-2 family. Uroplakin-2 is a component of the asymmetric unit membrane (AUM) and expressed in the ureter, a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. Uroplakin-2 forms heterodimer with UPK1A that is necessary for exiting out of the endoplasmic reticulum (ER). Uroplakin-2 may play an important role in regulating the assembly of the AUM. AUM is believed to strengthen the urothelium by preventing cell rupture during bladder distention.

Expression system: E. coli
Length: 85-184, Full Length of Mature Protein
Activity: Not Tested

Expression system: Baculovirus Insect Cells
Length: 1-460, Full Length
Activity: Enzyme activity

Expression system: HEK293 Cells
Length: 1-268, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-776, Full Length
Activity: Enzyme activity

Sorbitol dehydrogenase, also known as L-iditol 2-dehydrogenase and SORD, is a member of the zinc-containing alcohol dehydrogenase family. SORD exsits in a homotetramer and binds one zinc ion per subunit. SORD is expressed in kidney and epithelial cells of both benign and malignant prostate tissue. SORD can converts sorbitol to fructose and catalyzes the interconversion of polyols and their corresponding ketoses, and together with aldose reductase to make up the sorbitol pathway. SORD is up-regulated by androgens and down-regulated by castration. SORD may play a role in the sperm motility by providing an energetic source for sperm.

Expression system: HEK293 Cells
Length: 21-248, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 28-844, Extracellular Domain
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-859, Partial
Activity: Not Tested

Izumo is a sperm membrane protein that plays a key role in the fusion in the mouse. It has an Immunoglobulin (Ig) domain and an N-terminal domain for which neither the functions nor homologous sequences are known. Up to now, there four members has an N-terminal domain with significant homology to the N-terminal domain of Izumo. We call this domain the Izumo domain. The four proteins are Izumo 1, 2, 3, and 4. Izumo domain possesses the ability to form dimers, whereas the transmembrane domain or the cytoplasmic domain, or both of Izumo 1 are required for the formation of multimers of a higher order. Izumo 1-3 are transmembrane proteins expressed specifically in the testis, and Izumo 4 is a soluble protein expressed in the testis and other tissues. Izumo 1, 3, and 4 formed protein complexes on sperm, Izumo 1 forming several larger complexes, and Izumo 3 and 4 forming a single larger complex. Izumo1 is essential for sperm-egg plasma membrane binding and fusion.

Expression system: E. coli
Length: 2-457, Partial
Activity: Not Tested

Expression system: Baculovirus Insect Cells
Length: 1-94, Full Length
Activity: Not Tested

The Capillary Morphogenesis Gene 2 (CMG2) gene encodes an Anthrax toxin receptor (ANTXR2),ANTXR2 CMG2 was originally identified as a result of up-regulation during capillary morphogenesis of endothelial cells (ECs) cultured in vitro. ANTXR2 CMG2 functions to promote endothelial proliferation and morphogenesis during sprouting angiogenesis, consistent with the endothelial expression of ANTXR2 CMG2 in several vascular beds.

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.

Reticulocalbin-2 (RCN2, also named as ERC-55), is a 55-kDa Ca2+-binding protein containing six EF-hands, which was identified to be localized in endoplasmic reticulum. RCN2 is belonging to Reticulocalbin (RCN) family, the family members could play oncogenic roles in human malignancies and facilitate tumor cell proliferation and metastasis. Recently, studies on RCN2 functions mainly focused on its role in differentiation and endocrine regulation in mouse. Another study has suggested that RCN2 could be a potential tumor-associated antigen for mammary cancer immunological prevention. Up to now, the experimental evidence uncovering the role of RCN2 in cancer is very limited.

Expression system: HEK293 Cells
Length: 26-215, Partial
Activity: ELISA

Expression system: HEK293 Cells
Length: 25-363, Extracellular Domain
Activity: Not Tested

Expression system: HEK293 Cells
Length: 26-364, Extracellular Domain
Activity: ELISA

Expression system: HEK293 Cells
Length: 19-482, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 20-355, Partial
Activity: Not Tested

Expression system: E. coli
Length: 109-266, Partial
Activity: ELISA

Expression system: E. coli
Length: 1-436, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-214, Full Length
Activity: Not Tested

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