>85%, 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
97.7 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.
SDS-PAGE
130-160 kDa, reducing conditions
Publications
Read Publication using 4009-BC in the following applications:
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 PBS and EDTA.
Purity
>85%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 200 μg/mL in sterile deionized water.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Brevican Protein, CF
ALPBRE
BCAN
BEHAB
BEHABbrevican core protein
Brain-enriched hyaluronan-binding protein
Brevican
Chondroitin sulfate proteoglycan 7
chondroitin sulfate proteoglycan BEHAB
chondroitin sulfate proteoglycan BEHAB/brevican
CSPG7
CSPG7brevican proteoglycan
MGC13038
Background
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.
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