Recombinant Human Serine-threonine kinase receptor-associated protein (STRAP)

Code CSB-EP896713HU
MSDS
Size US$306
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
STRAP
Uniprot No.
Research Area
others
Alternative Names
MAP activator with WD repeats; MAWD; PTWD; Serine-threonine kinase receptor-associated protein; serine/threonine kinase receptor associated protein; strap; STRAP_HUMAN; UNR-interacting protein; UNRIP; WD 40 repeat protein PT WD; WD-40 repeat protein PT-WD
Species
Homo sapiens (Human)
Source
E.coli
Expression Region
1-350aa
Target Protein Sequence
MAMRQTPLTCSGHTRPVVDLAFSGITPYGYFLISACKDGKPMLRQGDTGDWIGTFLGHKGAVWGATLNKDATKAATAAADFTAKVWDAVSGDELMTLAHKHIVKTVDFTQDSNYLLTGGQDKLLRIYDLNKPEAEPKEISGHTSGIKKALWCSEDKQILSADDKTVRLWDHATMTEVKSLNFNMSVSSMEYIPEGEILVITYGRSIAFHSAVSLDPIKSFEAPATINSASLHPEKEFLVAGGEDFKLYKYDYNSGEELESYKGHFGPIHCVRFSPDGELYASGSEDGTLRLWQTVVGKTYGLWKCVLPEEDSGELAKPKIGFPETTEEELEEIASENSDCIFPSAPDVKA
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
65.4kDa
Protein Length
Full Length
Tag Info
N-terminal GST-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
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°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

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Target Background

Function
The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. STRAP plays a role in the cellular distribution of the SMN complex. Negatively regulates TGF-beta signaling but positively regulates the PDPK1 kinase activity by enhancing its autophosphorylation and by significantly reducing the association of PDPK1 with 14-3-3 protein.
Gene References into Functions
  1. these results suggest that STRAP increases invasion and metastasis of colorectal cancer partly through inhibiting ubiquitin-dependent degradation of beta-catenin and promoting Wnt/beta-catenin signaling PMID: 26910283
  2. Findings illuminated a novel STRAP-NOTCH1-HES1 molecular axis as a CSC regulator in colorectal cancer. PMID: 28827371
  3. MAWD and MAWBP were downregulated and associated with the differentiation grade in GC tissues. PMID: 26373288
  4. STRAP inhibits the transactivation function of Sp1 either by directly blocking its DNA binding domain or destabilizing Sp1 protein through ubiquitin-proteasome pathway in cell cycle G1 phase. PMID: 25483064
  5. Strap augments the apoptotic effects of mitochondrial p53. PMID: 25168243
  6. Coexpression of MAWBP and MAWD inhibited epithelial mesenchymal transformation, and EMT-aided malignant cell progression was suppressed in gastric cancer. PMID: 23687415
  7. Data indicate serine-threonine kinase receptor-associated protein (STRAP) as a novel regulator of the coordinated translation of collagen alpha1(I) and alpha2(I) mRNAs. PMID: 23918805
  8. both of the TPR and OB-fold domains localize to the chromatin of p53 target genes and exhibit intrinsic regulatory activity necessary for the Strap-dependent p53 response PMID: 22362889
  9. STRAP protein decreases ubiquitination of intracellular domain of Notch3 and may help to stabilize it. PMID: 21502811
  10. B-MYB acts as a positive regulator of STRAP PMID: 21148321
  11. gonucleotide pulldown identified STRAP (serine/threonine kinase receptor-associated protein) as a further protein recruited to the MMP28 promoter and acting functionally with Sp1. PMID: 20144149
  12. STRAP can act as a negative regulator of ASK1. PMID: 19880523
  13. unrip functions in the pathway of small nuclear ribonucleoproteins biogenesis PMID: 15848170
  14. biochemical evidence for the existence of another, yet atypical, SMN complex component, termed unr-interacting protein (unrip) PMID: 16159890
  15. STRAP acts as an intermediate signaling molecule linking between the phosphatidylinositol 3-kinase/PDK1 and the TGF-beta signaling pathways PMID: 16251192
  16. Gemin8 has an essential role in the proper structural organization of the SMN complex and the involvement of the heteromeric subunit containing Gemin6, Gemin7, Gemin8, and Unrip in the recruitment of Sm proteins to the snRNP assembly pathway PMID: 17023415
  17. the direct interaction of NM23-H1 and STRAP is important for the regulation of TGF-beta-dependent biological activity as well as NM23-H1 activity PMID: 17314099
  18. These results indicate that upregulation of STRAP might play a role in tumor development as an early event for colorectal cancers. PMID: 17316412
  19. an interplay between PPM1G and unrip determine compartment-specific phosphorylation patterns, localization, and function of the SMN complex PMID: 17984321
  20. Strap regulation reflects the coordinated interplay between different DNA damage-activated protein kinases, ATM and Chk2 (Checkpoint kinase 2), where phosphorylation by each kinase provides a distinct functional consequence on the activity of Strap. PMID: 18833288

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Subcellular Location
Cytoplasm. Nucleus. Note=Localized predominantly in the cytoplasm but also found in the nucleus.
Protein Families
WD repeat STRAP family
Database Links

HGNC: 30796

OMIM: 605986

KEGG: hsa:11171

STRING: 9606.ENSP00000392270

UniGene: Hs.743971

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