Recombinant Human Brevican Protein, CF Summary
Product Specifications
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
4009-BC
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS and EDTA. |
| Reconstitution | Reconstitute at 200 μg/mL in sterile deionized water. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Store the unopened product at -20 to -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date. |
Reconstitution Calculator
Background: Brevican
Brevican, also called BEHAB, is a secreted member of the the lectican family of proteoglycans that share a common domain structure (1). Brevican contains an Ig-like V-set domain, two link domains, a Glu-rich region, a central region with glycosaminoglycan (GAG) modifications, an EGF-like domain, a C-type lectin domain, and a C-terminal Sushi/CRP-like domain (2). Brevican is restricted to the CNS and is expressed by astrocytes, oligodendrocytes, and neurons (3-7). A GPI-anchored alternate splice form exists that is truncated following the central (GAG) region (2, 8). Brevican is cleaved by multiple proteases and exists in a number of distinct fragments (5, 9, 10). Full-length brevican consists of a 97 kDa core protein with up to approximately 100 kDa of attached chondroitin sulfate but not heparan sulfate chains (4, 7, 11, 12). Brevican associates with the extracellular matrix, perineuronal nets, and astrocyte cell surfaces by means of its chondroitin sulfate, GPI anchor, hyaluronic acid-binding link domains, and the core protein (4, 7, 8, 13). The secreted isoform is dominant during brain development and is up-regulated in astrocytes following brain injury (2, 14). In human and rat, an under-glycosylated form of brevican is up-regulated in highly aggressive glioma but not in low-grade glioma or other brain pathologies (15, 16). In mouse and rat, levels of an ADAMTS4-generated 55 kDa N-terminal fragment increase during remodeling after excitotoxic injury (11, 12). Human brevican shares 90%, 80%, and 80% aa sequence identity with bovine, mouse, and rat brevican, respectively. Within the Ig-like and two link domains, brevican shares 45%-51% aa sequence identity with aggrecan, neurocan, and versican.
- Viapiano, M.S. and R.T. Matthews (2006) Trends Mol. Med. 12:488.
- Gary, S.C. et al. (2000) Gene 256:139.
- Jaworski, D.M. et al. (1994) J. Cell Biol. 125:495.
- Seidenbecher, C.I. et al. (1995) J. Biol. Chem. 270:27206.
- Hamel, M.G. et al. (2005) J. Neurochem. 93:1533.
- Ogawa, T. et al. (2001) J. Comp. Neurol. 432:285
- Yamada, H. et al. (1997) J. Neurosci. 17:7784.
- Seidenbecher, C.I. et al. (2002) J. Neurochem. 83:738.
- Matthews, R.T. et al. (2000) J. Biol. Chem. 275:22695.
- Nakamura, H. et al. (2000) J. Biol. Chem. 275:38885.
- Mayer, J. et al. (2005) BMC Neurosci. 6:52.
- Yuan, W. et al. (2002) Neuroscience 114:1091.
- Deepa, S.S. et al. (2006) J. Biol. Chem. 281:17789.
- Jaworski, D.M. et al. (1999) Exp. Neurol. 157:327.
- Viapiano, M.S. et al. (2005) Cancer Res. 65:6726.
- Viapiano, M.S. et al. (2003) J. Biol. Chem. 278:33239.
Citation for Recombinant Human Brevican Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
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Cleavage of proteoglycans, plasma proteins and the platelet-derived growth factor receptor in the hemorrhagic process induced by snake venom metalloproteinases
Authors: AF Asega, MC Menezes, D Trevisan-S, D Cajado-Car, L Bertholim, AK Oliveira, A Zelanis, SMT Serrano
Sci Rep, 2020-07-31;10(1):12912.
Species: Snake
Sample Types: Protein
Applications: Bioassay
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