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Recombinant Human Vimentin Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

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Recombinant Human Vimentin Protein, CF Summary

Details of Functionality
Measured by its ability to bind Recombinant Human NKp46/NCR1 Fc Chimera (Catalog # 1850-NK) in a functional ELISA with an estimated KD < 2 nM. Garg, A. et al. (2006) J. Immunol. 177:6192.
Source
E. coli-derived human Vimentin protein
Ser2-Glu466 , with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Ser2
Protein/Peptide Type
Recombinant Proteins
Gene
VIM
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Binding Activity
Theoretical MW
54.4 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using
2105-VI in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with Trehalose.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile 4 mM HCl.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Vimentin Protein, CF

  • epididymis secretory sperm binding protein
  • FLJ36605
  • VIM
  • Vimentin

Background

The Vimentin protein is a 57 kDa class III intermediate filament (IF) protein that belongs to the intermediate filament family. Vimentin is the predominant intermediate filament in cells of mesenchymal origin such as vascular endothelium and blood cells (1-3). The human Vimentin cDNA encodes a 466 amino acid (aa) Vimentin protein that contains head and tail regions with multiple regulatory Ser/Thr phosphorylation sites, and a central rod domain with three coiled-coil regions separated by linkers (1, 2). The human Vimentin protein shares 97-98% aa identity with the mouse, rat, bovine and canine Vimentin proteins. Sixteen Vimentin coiled-coil dimers self-assemble to form intermediate (10-12 nm wide) filaments (4). These filaments then anneal longitudinally to form non-polarized fibers that support cell structure and withstand stress (4). Intermediate filament fibers are highly dynamic, and their half-life depends on the balance between kinase and phosphatase activity. For example, phosphorylation followed by dephosphorylation drives intermediate filament disintegration, followed by reorganization during mitosis (1, 5, 6). Interactions of head and tail domains link intermediate filaments with other structures such as actin and microtubule cytoskeletons (7). The Vimentin protein is involved in positioning autophagosomes, lysosomes and the Golgi complex within the cell (8). It facilitates cell migration and motility by recycling internalized trailing edge integrins back to the cell surface at the leading edge (9-11). Vimentin also helps maintain the lipid composition of cellular membranes, and caspase cleavage of the Vimentin protein is a key event in apoptosis (8, 12). Phosphorylation of the Vimentin protein promotes its secretion by TNF-alpha -stimulated macrophages (13). Extracellular Vimentin has been shown to associate with several microbes, and appears to promote an antimicrobial oxidative burst (13, 14). Cell-associated Vimentin can also interact with NKp46 to recruit NK cells to tuberculosis-infected monocytes (15).

  1. Omary, M.B. et al. (2006) Trends Biochem. Sci. 31:383.
  2. Ivaska, J. et al. (2007) Exp. Cell Res. 313:2050.
  3. Ferrari, S. et al. (1986) Mol. Cell. Biol. 6:3614.
  4. Sokolova, A.V. et al. (2006) Proc. Natl. Acad. Sci. USA 103:16206.
  5. Eriksson, J.E. et al. (2004) J. Cell Sci. 117:919.
  6. Li, Q.-F. et al. (2006) J. Biol. Chem. 281:34716.
  7. Esue, O. et al. (2006) J. Biol. Chem. 281:30393.
  8. Styers, M.L. et al. (2005) Traffic 6:359.
  9. McInroy, L. and A. Maata (2007) Biochem. Biophys. Res. Commun. 360:109.
  10. Nieminen, M. et al. (2006) Nat. Cell Biol. 8:156.
  11. Ivaska, J. et al. (2005) EMBO J. 24:3834.
  12. Byun, Y. et al. (2001) Cell Death Differ. 8:443.
  13. Mor-Vaknin, N. et al. (2003) Nat. Cell Biol. 5:59.
  14. Zou, Y. et al. (2006) Biochem. Biophys. Res. Commun. 351:625.
  15. Garg, A. et al. (2006) J. Immunol. 177:6192.

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2105-VI
Species: Hu
Applications: Binding Activity

Publications for Vimentin (2105-VI)(7)

We have publications tested in 3 confirmed species: Human, Mouse, N/A.

We have publications tested in 5 applications: Binding Assay, Bioassay, ELISA Capture, In Vivo, Western Blot.


