Brevican (BCAN) (AA 232-394) antibody

Details for Product No. ABIN968236
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Antigen
Synonyms fi32a12, wu:fi32a12, BCAN, Xbcan, Cspg7, ALPBRE, BEHAB, CSPG7
Epitope
AA 232-394
(18), (8), (7), (3), (2), (1), (1), (1), (1), (1)
Reactivity
Rat (Rattus)
(20), (19), (3), (3)
Host
Mouse
(24), (15), (1)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Western Blotting (WB), Immunofluorescence (IF)
(37), (19), (12), (12), (9), (3), (3), (1), (1), (1)
Pubmed 3 references available
Quantity 150 μg
Options
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Catalog No. ABIN968236
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Immunogen Rat Brevican
Clone 2
Isotype IgG1
Cross-Reactivity Mouse (Murine), Dog (Canine)
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
4. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
Purification Purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name Brevican
Background Neural tissue expresses a variety of cell surface heparan sulfate and extracellular chondroitin sulfate containing proteoglycans. Brevican, a chondroitin sulfate proteoglycan, is a member of the lectican family. Other members of this family are aggrecan, versican, and neurocan. These proteins are either heparan sulfate or keratan sulfate containing glycosylphosphatidylinositol (GPI) anchored or membrane spanning proteoglycans, or soluble chondroitin sulfate containing proteoglycans. Brevican exists as either a soluble or GPI-anchored plasma membrane protein. Brevican contains the shortest core protein of any of the family members. In addition, it is characterized by chondroitin sulfate chains, an N-terminal hyaluronic acid-binding domain (HA), an epidermal growth factor-like (EGF) repeat, and lectin-like and complement regulatory protein-like domains in its C-terminal region. Primary cerebellar astrocytes are the major site for mRNA expression and little, if any, is found in neurons. Although there is an 80 kDa N-terminal truncated form, full length brevican can be up to 145 kDa. Brevican is thought to play a role in the terminal differentiation and regulation of the adult nervous system. This antibody is routinely tested by western blot analysis.
Molecular Weight 140-145 kDa
Research Area Signaling, Extracellular Matrix, Alzheimer's Disease
Comment

Related Products: ABIN968545, ABIN967389

Restrictions For Research Use only
Format Liquid
Concentration 250 µg/ml
Buffer Aqueous buffered solution containing BSA, glycerol.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
anti-Brevican (BCAN) (AA 232-394) antibody Western blot analysis of Brevican on a rat cerebrum lysate. Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of the mouse anti- Brevican antibody.
anti-Brevican (BCAN) (AA 232-394) antibody (2) anti-Brevican (BCAN) (AA 232-394) antibody (Image 2)
Product cited in: Seidenbecher, Richter, Rauch et al.: "Brevican, a chondroitin sulfate proteoglycan of rat brain, occurs as secreted and cell surface glycosylphosphatidylinositol-anchored isoforms." in: The Journal of biological chemistry, Vol. 270, Issue 45, pp. 27206-12, 1995 (PubMed).

Yamada, Watanabe, Shimonaka et al.: "Molecular cloning of brevican, a novel brain proteoglycan of the aggrecan/versican family." in: The Journal of biological chemistry, Vol. 269, Issue 13, pp. 10119-26, 1994 (PubMed).

Aspberg, Miura, Bourdoulous et al.: "The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 94, Issue 19, pp. 10116-21, 1997 (PubMed).

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