Technical Data
L2200
Lim-1 (Homeobox Protein Lim1, LIM Homeobox Protein 1, LHX1, LIM/Homeobox Protein Lhx1, MGC126723, MGC138141)
Description:
The LIM motif defines a zinc-binding domain that is found in a variety of transcriptional regulators and proto-oncogenes products. LIM domain mediates protein-protein interactions and, with LIM-homeodomain proteins, act as negative regulators of the transcriptional activation function of the protein. This transcription factor is required for embryonic survival and for the determination of many cell types.

Applications:
Suitable for use in Immunohistochemistry, Western Blot, Immunocytochemistry and Immunoprecipitation. Not suitable for Immunofluorescence. Other applications have not been tested.

Recommended Dilutions:
Immunohistochemistry (Paraffin): 1:200-1:1000 (Fish and whole mounts: 1:500) Recommended fixative MEMFA.
Western Blot: 1:3000-1:6000
Immunocytochemistry: 1:500 on P19 cell line
Immunoprecipitation: 1:200
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
TypeIsotypeCloneGrade
PabIgGPurified
SizeStorageShippingSourceHost
100ug-20CBlue IceFrogRabbit
Concentration:
~1mg/ml
Immunogen:
Synthetic peptide corresponding to C-terminal portion of frog Lim-1.
Purity:
Purified
Form
Supplied as a liquid in 0.02M PBS, pH 7.6, 0.1% sodium azide.
Specificity:
Recognizes frog Lim-1. Does not crossreact with Lim-5 (the closest homolog of Lim-1 in frog) on tissue sections but does crossreact with Lim-5 in Western Blot and Immunoprecipitation. Species Crossreactivity: human, rat, mouse and fish. Also reacts with Lim-1 from whole-mount fish embryo.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Karavanov, A., et al., Int. J. Dev. Biol. 40: 453462 (1996).