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Purified Mouse Anti-Melusin
Product Details
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BD Transduction Laboratories™
Rat (QC Testing), Human, Mouse (Tested in Development)
Mouse IgG1
Mouse Melusin aa. 61-258
Western blot (Routinely Tested), Immunofluorescence (Tested During Development)
38 kDa
250 µg/ml
AB_399374
Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.
RUO


Preparation And Storage

The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography. Store undiluted at -20°C.

Recommended Assay Procedures

Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml.

Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Please refer to www.bdbiosciences.com/us/s/resources 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.
611894 Rev. 1
Antibody Details
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42/Melusin

Integrins are membrane receptors that mediate cell-cell or cell-matrix adhesion. All integrins are transmembrane heterodimers composed of α and β subunits that are connected to the cytoskeleton. In mammals, at least 17 α subunits and 8 β subunits have been identified, and these proteins can heterodimerize to form at least 22 different receptors. The β1 subgroup of the integrin receptors consists of at least 6 different dimer combinations. A variety of signal transduction proteins have been shown to bind the cytoplamic domain of β1 integrins. These include melusin, ILK, ICAP, and RACK1. Melusin is expressed preferentially in muscle and heart, and contains putative SH3 domain binding motifs in the N-terminal region, two putative SH2 binding sites, and a C-terminal acidic amino acid stretch (CAAS) similar to the calcium binding proteins, calreticulin and calsequestrin. In muscle, melusin protein is localized in two rows flanking α-actinin at Z-lines, and melusin mRNA is upregulated during neonatal development. Differentiation of C2C12 murine myogenic cell line by serum starvation also upregulates melusin protein and mRNA. Thus, melusin may be an important signal transducer for β1 integrins during muscle development.

611894 Rev. 1
Format Details
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Purified
Tissue culture supernatant is purified by either protein A/G or affinity purification methods. Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. This format provides pure antibody that is suitable for a number of downstream applications including: secondary labeling for flow cytometry or microscopy, ELISA, Western blot, etc.
Purified
611894 Rev.1
Citations & References
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Development References (1)

  1. Brancaccio M, Guazzone S, Menini N, et al. Melusin is a new muscle-specific interactor for beta(1) integrin cytoplasmic domain. J Biol Chem. 1999; 274(41):29282-29288. (Biology). View Reference
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Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims.  Comparisons are not made against non-BD technologies, unless otherwise noted.

Non-IVD products are For Research Use Only. Not for use in diagnostic or therapeutic procedures.

 

23-22940-00