| Name: | Recombinant full length human vimentin |
| HGNC Name: | VIM |
| RRID: | NA |
| Format: | 1mg/mL in 6M Urea, 10mM phosphate pH=7.5 |
| Applications: | Protein standard for ELISA, MSD, Luminex and Simoa assays, also immunogen for antibody production |
| Storage: | Stable at 4°C for several months. For longer term store at -20°C or lower |
| Uniprot: | P08670 |
Coomassie Brilliant Blue stained SDS-PAGE gel of various recombinant proteins expressed in and purified from E. coli. 1µg of protein was run on each lane, and the lane indicated with “NF-L” contains the human neurofilament NF-L protein. The other lanes show recombinant human peripherin (Peri), human α-internexin (α-int) and human vimentin (Vim) as indicated. Protein molecular weight standards are in the first lane and apparent molecular weights of the recombinant proteins are as indicated. In each case the proteins run at about 5kDa higher than the native protein due to the presence of the His-tag and other vector derived sequence. The band below the major NF-L band represents a proteolytic fragment seen in bacterial preparations and also in vivo. The lower band stains with most NF-L antibodies but not with those directed against the extreme C-terminus (see for example MCA-6H112).
Recombinant Human Vimentin
Cat# Prot-r-Vim
$300.00 – $2,000.00
Vimentin is a member of the intermediate or 10nm family of proteins, which are abundant structural components of most eukaryotic cells. Vimentin is found in most cell lines grown in tissue culture (1). In adult animals vimentin is expressed in mesenchymal cells, lymphocytes, some types of glia, endothelial cells and many other cell types particularly early in development (2). Several recent studies suggest that vimentin may be detected in blood in increased levels in association with various disease processes, so that detection of serum or plasma vimentin might be useful as a diagnostic or prognostic biomarker of damage or disease (e.g. 3,4).
We designed a cDNA to encode human vimentin optimized or expression in E. coli which was inserted into the pET30a(+) vector. This vector adds an N-terminal His-tag and some other vector sequence which can be removed with thrombin or enterokinase proteases. The His-tag allows convenient purification using Nickel affinity chromatography. Sensitive ELISA, MSD, Luminex and Simoa assays for vimentin have been developed and are widely used in research and clinical contexts. This recombinant protein can be used as a convenient protein standard for such assays. The product data and MSDS information can be downloaded from the “Data Sheets” tab below.
The human vimentin sequence is identical to that in Genbank entry NP_003371.2 which was inserted into the eukaryotic expression vector pET30a(+) which adds an N-terminal His tag and some other sequence, underlined below. This sequence includes a thrombin cleavage site (blue), an S-tag affinity peptide (red) and an enterokinase cleavage site (green).
MHHHHHHSSG LVPRGSGMKE TAAAKFERQH MDSPDLGTDD DDKAMADIGS EFMSTRSVSS 60
SSYRRMFGGP GTASRPSSSR SYVTTSTRTY SLGSALRPST SRSLYASSPG GVYATRSSAV 120
RLRSSVPGVR LLQDSVDFSL ADAINTEFKN TRTNEKVELQ ELNDRFANYI DKVRFLEQQN 180
KILLAELEQL KGQGKSRLGD LYEEEMRELR RQVDQLTNDK ARVEVERDNL AEDIMRLREK 240
LQEEMLQREE AENTLQSFRQ DVDNASLARL DLERKVESLQ EEIAFLKKLH EEEIQELQAQ 300
IQEQHVQIDV DVSKPDLTAA LRDVRQQYES VAAKNLQEAE EWYKSKFADL SEAANRNNDA 360
LRQAKQESTE YRRQVQSLTC EVDALKGTNE SLERQMREME ENFAVEAANY QDTIGRLQDE 420
IQNMKEEMAR HLREYQDLLN VKMALDIEIA TYRKLLEGEE SRISLPLPNF SSLNLRETNL 480
DSLPLVDTHS KRTLLIKTVE TRDGQVINET SQHHDDLE 518
Number of amino acids: 518
Molecular weight: 59359.89
Theoretical pI: 5.14
Amino acid composition:
Ala (A) 38 7.3%
Arg (R) 45 8.7%
Asn (N) 23 4.4%
Asp (D) 36 6.9%
Cys (C) 1 0.2%
Gln (Q) 34 6.6%
Glu (E) 58 11.2%
Gly (G) 19 3.7%
His (H) 13 2.5%
Ile (I) 16 3.1%
Leu (L) 57 11.0%
Lys (K) 25 4.8%
Met (M) 14 2.7%
Phe (F) 12 2.3%
Pro (P) 11 2.1%
Ser (S) 48 9.3%
Thr (T) 27 5.2%
Trp (W) 1 0.2%
Tyr (Y) 13 2.5%
Val (V) 27 5.2%
Total number of negatively charged residues (Asp + Glu): 94
Total number of positively charged residues (Arg + Lys): 70
Extinction coefficients are in units of M-1 cm-1, at 280 nm measured in water.
Ext. coefficient 24870
Abs 0.1% (=1 g/l) 0.419, assuming all pairs of Cys residues form cystines
Ext. coefficient 24870
Abs 0.1% (=1 g/l) 0.419, assuming all Cys residues are reduced
1. Franke WW, et al. Different intermediate-sized filaments distinguished by immunofluorescence microscopy. PNAS 75:5034–8 (1978).
2. Muller M, et al. Dominant cataract formation in association with a vimentin assembly disrupting mutation. Hum. Molec. Genet. 18:1052-7 (2009).
3. Chaw SY, et al. Epithelial to mesenchymal transition (EMT) biomarkers – E-cadherin, beta-catenin, APC and Vimentin – in oral squamous cell carcinogenesis and transformation Oral Oncol. 48:997-1006 (2012).
4. Toiyama Y, et al. Increased expression of Slug and Vimentin as novel predictive biomarkers for lymph node metastasis and poor prognosis in colorectal cancer. Carcinogenesis 34:2548-57 (2013).
