Boster Immunoleader

antibody

Anti-MAX Antibody

PA1768

100 ug/vial

200 USD

polyclonal

rabbit

human, mouse, rat

Anti-MAX Antibody

PA1768

Polyclonal

Rabbit IgG polyclonal antibody for Protein max(MAX) detection. Tested with WB in Human;Mouse;Rat.

200 USD

Rabbit IgG

100 ug/vial

Lyophilized

No cross reactivity with other proteins.

Reacts with: human Predicted to work with: mouse, rat

WB

Concentration: 0.1-0.5μg/ml; Tested Species: Human; Predicted Species: Mouse, Rat

Tested Species: In-house tested species with positive results. Predicted Species: Species predicted to be fit for the product based on sequence similarities. Other applications have not been tested. Optimal dilutions should be determined by end users.

A synthetic peptide corresponding to a sequence at the N-terminus of human MAX(32-48aa ERKRRDHIKDSFHSLRD), identical to the related rat and mouse sequences.

Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.

Immunogen affinity purified.

Add 0.2ml of distilled water will yield a concentration of 500ug/ml.

At -20˚C for one year. After reconstitution, at 4˚C for one month. It can also be aliquotted and stored frozen at -20˚C for a longer time. Avoid repeated freezing and thawing.

Boster provides a series of assays reacted with primary antibodies. Antibody can be supported by chemiluminescence kit EK1002 in WB.

MAX(Max protein), also called Myc-associated factor x, is the most conserved dimerization component of the MYC-MAX-MXD1 network of basic helix-loop-helix leucine zipper(bHLHZ) transcription factors that regulate cell proliferation, differentiation, and apoptosis. The conservation of the MAX sequence is particularly high in the bHLHZ domain, which is involved in protein-protein interactions and DNA binding. The MAX gene is located on chromosome 14q23 by fluorescence in situ chromosomal hybridization. Both quasisymmetric heterodimers resemble the symmetric MAX homodimer, albeit with marked structural differences in the coiled-coil leucine zipper regions that explain preferential homo- and heteromeric dimerization of these 3 evolutionarily related DNA-binding proteins. MAX acts as a classic tumor suppressor gene. Normal lymphocytes from patients showed absence of methylation of the MAX promoter and biallelic expression of MAX, which ruled out an imprinting-mediated effect on MAX expression. The ability of these cells to divide, differentiate, and apoptose in the absence of Max demonstrated for the first time that these processes can occur via Max- and possibly Myc-independent mechanisms.

1. Blackwood, E., Eisenman, R. N. Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc.Science 251: 1211-1217, 1991. 2. Gilladoga, A. D., Edelhoff, S., Blackwood, E. M., Eisenman, R. N., Disteche, C. M. Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in situ hybridization. Oncogene 7: 1249-1251, 1992. 3. Hopewell, R., Ziff, E. B. The nerve growth factor-responsive PC12 cell line does not express the Myc dimerization partner Max. Molec. Cell Biol. 15: 3470-3478, 1995.

MAX

Protein max

MYC associated factor X

bHLHd4 antibody bHLHd5 antibody bHLHd6 antibody bHLHd7 antibody bHLHd8 antibody Helix loop helix zipper protein antibody MAX protein antibody MGC10775 antibody MGC11225 antibody MGC18164 antibody MGC34679 antibody MGC36767 antibody Myc associated factor X antibody Myc binding novel HLH/LZ protein antibody Orf 1 antibody Orf1 antibody Protein max antibody

P61244