SNAI1

  • Official Full Name

    snail homolog 1
  • Overview

    Snail is a zinc-finger transcription factor that can repress E-cadherin transcription. Downregulation of E-cadherin is associated with epithelial-mesenchymal transition during embryonic development, a process also exploited by invasive cancer cells (1-3).
  • Synonyms

    SNAI1;snail homolog 1 (Drosophila);snail 1 (drosophila homolog), zinc finger protein;zinc finger protein SNAI1;SLUGH2;SNA;SNAH;SNAIL;SNAIL1;protein sna;snail 1 homolog;protein snail homolog 1;snail 1 zinc finger protein;snail 1, zinc finger p

Recombinant Proteins

  • Mouse
  • Human
  • Chicken
  • Mammalian Cell
  • HEK293
  • E.coli
  • Wheat Germ
  • Mamanlian cells
  • HEK293T
  • His
  • Myc&DDK
  • His&T7
  • Non
  • Flag
  • His&Fc&Avi
Cat.# Product name Source (Host) Species Tag Protein Length Price
SNAI1-15660M Recombinant Mouse SNAI1 Protein Mammalian Cell Mouse His
SNAI1-16H Recombinant Human SNAI1, MYC/DDK-tagged HEK293 Human Myc&DDK
SNAI1-178H Recombinant Human SNAI1 protein, T7/His-tagged E.coli Human His&T7
SNAI1-30016TH Recombinant Human SNAI1 Wheat Germ Human Non 110 amino acids
SNAI1-330H Recombinant Human snail family zinc finger 1, His-tagged E.coli Human His 1-264 a.a.
SNAI1-6699C Recombinant Chicken SNAI1 Mammalian Cell Chicken His
SNAI1-1643HCL Recombinant Human SNAI1 293 Cell Lysate HEK293 Human Non
SNAI1-2376HFL Recombinant Full Length Human SNAI1, Flag-tagged Mamanlian cells Human Flag Full L.
SNAI1-3405H Recombinant Human SNAI1 Protein (Met1-Arg264), His tagged E.coli Human His Met1-Arg264
SNAI1-4718H Recombinant Human SNAI1 Protein, Myc/DDK-tagged, C13 and N15-labeled HEK293T Human Myc&DDK
Snai1-5989M Recombinant Mouse Snai1 Protein, Myc/DDK-tagged HEK293T Mouse Myc&DDK
SNAI1-8511M Recombinant Mouse SNAI1 Protein, His (Fc)-Avi-tagged HEK293 Mouse His&Fc&Avi
SNAI1-8511M-B Recombinant Mouse SNAI1 Protein Pre-coupled Magnetic Beads HEK293 Mouse

    Involved Pathway

    SNAI1 involved in several pathways and played different roles in them. We selected most pathways SNAI1 participated on our site, such as Adherens junction, which may be useful for your reference. Also, other proteins which involved in the same pathway with SNAI1 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein
    Adherens junction PTPN1,WASL,ACTN1,TCF7,LEF1,NLK,WASF3,TGFBR2,ERBB2,ACP1

    Protein Function

    SNAI1 has several biochemical functions, for example, RNA polymerase II regulatory region sequence-specific DNA binding,kinase binding,metal ion binding. Some of the functions are cooperated with other proteins, some of the functions could acted by SNAI1 itself. We selected most functions SNAI1 had, and list some proteins which have the same functions with SNAI1. You can find most of the proteins on our site.

    Function Related Protein
    metal ion binding CRYAB,ZFP428,NT5C3L,C1GALT1,TNK2,SAP30L,JADE1,KCND2,DAGLB,TOP2B
    transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding BCL11AA,KLF17,ZFP536,POU4F2,TCF3,TCF21,BATF3,ZNF148,NFIL3-4,HHEX
    kinase binding ABI2,JAKMIP1,PFKM,CHP,C2orf44,WWC1,GFAP,WWC2,CEBPA,LDHA
    protein binding TFAP2B,SLC16A3,KIAA1109,NDUFAF3,POLD1,CD36,TIMP1,SCIMP,HNRPDL,DDX5
    RNA polymerase II regulatory region sequence-specific DNA binding FOXK1,BCL6,IRF2,FERD3L,GATA1,AEBP1,ZNF256,PRDM12B,XBP1,ALX1

    Interacting Protein

    SNAI1 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with SNAI1 here. Most of them are supplied by our site. Hope this information will be useful for your research of SNAI1.

    KDM1A

    Resources

    References

    • Ohnuki, K; Umezono, T; et al. Expression of transcription factor Snai1 and tubulointerstitial fibrosis in progressive nephropathy. JOURNAL OF NEPHROLOGY 25:233-239(2012).
    • Li, ZD; Wermuth, PJ; et al. Caveolin-1 Deficiency Induces Spontaneous Endothelial-to-Mesenchymal Transition in Murine Pulmonary Endothelial Cells in Vitro. AMERICAN JOURNAL OF PATHOLOGY 182:325-331(2013).

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