Recombinant Human Stress-Induced-Phosphoprotein 1 (STIP1) Protein (His-SUMO)

Name: Recombinant Human Stress-Induced-Phosphoprotein 1 (STIP1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09992P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins, Recombinant proteins fall special offers - full-length proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Stress-Induced-Phosphoprotein 1 (STIP1) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P31948
Target Symbol	STIP1
Synonyms	Epididymis secretory sperm binding protein Li 94n; HEL S 94n; Hop; Hsc70/Hsp90 organizing protein; Hsc70/Hsp90-organizing protein; IEF SSP 3521; NY REN 11 antigen; P60; Renal carcinoma antigen NY-REN-11; STI1; STI1L; STIP1; STIP1_HUMAN; Stress induced phosphoprotein 1; Stress-induced-phosphoprotein 1; Transformation sensitive protein IEF SSP 3521; Transformation-sensitive protein IEF SSP 3521
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MEQVNELKEKGNKALSVGNIDDALQCYSEAIKLDPHNHVLYSNRSAAYAKKGDYQKAYEDGCKTVDLKPDWGKGYSRKAAALEFLNRFEEAKRTYEEGLKHEANNPQLKEGLQNMEARLAERKFMNPFNMPNLYQKLESDPRTRTLLSDPTYRELIEQLRNKPSDLGTKLQDPRIMTTLSVLLGVDLGSMDEEEEIATPPPPPPPKKETKPEPMEEDLPENKKQALKEKELGNDAYKKKDFDTALKHYDKAKELDPTNMTYITNQAAVYFEKGDYNKCRELCEKAIEVGRENREDYRQIAKAYARIGNSYFKEEKYKDAIHFYNKSLAEHRTPDVLKKCQQAEKILKEQERLAYINPDLALEEKNKGNECFQKGDYPQAMKHYTEAIKRNPKDAKLYSNRAACYTKLLEFQLALKDCEECIQLEPTFIKGYTRKAAALEAMKDYTKAMDVYQKALDLDSSCKEAADGYQRCMMAQYNRHDSPEDVKRRAMADPEVQQIMSDPAMRLILEQMQKDPQALSEHLKNPVIAQKIQKLMDVGLIAIR
Expression Range	1-543aa
Protein Length	Full Length
Mol. Weight	78.6kDa
Research Area	Signal Transduction
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	Acts as a co-chaperone for HSP90AA1. Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90.
Subcellular Location	Cytoplasm. Nucleus. Dynein axonemal particle.
Database References	HGNC: 11387 OMIM: 605063 KEGG: hsa:10963 STRING: 9606.ENSP00000305958 UniGene: PMID: 29673672 Significant genetic association was identified at the rs2236647 (T/C) SNP in STIP1 and risk of asthma (p < 0.001). The C allele and CC genotype of this SNP were significantly higher in asthmatics compared with controls. PMID: 29749828 Functional studies showed that STIP1 promoted the growth, colony formation and migration of cancer cells. However, knocking down the expression of STIP1 inhibited the growth, colony formation and migration of cancer cells. PMID: 29596884 In vitro experiments revealed that STIP1 was capable of binding to the MMP-9 promoter and enhanced its transcriptional expression PMID: 29304094 STIP1 modulates the function of the HSP90-JAK2-STAT3 complex PMID: 27409672 Hsp70/Hsp90-organizing protein promoter activity was highest in Hs578T which expressed mutant or inactive p53. HRAS activation of the Hsp70/Hsp90-organizing protein promoter was inhibited by p53 overexpression. PMID: 27987076 the modulation of HOP-PrP(C) engagement or the decrease of PrP(C) and HOP expression may represent a potential therapeutic intervention in glioblastoma. PMID: 28412969 In conclusion, STIP1 is upregulated in HCC and associated with poor clinical prognosis. Blocking STIP1 activity suppresses HCC cell growth, providing the rationale for STIP1 as a potential therapeutic target in HCC. PMID: 28887036 Data suggest that calcium signaling plays important role in prevention of protein misfolding; complexes of S100A1 and STIP1 are key players in this pathway; the stoichiometry of S100A1/STIP1 interaction appears to be three S100A1 dimers plus one STIP1 monomer; each S100A1-STIP1-binding interaction is entropically driven. (S100A1 = S100 calcium binding protein A1; STIP1 = stress-induced-phosphoprotein 1) [REVIEW] PMID: 28819010 Results indicte the great potential of STIP1 (stress-induced phosphoprotein 1) as a biomarker and therapeutic target in renal cell carcinoma (RCC) bone metastasis. PMID: 28199984 Data suggest that three dimers of S100A1 (S100 calcium binding protein A1) associate with one molecule of STIP1 (stress-inducible phosphoprotein 1) in a calcium-dependent manner; individual STIP1 TPR (tetratricopeptide repeat) domains, TPR1, TPR2A and TPR2B, bind a single S100A1 dimer with significantly