SCAND1
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Official Full Name
SCAN domain containing 1 -
Overview
This gene encodes a SCAN box domain-containing protein. The SCAN domain is a highly conserved, leucine-rich motif of approximately 60 aa originally found within a subfamily of zinc finger proteins. This gene belongs to a family of genes that encode an isolated SCAN domain, but no zinc finger motif. This protein binds to and may regulate the function of the transcription factor myeloid zinc finger 1B. Alternate splicing results in multiple transcript variants. -
Synonyms
SCAND1;SCAN domain containing 1;SCAN domain-containing protein 1;RAZ1;SDP1;Leap1;Leucine rich domain interacting protein 1;Pgc2;PPAR gamma cofactor 2;Ppargc2;SCAN domain containing protein 1;SCAN related protein RAZ1;SCAN domain-containing 1;SCAN-related protein RAZ1
Recombinant Proteins
- Human
- Rhesus macaque
- Mouse
- E.coli
- Mammalian Cell
- HEK293
- HEK293T
- GST
- His
- Non
- Myc&DDK
- His&Fc&Avi
| Cat.# | Product name | Source (Host) | Species | Tag | Protein Length | Price |
|---|---|---|---|---|---|---|
| SCAND1-2522H | Recombinant Human SCAND1, GST-tagged | E.coli | Human | GST | 1-179aa | |
| SCAND1-2848H | Recombinant Human SCAN Domain Containing 1, His-tagged | E.coli | Human | His |
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| SCAND1-4087R | Recombinant Rhesus monkey SCAND1 Protein, His-tagged | Mammalian Cell | Rhesus macaque | His |
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| SCAND1-577HCL | Recombinant Human SCAND1 lysate | HEK293 | Human | Non |
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| SCAND1-3494H | Recombinant Human SCAND1 Protein, Myc/DDK-tagged, C13 and N15-labeled | HEK293T | Human | Myc&DDK |
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| SCAND1-3904R | Recombinant Rhesus Macaque SCAND1 Protein, His (Fc)-Avi-tagged | HEK293 | Rhesus macaque | His&Fc&Avi |
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| SCAND1-3904R-B | Recombinant Rhesus Macaque SCAND1 Protein Pre-coupled Magnetic Beads | HEK293 | Rhesus macaque |
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| SCAND1-468H | Recombinant Human SCAND1 Protein, MYC/DDK-tagged | HEK293 | Human | Myc&DDK |
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| Scand1-5702M | Recombinant Mouse Scand1 Protein, Myc/DDK-tagged | HEK293T | Mouse | Myc&DDK |
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Involved Pathway
SCAND1 involved in several pathways and played different roles in them. We selected most pathways SCAND1 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with SCAND1 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|
Protein Function
SCAND1 has several biochemical functions, for example, RNA polymerase II transcription factor activity, sequence-specific DNA binding,identical protein binding,protein binding. Some of the functions are cooperated with other proteins, some of the functions could acted by SCAND1 itself. We selected most functions SCAND1 had, and list some proteins which have the same functions with SCAND1. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| transcription factor activity, sequence-specific DNA binding | GTF2H4,Aff1,TAF4B,L3MBTL1,PPARDB,SLC30A9,EGR3,ZNF182,FOXP2,CEBP1 |
| RNA polymerase II transcription factor activity, sequence-specific DNA binding | TWIST1,SP3,TFDP1B,ERF,PAX6A,ETV4,ERG,FOXI3A,FOXD2,TAL2 |
| identical protein binding | RIPK1,TOPBP1,PPP5C,TTR,BRAF,SMN1,NELL2,GBP5,L1CAM,STIM1 |
| transcription coactivator activity | NFATC4,TFDP1B,ATXN7L3,HINFP,CREBBP,SIX3,TDRD3,MED23,BCL10,GATA3 |
| protein binding | C1orf216,NECAB2,HSPA13,TDO2,NFIX,CDX1,MAL,KRT38,MAP2K5,PNKD |
Interacting Protein
SCAND1 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 SCAND1 here. Most of them are supplied by our site. Hope this information will be useful for your research of SCAND1.
ZKSCAN7;ZNF449;PNMA1;ZKSCAN4;PGBD1;GORASP2;ZNF263
Resources
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References
- Katagiri, F; Takagi, M; et al. Screening of integrin-binding peptides in a laminin peptide library derived from the mouse laminin beta chain short arm regions. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS 550:33-41(2014).
- Tishchenko, VM; et al. Relations between macro- and microstability of C(H)2 domains and human IgG2 and their biological activity: 1. Analysis of calorimetric and optical melting curves. MOLECULAR BIOLOGY 48:414-423(2014).
