Transmembrane emp24 domain-containing protein 9 Recombinant Protein | GP25L2 recombinant protein

Recombinant Human Transmembrane emp24 domain-containing protein 9

Cat. Num. AAA717282

• Gene Names: TMED9; p25; GMP25; HSGP25L2G
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Transmembrane emp24 domain-containing protein 9; Recombinant Human Transmembrane emp24 domain-containing protein 9; GMP25; Glycoprotein 25; L2; p24 family protein alpha-2; p24; alpha2; p25; GP25L2 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 40-197aa; Partial
• Sequence: FHIGETEKKCFIEEIPDETMVIGNYRTQLYDKQREEYQPATPGLGMFVEVKDPEDKVILARQYGSEGRFTFTSHTPGEHQICLHSNSTKFSLFAGGMLRVHLDIQVGEHANDYAEIAAKDKLSELQLRVRQLVEQVEQIQKEQNYQRWREERFRQTSE
• Sequence Length: 235

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for GP25L2 recombinant protein

Appears to be involved in vesicular protein trafficking, mainly in the early secretory pathway. In COPI vesicle-mediated retrograde transport involved in the coatomer recruitment to membranes of the early secretory pathway. Increases coatomer-dependent activity of ARFGAP2. Thought to play a crucial role in the specific retention of p24 complexes in cis-Golgi membranes; specifically contributes to the coupled localization of TMED2 and TMED10 in the cis-Golgi network. May be involved in organization of intracellular membranes, such as of the ER-Golgi intermediate compartment and the Golgi apparatus. Involved in ER localization of PTPN2 isoform PTPB.

Product Categories/Family for GP25L2 recombinant protein

Signal Transduction

References

The DNA sequence and comparative analysis of human chromosome 5.Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.Nature 431:268-274(2004) Dominguez M., Fazel A., Parlati F., Bell A.W., Thomas D.Y., Bergeron J.J.M. A novel human cDNA that shares sequence homology with Homo sapiens mRNAs LOC96645 and gp25L2.Wang C., Li Y.Bienvenut W.V.Submitted (MAR-2005) to UniProtKB Localization and recycling of gp27 (hp24gamma3) complex formation with other p24 family members.Fullekrug J., Suganuma T., Tang B.L., Hong W., Storrie B., Nilsson T.Mol. Biol. Cell 10:1939-1955(1999) Coupled transport of p24 family members.Emery G., Rojo M., Gruenberg J.J. Cell Sci. 113:2507-2516(2000) Oligomeric state and stoichiometry of p24 proteins in the early secretory pathway.Jenne N., Frey K., Brugger B., Wieland F.T.J. Biol. Chem. 277:46504-46511(2002) The trans-membrane protein p25 forms highly specialized domains that regulate membrane composition and dynamics.Emery G., Parton R.G., Rojo M., Gruenberg J.J. Cell Sci. 116:4821-4832(2003) Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.Zhang H., Li X.-J., Martin D.B., Aebersold R.Nat. Biotechnol. 21:660-666(2003) The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B.Reid E., Connell J.W., Edwards T.L., Duley S., Brown S.E., Sanderson C.M.Hum. Mol. Genet. 14:19-38(2005) Evidence for a role of transmembrane protein p25 in localization of protein tyrosine phosphatase TC48 to the ER.Gupta V., Swarup G.J. Cell Sci. 119:1703-1714(2006) Coatomer, the coat protein of COPI transport vesicles, discriminates endoplasmic reticulum residents from p24 proteins.Bethune J., Kol M., Hoffmann J., Reckmann I., Brugger B., Wieland F.Mol. Cell. Biol. 26:8011-8021(2006) The cargo receptors Surf4, endoplasmic reticulum-Golgi intermediate compartment (ERGIC) -53, and p25 are required to maintain the architecture of ERGIC and Golgi.Mitrovic S., Ben-Tekaya H., Koegler E., Gruenberg J., Hauri H.-P.Mol. Biol. Cell 19:1976-1990(2008) Arf GAP2 is positively regulated by coatomer and cargo.Luo R., Ha V.L., Hayashi R., Randazzo P.A.Cell. Signal. 21:1169-1179(2009) Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.J. Proteome Res. 8:651-661(2009) p28, a novel ERGIC/cis Golgi protein, required for Golgi ribbon formation.Koegler E., Bonnon C., Waldmeier L., Mitrovic S., Halbeisen R., Hauri H.P.Traffic 11:70-89(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) Syntaxin 17 cycles between the ER and ERGIC and is required to maintain the architecture of ERGIC and Golgi.Muppirala M., Gupta V., Swarup G.Biol. Cell 103:333-350(2011)

NCBI and Uniprot Product Information

• NCBI GI #: 39725636
• NCBI GeneID: 54732
• NCBI Accession #: NP_059980.2
• NCBI GenBank Nucleotide #: NM_017510.4
• UniProt Accession #: Q9BVK6; Q14437; Q8WZ61
• Molecular Weight: 45.5 kDa
• NCBI Official Full Name: transmembrane emp24 domain-containing protein 9
• NCBI Official Synonym Full Names: transmembrane p24 trafficking protein 9
• NCBI Official Symbol: TMED9
• NCBI Official Synonym Symbols: p25; GMP25; HSGP25L2G
• NCBI Protein Information: transmembrane emp24 domain-containing protein 9
• UniProt Protein Name: Transmembrane emp24 domain-containing protein 9
• Protein Family: Transmembrane emp24 domain-containing protein
• UniProt Gene Name: TMED9
• UniProt Synonym Gene Names: GP25L2; p24alpha2
• UniProt Entry Name: TMED9_HUMAN

NCBI Description

This gene is a member of a family of genes encoding transport proteins located in the endoplasmic reticulum and the Golgi. A similar gene in mouse is the target of microRNA miR-296, which is part of an imprinted cluster. [provided by RefSeq, Jul 2016]

Uniprot Description

TMED9: Appears to be involved in vesicular protein trafficking, mainly in the early secretory pathway. In COPI vesicle-mediated retrograde transport involved in the coatomer recruitment to membranes of the early secretory pathway. Increases coatomer- dependent activity of ARFGAP2. Thought to play a crucial role in the specific retention of p24 complexes in cis-Golgi membranes; specifically contributes to the coupled localization of TMED2 and TMED10 in the cis-Golgi network. May be involved in organization of intracellular membranes, such as of the ER-Golgi intermediate compartment and the Golgi apparatus. Involved in ER localization of PTPN2 isoform PTPB. Belongs to the EMP24/GP25L family.

Protein type: Membrane protein, integral

Chromosomal Location of Human Ortholog: 5q35.3

Cellular Component: endoplasmic reticulum; endoplasmic reticulum membrane; ER-Golgi intermediate compartment; ER-Golgi intermediate compartment membrane; Golgi apparatus; Golgi membrane; integral to membrane; trans-Golgi network transport vesicle; transport vesicle

Molecular Function: protein binding; syntaxin binding

Biological Process: cellular protein metabolic process; COPI coating of Golgi vesicle; ER to Golgi vesicle-mediated transport; Golgi organization and biogenesis; post-translational protein modification; protein amino acid N-linked glycosylation via asparagine; protein exit from endoplasmic reticulum