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Purified Mouse Anti-Id1
Purified Mouse Anti-Id1
Western blot analysis of recombinant human Id1. Purified mouse anti-Id1 antibody (clone B30-1) used at 2 µg/mL recognizes a ~ 45 kDa band on 100 ng of recombinant human Id1-GST protein (Abnova Cat. No. H00003397-P01).  Id1 has a calculated molecular weight of ~ 17 kD and GST at ~28 kDa.
Western blot analysis of recombinant human Id1. Purified mouse anti-Id1 antibody (clone B30-1) used at 2 µg/mL recognizes a ~ 45 kDa band on 100 ng of recombinant human Id1-GST protein (Abnova Cat. No. H00003397-P01).  Id1 has a calculated molecular weight of ~ 17 kD and GST at ~28 kDa.
Product Details
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BD Pharmingen™
Human (QC Testing), Mouse (Tested in Development)
Mouse IgG2a, κ
Mouse Id1 (full-length)-GST Recombinant Protein
Western blot (Routinely Tested)
45 kDa
0.5 mg/ml
AB_396445
Aqueous buffered solution containing ≤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 4°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.
556522 Rev. 5
Antibody Details
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B30-1

Id proteins were originally characterized as inhibitors of DNA binding and cell differentiation.  Id1 through 4 contain an evolutionarily conserved helix-loop-helix (HLH) sequence which is critical for protein-protein interaction(s).  Most HLH transcription factors contain a basic amino acid region adjacent to the HLH sequence, the bHLH sequence, which is responsible for DNA binding.  bHLH transcription factors fall into 2 major groups designated class A factors, such as E2/2 and E47, and class B factors, such as MyoD, myogenin.  In vitro studies demonstrate distinct interaction(s) between Id proteins and bHLH transcription factors.  While Id proteins contain an HLH domain, they lack the basic region which is required for DNA binding.  Therefore, Id proteins are negative regulators of transcription since complexes which contain them do not bind DNA.  Id proteins are variably expressed throughout the cell cycle and are regulated by phosphorylation by cyclin-cdk complexes.  Thus, Id proteins play an important role in transcriptional regulation of cell cycle related genes. Overexpression of Id1 can induce apoptosis in serum-starved fibroblasts and is correlated with cell cycle progression promoted by Id family members. Human Id1 has been reported to have a molecular weight of ~16-17 kDa.  This antibody has been reported to recognize mouse Id1 and not to crossreact with either mouse Id2 or mouse Id3.

This antibody is routinely tested by the western blot analysis.  Other applications were tested at the BD Biosciences Pharmingen during antibody development only or reported in the literature.

556522 Rev. 5
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
556522 Rev.5
Citations & References
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Development References (8)

  1. Cooper CL, Brady G, Bilia F, Iscove NN, Quesenberry PJ. Expression of the Id family helix-loop-helix regulators during growth and development in the hematopoietic system. Blood. 1997; 89(9):3155-3165. (Biology). View Reference
  2. Deed RW, Jasiok M, Norton JD. Nucleotide sequence of the cDNA encoding human helix-loop-helix Id-1 protein: identification of functionally conserved residues common to Id proteins. Biochem Biophys Res Commun. 1994; 1219(1):160-162. (Biology). View Reference
  3. Hara E, Hall M, Peters G. Cdk2-dependent phosphorylation of Id2 modulates activity of E2A-related transcription factors. EMBO J. 1997; 16(2):332-342. (Biology). View Reference
  4. Kadesch T. Consequences of heteromeric interactions among helix-loop-helix proteins. Cell Growth Differ. 1993; 4(1):49-55. (Biology). View Reference
  5. Langlands K, Yin X, Anand G, Prochownik EV. Differential interactions of Id proteins with basic-helix-loop-helix transcription factors. J Biol Chem. 1997; 272(32):19785-19793. (Biology). View Reference
  6. Norton JD, Atherton GT. Coupling of cell growth control and apoptosis functions of Id proteins. Mol Cell Biol. 1998; 18(4):2371-2381. (Biology). View Reference
  7. Norton JD, Deed RW, Craggs G, Sablitzky F. Id helix-loop-helix proteins in cell growth and differentiation. Trends Cell Biol. 1998; 8(2):58-65. (Biology). View Reference
  8. Riechmann V, van Crüchten I, Sablitzky F. The expression pattern of Id4, a novel dominant negative helix-loop-helix protein, is distinct from Id1, Id2 and Id3. Nucleic Acids Res. 1994; 22(5):749-755. (Biology). View Reference
View All (8) View Less
556522 Rev. 5

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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.

For Research Use Only. Not for use in diagnostic or therapeutic procedures.