Spectrin Beta, Non-Erythrocytic 1 (SPTBN1) (AA 2101-2189) antibody

Details for Product No. ABIN968883
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

 
Antigen
Synonyms 9930031C03Rik, AL033301, SPTB2, Spnb-2, Spnb2, elf1, elf3, mKIAA4049, Spnb1, ELF, betaSpII
Epitope
AA 2101-2189
(3), (1), (1), (1), (1)
Reactivity
Human
(15), (7), (7)
Host
Mouse
(15)
Clonality (Clone)
Monoclonal ()
Application
Western Blotting (WB), Immunofluorescence (IF)
(15), (10), (5), (1), (1)
Pubmed 3 references available
Catalog no. ABIN968883
Quantity 150 µg
Price
Contact our Customer Service for availability and price in your country.
Options
Shipping to United States (Change)
Add to Basket

Order hotline:

  • +1 404 474 4654
  • +1 888 205 9894 (TF)
Immunogen Human beta-Spectrin II
Clone BF12
Isotype IgG1
Cross-Reactivity Mouse (Murine), Rat (Rattus), Dog (Canine)
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
3. 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.
4. Please refer to us for technical protocols.
Purification Purified from tissue culture supernatant or ascites by affinity chromatography.
Purity Purified
Alternative Name beta-Spectrin II
Background Spectrins are central components of the cytoskeleton that form a scaffold below the plasma membrane. Spectrins contain two subunits, alpha and ß, which intertwine to form heterodimers that can self associate into elongated tetramers. alpha-spectin I and ß-spectrin I form heterodimers in red blood cells, while nonerythroid mammalian cells contain heterodimers of alpha-spectin I and II with ß-spectrin I to V. The structure of spectrins includes a succession of triple-helical repeats alongwith various domains, such as SH3 domain, EF hands, PH domains, and binding domains for ankyrin, actin, band 4.1, and calmodulin. alpha-spectrin II is a widely expressed non-erythroid alpha-spectrin that contains an SH3 domain, a calmodulin binding site, and two cleavage sites for proteases, such as calpains and caspase-3. ß-spectrin II is a widely expressed non-erythroid ß-spectrin that contains a C-terminal region that interacts with alpha-spectrins and a PH domain. alpha-spectrin II and ß-spectrin II, like many other spectrins, can form heterodimers that can self associate into tetramers, as well as interact with Band 4.1, F-actin, and other proteins near the plasma membrane. This scaffold of cytoskeletal and plasma membrane proteins is critical for the maintenance of cell structure.
Molecular Weight 280 kDa
Comment

Related Products: ABIN968537, ABIN967389

Restrictions For Research Use only
Format Liquid
Concentration 250 µg/ml
Buffer Aqueous buffered solution containing BSA, glycerol.
Preservative Sodium azide
Storage -20 °C
Supplier Images
anti-Spectrin Beta, Non-Erythrocytic 1 (SPTBN1) (AA 2101-2189) antibody Western blot analysis of beta-Spectrin II on a Jurkat cell lysate (Human T-cell leukemia, ATCC TIB-152). Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of the mouse anti- beta-Spectrin II antibody.
anti-Spectrin Beta, Non-Erythrocytic 1 (SPTBN1) (AA 2101-2189) antibody (2) Immunofluorescent staining of Hela cells (Human cervical epitheloid carcinoma, ATCC CCL-2.2).
Product cited in: Hu, Watanabe, Bennett: "Characterization of human brain cDNA encoding the general isoform of beta-spectrin." in: The Journal of biological chemistry, Vol. 267, Issue 26, pp. 18715-22, 1992 (PubMed).

Moon, McMahon: "Generation of diversity in nonerythroid spectrins. Multiple polypeptides are predicted by sequence analysis of cDNAs encompassing the coding region of human nonerythroid alpha-spectrin." in: The Journal of biological chemistry, Vol. 265, Issue 8, pp. 4427-33, 1990 (PubMed).

Nicolas, Fournier, Galand et al.: "Tyrosine phosphorylation regulates alpha II spectrin cleavage by calpain." in: Molecular and cellular biology, Vol. 22, Issue 10, pp. 3527-36, 2002 (PubMed).

Hosts (15)
Reactivities (15), (7), (7)
Applications (15), (10), (5), (1), (1)
Epitopes (3), (1), (1), (1), (1)
back to top