Max ELISA Kit for Mouse(Mus musculus) | EIAab.comMax ELISA Kit for Mouse(Mus musculus)

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Max (Gene name),

Protein max (Protein name ), MAX_MOUSE from NCBI database.

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General Annotation

Antigen Annotation

Predicted Eptitope

Vaild Sequence

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Gene name:

Max(Myn);

Protein name:

Protein max;

Alternative:

Myc-binding novel HLH/LZ protein;Myc-associated factor X;Protein myn;

Organism:

Mouse (Mus musculus).

General Annotation

Sub Unit:

Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MYC or MAD. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Component of some MLL1/MLL complex, at least composed of the core components MLL, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components C17orf49, CHD8, E2F6, HSP70, IN80C, KIAA1267, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (By similarity). Interacts with SPAG9.

Function:

Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC-MAX complex is a transcriptional activator, whereas the MAD-MAX complex is a repressor. CpG methylation of the recognition site greatly inhibits DNA binding, suggesting that DNA methylation may regulate the MYC/MAX complex in vivo. May repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity.

Subcellular Location:

Nucleus

Protein Attributes:

Sequence length:

160

Sequence:

50:

100:

150:

160:

SRKKLRMEAS |

3D Structure:

N/A

Predicted Eptitope:

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Vaild Sequence:

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Related Databases

UniGene:

Mm.268548

String:

P28574

SMR:

P28574

STRING:

10090.ENSMUSP00000106025

Pfam:

PF00010

Uniprot:

P28574

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ELISA Kit for Mouse Protein max

Cat.:

E0404h

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Manual:

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MSDS:

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Packing:

96T

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ELISA Kit for Mouse Protein max

Cat.:

E0404m

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MSDS:

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Packing:

96T

ELISA Kit for Mouse Protein max

Cat.:

E0404c

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MSDS:

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Packing:

96T

ELISA Kit for Mouse Protein max

Cat.:

E0404r

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MSDS:

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Packing:

96T

CLIA Kit for Mouse Protein max

Cat.:

U0404m

Price:

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MSDS:

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Packing:

96T

CLIA Kit for Mouse Protein max

Cat.:

U0404c

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MSDS:

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Packing:

96T

CLIA Kit for Mouse Protein max

Cat.:

U0404h

Price:

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Manual:

Looking for manual.

MSDS:

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Packing:

96T

Range:

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CLIA Kit for Mouse Protein max

Cat.:

U0404r

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MSDS:

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Packing:

96T

Polyclonal Antibody for Mouse Protein max

Cat.:

P0404Rb-r

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Packing:

40ug/0.2ml

Polyclonal Antibody for Mouse Protein max

Cat.:

P0404Rb-h

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Packing:

40ug/0.2ml

Polyclonal Antibody for Mouse Protein max

Cat.:

P0404Rb-m

Price:

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Packing:

40ug/0.2ml

Monoclonal Antibody for Mouse Protein max

Protein for Mouse Protein max

R&D Technical Data

For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.

Precision

For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.

Recovery

For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.

Linearity

For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.

References

1.

"Association of Myn, the murine homolog of max, with c-Myc stimulates methylation-sensitive DNA binding and ras cotransformation."
Prendergast G.C. , Lawe D. , Ziff E.B.
Cell65:395-407(1991) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA]
2.

"JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors."
Lee C.M. , Onesime D. , Reddy C.D. , Dhanasekaran N. , Reddy E.P.
Proc. Natl. Acad. Sci. U.S.A.99:14189-14194(2002) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH SPAG9
3.

"Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper."
Lavigne P. , Crump M.P. , Gagne S.M. , Hodges R.S. , Kay C.M. , Sykes B.D.
J. Mol. Biol.281:165-181(1998) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: STRUCTURE BY NMR OF 70-102 IN COMPLEX WITH MYC

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