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SPTBN1 antibody (AA 2101-2189)

The Mouse Monoclonal anti-SPTBN1 antibody has been validated for WB and IF. It is suitable to detect SPTBN1 in samples from Human, Mouse, Rat and Dog. There are 3+ publications available.
Catalog No. ABIN968882

Quick Overview for SPTBN1 antibody (AA 2101-2189) (ABIN968882)

Target

See all SPTBN1 Antibodies
SPTBN1 (Spectrin Beta, Non-Erythrocytic 1 (SPTBN1))

Reactivity

  • 30
  • 21
  • 16
  • 4
  • 4
  • 4
  • 4
  • 3
  • 2
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
Human, Mouse, Rat, Dog

Host

  • 25
  • 10
Mouse

Clonality

  • 24
  • 11
Monoclonal

Conjugate

  • 24
  • 2
  • 2
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
This SPTBN1 antibody is un-conjugated

Application

  • 28
  • 14
  • 11
  • 8
  • 5
  • 4
  • 2
  • 1
Western Blotting (WB), Immunofluorescence (IF)

Clone

42-B
  • Binding Specificity

    • 5
    • 3
    • 2
    • 2
    • 2
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    AA 2101-2189

    Cross-Reactivity

    Dog (Canine), Mouse (Murine), Rat (Rattus)

    Characteristics

    1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
    2. Please refer to us for technical protocols.
    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. Source of all serum proteins is from USDA inspected abattoirs located in the United States.

    Purification

    The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.

    Immunogen

    Human beta-Spectrin II aa. 2101-2189

    Isotype

    IgG1
  • Application Notes

    For western blot analysis use at 1:1000.

    Comment

    Related Products: ABIN968537

    Restrictions

    For Research Use only
  • Format

    Liquid

    Concentration

    250 μg/mL

    Buffer

    Aqueous buffered solution containing BSA, glycerol, and ≤0.09 % sodium azide.

    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

    Storage Comment

    Store undiluted at -20° C.
  • Nicolas, Fournier, Galand, Malbert-Colas, Bournier, Kroviarski, Bourgeois, Camonis, Dhermy, Grandchamp, Lecomte: "Tyrosine phosphorylation regulates alpha II spectrin cleavage by calpain." in: Molecular and cellular biology, Vol. 22, Issue 10, pp. 3527-36, (2002) (PubMed).

    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).

  • Target

    SPTBN1 (Spectrin Beta, Non-Erythrocytic 1 (SPTBN1))

    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. This antibody is routinely tested by the Western blot analysis.

    Molecular Weight

    280 kDa

    Pathways

    Regulation of Actin Filament Polymerization, Protein targeting to Nucleus
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