Recombinant Human Zinc finger and BTB domain-containing protein 32(ZBTB32),partial CSB-EP897538HU1
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
(FANCC-interacting protein)(Fanconi anemia zinc finger protein)(Testis zinc finger protein)(Zinc finger protein 538)
Species: (Organism)
Homo sapiens (Human)
Gene Names:
ZBTB32
Tag info:
N-terminal 6xHis-tagged
Target Protein AA Sequence:
MSLPPIRLPSPYGSDRLVQLAARLRPALCDTLITVGSQEFPAHSLVLAGVSQQLGRRGQWALGEGISPSTFAQLLNFVYGESVELQPGELRPLQEAARALGVQSLEEACWRARGDRAKKPDPGLKKHQEEPEKPSRNPERELGDPGEKQKPEQVSRTGGREQEMLHKHSPPRGRPEMAGATQEAQQEQTRSKEKRLQAPVGQRGADGKHGVLTWLRENPGGSEESLRKLPGPLPPAGSLQTSVTPRPSWAEAPWLVGGQPALWSILLMPPRYGIPFYHSTPTTGAWQEVWREQR
Expression Region:
1-294aa
Subcellular Location:
Tissue Specificity:
Protein Length:
Partial
Pathway:
Mol. Weight:
36.5 kDa
Purity:
Greater than 85% as determined by SDS-PAGE.
Form:
Liquid or Lyophilized powder
Buffer:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Research Areas:
Epigenetics and Nuclear Signaling
Function:
Involvement in disease:
Relevance:
DNA-binding protein that binds to the to a 5'-TGTACAGTGT-3' core sequence. May function as a transcriptional transactivator and transcriptional repressor. Probably exerts its repressor effect by preventing GATA3 from binding to DNA. May play a role in regulating the differentiation and activation of helper T-cells.
Reconstitution:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Protein Families:
Reference:
"Insights into strand exchange in BTB domain dimers from the crystal structures of FAZF and Miz1." Stogios P.J., Cuesta-Seijo J.A., Chen L., Pomroy N.C., Prive G.G. J. Mol. Biol. 400:983-997(2010)