different affinities; TPR2B domain possesses highest affinity for S100A1. PMID: 28408431 Data confirmed the significant up-regulation of STIP1 in tumorous cholangiocytes relative to normal hepatocytes and non-tumorous cells and show prooved it as a reliable diagnostic biomarker when using immunohistochemistry. PMID: 25034945 STIP1 and moesin may be novel and differential sero-diagnostic markers for psoriasis vulgaris and psoriatic arthritis PMID: 25010044 Stip1 has a role in the male reproductive system and is expressed during the stress response PMID: 25311551 Increased STIP1 expression is associated with poor survival outcome in epithelial ovarian cancer (EOC), and STIP1 may represent a useful therapeutic target in EOC patients. PMID: 24488757 our findings provide evidences that positive expression of STIP1 in papillary thyroid carcinoma may be important in the acquisition of an aggressive phenotype PMID: 24163084 These results indicate that HOP is a unique co-chaperone that undergoes an ATP-dependent conformational change. PMID: 24535459 STIP1 histoscores may be useful in detecting invasive human ovarian cancer in patients with low serum CA125 levels. PMID: 23915849 stress-inducible protein-1 has a role in recruitment of bone marrow derived cells into the ischemic brains PMID: 23836498 results show phosphorylation of the C-terminal region of Hsp70 and Hsp90 is critical for the decision between folding or degradation of client proteins by altering the binding of CHIP and HOP; also show increased phosphorylation in cancer cells with increased levels of the co-chaperone HOP PMID: 22824801 Luminal iron levels govern intestinal tumorigenesis after Apc loss in vivo. PMID: 22884369 HOP as a novel regulator of angiogenesis that functions through promoting vascular endothelial cell polarization and migration PMID: 22558459 STIP-1 is an antigenic target in cultured hippocampal neurons in sera and/or cerebrospinal fluids of patients with neuro-Behcet's disease. PMID: 21875754 We found no genome-wide statistically significant associations but identified several plausible candidate genes among findings at p < 5E-05: STIP1, TMEM132D, LRRC7, SEMA3A, and ALK. PMID: 21784300 High STIP1 is associated with pancreatic Cancer. PMID: 21470770 This study has revealed that Rho GDP-dissociation inhibitor 2, Y-box binding protein 1, and the HSP70/90 organizing protein have a critical role to play in resistance to cyclin-depedent kinases inhibitor. PMID: 21067243 show that stress-induced phosphoprotein 1 (STIP1) was secreted by ovarian cancer tissues into the peripheral blood of patients, resulting in a significant increase of serum levels of STIP1 in cancer patients compared with those in normal controls PMID: 20501939 Presented: Hop-D456G, a Hop mutant within the TPR2B-domain, that is a mixture of monomeric and dimeric species, suggesting the TPR2B-domain may also play a role in dimerization. PMID: 19961430 Sedimentation equilibrium AUC clearly shows that HOP is a monomer, with no indication of higher MW species. An in vivo coexpression assay that also supports the conclusion that HOP is a monomer. PMID: 19866486 TPR1 and TPR2A domains of the Hsp70/Hsp90 adapter protein p60/Hop specifically bind to short peptides corresponding to the C-terminal tails of Hsp70 and Hsp90 PMID: 11877417 Hsp70/Hsp90 organizing protein (Hop) coordinates Hsp70 and Hsp90 interactions during assembly of steroid receptor complexes. PMID: 15632128 STI1 is secreted by and induces proliferation in glioma cells, an effect that is modulated by the Erk and PI3K pathways. STI1 does not induce proliferation of normal glia, in contrast to glioma cells. PMID: 17886292 It is likely that Hop binds to both monomers of Hsp90 in the form of a clamp, interacting with residues in the middle domain of Hsp90, preventing ATP hydrolysis, possibly by the preventing binding of N-terminal and middle domains in Hsp90 monomers. PMID: 18485364 STIP1 genetic variations might play a role in regulating corticosteroid response in asthmatic subjects with reduced lung function. PMID: 19254810

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.