Recombinant Human Serine-Threonine Kinase Receptor-Associated Protein (STRAP) Protein (GST)

Name: Recombinant Human Serine-Threonine Kinase Receptor-Associated Protein (STRAP) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08642P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Serine-Threonine Kinase Receptor-Associated Protein (STRAP) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9Y3F4
Target Symbol	STRAP
Synonyms	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)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MAMRQTPLTCSGHTRPVVDLAFSGITPYGYFLISACKDGKPMLRQGDTGDWIGTFLGHKGAVWGATLNKDATKAATAAADFTAKVWDAVSGDELMTLAHKHIVKTVDFTQDSNYLLTGGQDKLLRIYDLNKPEAEPKEISGHTSGIKKALWCSEDKQILSADDKTVRLWDHATMTEVKSLNFNMSVSSMEYIPEGEILVITYGRSIAFHSAVSLDPIKSFEAPATINSASLHPEKEFLVAGGEDFKLYKYDYNSGEELESYKGHFGPIHCVRFSPDGELYASGSEDGTLRLWQTVVGKTYGLWKCVLPEEDSGELAKPKIGFPETTEEELEEIASENSDCIFPSAPDVKA
Expression Range	1-350aa
Protein Length	Full Length
Mol. Weight	65.4kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location	Cytoplasm. Nucleus. Note=Localized predominantly in the cytoplasm but also found in the nucleus.
Protein Families	WD repeat STRAP family
Database References	HGNC: 30796 OMIM: 605986 KEGG: hsa:11171 STRING: 9606.ENSP00000392270 UniGene: PMID: 26910283 Findings illuminated a novel STRAP-NOTCH1-HES1 molecular axis as a CSC regulator in colorectal cancer. PMID: 28827371 MAWD and MAWBP were downregulated and associated with the differentiation grade in GC tissues. PMID: 26373288 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 Strap augments the apoptotic effects of mitochondrial p53. PMID: 25168243 Coexpression of MAWBP and MAWD inhibited epithelial mesenchymal transformation, and EMT-aided malignant cell progression was suppressed in gastric cancer. PMID: 23687415 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 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 STRAP protein decreases ubiquitination of intracellular domain of Notch3 and may help to stabilize it. PMID: 21502811 B-MYB acts as a positive regulator of STRAP PMID: 21148321 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 STRAP can act as a negative regulator of ASK1. PMID: 19880523 unrip functions in the pathway of small nuclear ribonucleoproteins biogenesis PMID: 15848170 biochemical evidence for the existence of another, yet atypical, SMN complex component, termed unr-interacting protein (unrip) PMID: 16159890 STRAP acts as an intermediate signaling molecule linking between the phosphatidylinositol 3-kinase/PDK1 and the TGF-beta signaling pathways PMID: 16251192 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 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 These results indicate that upregulation of STRAP might play a role in tumor development as an early event for colorectal cancers. PMID: 17316412 an interplay between PPM1G and unrip determine compartment-specific phosphorylation patterns, localization, and function of the SMN complex PMID: 17984321 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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.