Human Brevican Alexa Fluor® 700-conjugated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

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 upregulated in astrocytes following brain injury (2, 14). In human and rat, an under-glycosylated form of brevican is upregulated 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.

Product Datasheets

Related Research Areas

• Hyaluronan (HA) and HA-binding Proteins
• Proteoglycans