protein

Recombinant Human Probable serine carboxypeptidase CPVL

MBS1449179

0.01 mg (E-Coli)

160 USD

Recombinant Protein

Recombinant Human Probable serine carboxypeptidase CPVL

[Probable serine carboxypeptidase CPVL]

[Carboxypeptidase, vitellogenic-like; Vitellogenic carboxypeptidase-like protein; VCP-like protein; hVLP]

[probable serine carboxypeptidase CPVL; Probable serine carboxypeptidase CPVL; probable serine carboxypeptidase CPVL; carboxypeptidase, vitellogenic like; Carboxypeptidase, vitellogenic-like; Vitellogenic carboxypeptidase-like protein; VCP-like protein; hVLP]

[CPVL]

[CPVL; CPVL; HVLP; VLP; VCP-like protein; hVLP]

CPVL_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

[23-476aa; Full Length]

476

LFRSLYRSVSMPPKGDSGQPLFLTPYIEAGKIQKGRELS
LVGPFPGLNMKSYAGFLTVNKTYNSNLFFWFFPAQIQPE
DAPVVLWLQGGPGGSSMFGLFVEHGPYVVTSNMTLRDRD
FPWTTTLSMLYIDNPVGTGFSFTDDTHGYAVNEDDVARD
LYSALIQFFQIFPEYKNNDFYVTGESYAGKYVPAIAHLI
HSLNPVREVKINLNGIAIGDGYSDPESIIGGYAEFLYQI
GLLDEKQKKYFQKQCHECIEHIRKQNWFEAFEILDKLLD
GDLTSDPSYFQNVTGCSNYYNFLRCTEPEDQLYYVKFLS
LPEVRQAIHVGNQTFNDGTIVEKYLREDTVQSVKPWLTE
IMNNYKVLIYNGQLDIIVAAALTERSLMGMDWKGSQEYK
KAEKKVWKIFKSDSEVAGYIRQAGDFHQVIIRGGGHILP
YDQPLRAFDMINRFIYGKGWDPYVG

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Cell Biology

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.

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)

83641876

NP_061902.2

NM_019029.2

Q9H3G5

67.9kD

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]

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

0.01 mg (E-Coli)

160 USD

0.05 mg (E-Coli)

200

0.1 mg (E-Coli)

295

0.2 mg (E-Coli)

480

0.5 mg (E-Coli)

790

1 mg (E-Coli)

1215