Probable serine carboxypeptidase CPVL Recombinant Protein | CPVL recombinant protein

Recombinant Human Probable serine carboxypeptidase CPVL

Cat. Num. AAA1449179

• Gene Names: CPVL; HVLP
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Probable serine carboxypeptidase CPVL; Recombinant Human Probable serine carboxypeptidase CPVL; Carboxypeptidase; vitellogenic-like; Vitellogenic carboxypeptidase-like protein; VCP-like protein; hVLP; CPVL recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 23-476aa; Full Length
• Sequence: LFRSLYRSVSMPPKGDSGQPLFLTPYIEAGKIQKGRELSLVGPFPGLNMKSYAGFLTVNKTYNSNLFFWFFPAQIQPEDAPVVLWLQGGPGGSSMFGLFVEHGPYVVTSNMTLRDRDFPWTTTLSMLYIDNPVGTGFSFTDDTHGYAVNEDDVARDLYSALIQFFQIFPEYKNNDFYVTGESYAGKYVPAIAHLIHSLNPVREVKINLNGIAIGDGYSDPESIIGGYAEFLYQIGLLDEKQKKYFQKQCHECIEHIRKQNWFEAFEILDKLLDGDLTSDPSYFQNVTGCSNYYNFLRCTEPEDQLYYVKFLSLPEVRQAIHVGNQTFNDGTIVEKYLREDTVQSVKPWLTEIMNNYKVLIYNGQLDIIVAAALTERSLMGMDWKGSQEYKKAEKKVWKIFKSDSEVAGYIRQAGDFHQVIIRGGGHILPYDQPLRAFDMINRFIYGKGWDPYVG
• Sequence Length: 476

• 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 CPVL recombinant protein

May be involved in the digestion of phagocytosed particles in the lysosome, participation in an inflammatory protease cascade, and trimming of peptides for antigen presentation.

Product Categories/Family for CPVL recombinant protein

Cell Biology

References

Cloning and characterization of CPVL, a novel serine carboxypeptidase, from human macrophages.Mahoney J.A., Ntolosi B., DaSilva R.P., Gordon S., McKnight A.J.Genomics 72:243-251(2001) Cloning of VCP-like protein expressed in human heart and placenta.Cho J.-J., Baik H.-H.The secreted protein discovery initiative (SPDI) , a large-scale effort to identify novel human secreted and transmembrane proteins a bioinformatics assessment.Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.Genome Res. 13:2265-2270(2003) Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries.Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.DNA Res. 12:117-126(2005) Human chromosome 7 DNA sequence and biology.Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.Science 300:767-772(2003)

NCBI and Uniprot Product Information

• NCBI GI #: 83641876
• NCBI GeneID: 54504
• NCBI Accession #: NP_061902.2
• NCBI GenBank Nucleotide #: NM_019029.2
• UniProt Accession #: Q9H3G5; Q6UX20; Q8NBL7; Q96AR7; Q9HB41; A4D1A4
• Molecular Weight: 67.9 kDa
• NCBI Official Full Name: probable serine carboxypeptidase CPVL
• NCBI Official Synonym Full Names: carboxypeptidase, vitellogenic like
• NCBI Official Symbol: CPVL
• NCBI Official Synonym Symbols: HVLP
• NCBI Protein Information: probable serine carboxypeptidase CPVL
• UniProt Protein Name: Probable serine carboxypeptidase CPVL
• Protein Family: Probable serine carboxypeptidase
• UniProt Gene Name: CPVL
• UniProt Synonym Gene Names: VLP; VCP-like protein; hVLP
• UniProt Entry Name: CPVL_HUMAN

NCBI Description

The protein encoded by this gene is a carboxypeptidase and bears strong sequence similarity to serine carboxypeptidases. Carboxypeptidases are a large class of proteases that act to cleave a single amino acid from the carboxy termini of proteins or peptides. The exact function of this protein, however, has not been determined. At least two alternatively spliced transcripts which encode the same protein have been observed. [provided by RefSeq, Jul 2008]

Uniprot Description

CPVL: May be involved in the digestion of phagocytosed particles in the lysosome, participation in an inflammatory protease cascade, and trimming of peptides for antigen presentation. Belongs to the peptidase S10 family.

Protein type: Protease; Secreted, signal peptide; Secreted; EC 3.4.16.-

Chromosomal Location of Human Ortholog: 7p15.1

Molecular Function: serine carboxypeptidase activity

Biological Process: proteolysis involved in cellular protein catabolic process