Filter By Application
Binding Assay
(1)
Bioassay
(4)
ELISA Capture
(1)
In Vivo
(1)
Western Blot
(1)
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Filter By Species
Human
(6)
Mouse
(1)
N/A
(1)
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Showing Publications 1 - 7 of 7.
Publications using 2105-VI Applications Species
A Umemoto, T Kuwada, K Murata, M Shiokawa, S Ota, Y Murotani, A Itamoto, K Nishitani, H Yoshitomi, T Fujii, A Onishi, H Onizawa, K Murakami, M Tanaka, H Ito, H Seno, A Morinobu, S Matsuda Identification of anti-citrullinated osteopontin antibodies and increased inflammatory response by enhancement of osteopontin binding to fibroblast-like synoviocytes in rheumatoid arthritis Arthritis Research & Therapy, 2023-02-17;25(1):25. 2023-02-17 [PMID: 36804906] (Bioassay, ELISA Capture, Human, N/A) Bioassay, ELISA Capture Human, N/A
E Sugawara, M Kato, Y Kudo, W Lee, R Hisada, Y Fujieda, K Oku, T Bohgaki, O Amengual, S Yasuda, T Onodera, S Hatakeyama, T Atsumi Autophagy promotes citrullination of VIM (vimentin) and its interaction with major histocompatibility complex class II in synovial fibroblasts Autophagy, 2019-09-08;0(0):1-10. 2019-09-08 [PMID: 31486697] (Western Blot, Human) Western Blot Human
Potential Function of Exogenous Vimentin on the Activation of Wnt Signaling Pathway in Cancer Cells J Cancer, 2016-08-12;7(13):1824-1832. 2016-08-12 [PMID: 27698922] (Bioassay, Human) Bioassay Human
Cigarette Smoke Induces Immune Responses to Vimentin in both, Arthritis-Susceptible and -Resistant Humanized Mice PLoS ONE, 2016-09-07;11(9):e0162341. 2016-09-07 [PMID: 27602574] (In Vivo, Mouse) In Vivo Mouse
Conti F, Capozzi A, Truglia S, Lococo E, Longo A, Misasi R, Alessandri C, Valesini G, Sorice M The mosaic of &quot;seronegative&quot; antiphospholipid syndrome. J Immunol Res, 2014-03-17;2014(0):389601. 2014-03-17 [PMID: 24741593] (Bioassay, Human) Bioassay Human
Satelli A, Mitra A, Cutrera J, Devarie M, Xia X, Ingram D, Dibra D, Somaiah N, Torres K, Ravi V, Ludwig J, Kleinerman E, Li S Universal marker and detection tool for human sarcoma circulating tumor cells. Cancer Res, 2014-01-21;74(6):1645-50. 2014-01-21 [PMID: 24448245] (Bioassay, Human) Bioassay Human
Ortona E, Capozzi A, Colasanti T, Conti F, Alessandri C, Longo A, Garofalo T, Margutti P, Misasi R, Khamashta MA, Hughes GR, Valesini G, Sorice M Vimentin/cardiolipin complex as a new antigenic target of the antiphospholipid syndrome. Blood, 2010-07-15;116(16):2960-7. 2010-07-15 [PMID: 20634382] (Binding Assay, Human) Binding Assay Human

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Blogs on Vimentin. Showing 1-10 of 14 blog posts - Show all blog posts.

Taking Biomarker Discovery From 2D to 3D: Increased Biological Activity of EVs Isolated From 3D Prostate Cancer Cultures
Jamshed Arslan, Pharm D, PhD Tissues within the human body are made of a three-dimensional (3D) arrangement of cells working together to perform vital functions. The commonly used 2D monolayer cultures have limited ...  Read full blog post.


  Read full blog post.

Antibody treatment can generate microglia-like cells from bone marrow
By Jennifer Sokolowski, MD, PhD.Microglia play important roles in the brain in both homeostatic and pathological conditions, acting to clear debris and dying cells. There is evidence to suggest that microglial dys...  Read full blog post.

Stemness is responsible for onset and metastasis of colorectal cancer
By Jamshed Arslan, Pharm. D., PhD. Colorectal cancer stem cells are a rare subpopulation of colorectal cancer cells that can self-renew and initiate and sustain tumor growth when transplanted into an animal host.1,2 C...  Read full blog post.

The use of Beta Actin (AC-15) as a loading control across multiple species
Actin is a fundamental component of the cytoskeleton, where it has the ability to create and break down actin filament formation in response to various cell needs.  Actin has six highly conserved isoforms, however beta and gamma actin are the two...  Read full blog post.

The use of actin as a loading control in research on fruiting-body development and vegetative growth in Sordaria macrospora research
Sordaria macrospora is a filamentous fungus that serves as very useful system for scientific research due to a short life cycle and easy manipulation.  Just like any other model organism, it is important to have an effective loading control to va...  Read full blog post.

Alpha-smooth muscle actin and the modulation of endothelial and epithelial cell biology
Actin is essential for a wide range of cell functions, ranging from cell division and chromatin remodeling to vesicle trafficking and maintenance of cellular structure. In fact, mislocalization of actin to cell junctions during development leads t...  Read full blog post.

Epithelial-Mesenchymal Transition (EMT) Markers
Epithelial-Mesenchymal Transition (EMT) is the trans-differentiation of stationary epithelial cells into motile mesenchymal cells. During EMT, epithelial cells lose their junctions and apical-basal polarity, reorganize their cytoskeleton, undergo a...  Read full blog post.

CD63: is it pro-metastatic or anti-metastatic?
CD63 is a type II membrane protein belonging to tetraspanin superfamily and it play key roles in the activation of several cellular signaling cascades along with acting as TIMP1 receptor. It is expressed by activated platelets, monocytes,...  Read full blog post.

Vimentin: Regulating EMT and Cancer
Vimentin, a member of the intermediate filament (IF) family, is a protein responsible for maintaining cellular integrity and reducing damage caused by stress. The vimentin protein is ubiquitously expressed in normal mesenchymal cells, and recent resea...  Read full blog post.

Showing 1-10 of 14 blog posts - Show all blog posts.
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Bioinformatics

Gene Symbol VIM
Uniprot