STIP1 Mouse
Stress-Induced-Phosphoprotein 1 Mouse Recombinant
Cat. No.
BT4319
Source
Escherichia Coli.
Synonyms
Hop, p60, Sti1, STI1, mSTI1, Stress-induced-phosphoprotein
1, Hsc70/Hsp90-organizing protein.
Appearance
Sterile Filtered clear colorless solution.
Purity
Greater than 95% as determined by SDS-PAGE.
Usage
THE BioTeks products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs 
In Stock 
Description
STIP1 Mouse Recombinant produced in E.coli is a single,
non-glycosylated polypeptide chain containing 563 amino acids (1-543) and
having a molecular mass of 64.7kDa. STIP1 is fused to a 20 amino acid His-tag at N-terminus
& purified by proprietary chromatographic techniques.
Product Specs
Introduction
STIP1, also known as Stress-induced-phosphoprotein 1, is an adaptor protein that links the functions of HSP70 and HSP90 in the protein folding pathway. It facilitates the transfer of client proteins from HSP70 to HSP90 by simultaneously binding to both HSP90 and substrate-bound HSP70. STIP1 exhibits a regulatory role over these chaperones by stimulating the ATPase activity of HSP70 while inhibiting that of HSP90. This suggests STIP1's influence on the conformational changes and ATPase cycles of both HSP70 and HSP90. Genetic variations in STIP1 have been implicated in the regulation of corticosteroid response among asthmatic individuals experiencing reduced lung function.
Description
Recombinant STIP1 Mouse protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein consists of 563 amino acids, with residues 1-543 representing the STIP1 sequence, and has a molecular weight of 64.7 kDa. A 20 amino acid His-tag is fused to the N-terminus to facilitate purification. The protein undergoes purification using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The STIP1 solution is provided at a concentration of 1 mg/ml and is formulated in a buffer containing 20 mM Tris-HCl (pH 8.0), 0.1 M NaCl, 1 mM DTT, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the STIP1 solution should be kept at 4°C. For extended storage, it is recommended to store the solution at -20°C. The addition of a carrier protein, such as HSA or BSA (0.1%), is advised for long-term storage. Repeated freeze-thaw cycles should be avoided.
Purity
The purity of STIP1 is determined to be greater than 95% using SDS-PAGE analysis.
Synonyms
Hop, p60, Sti1, STI1, mSTI1, Stress-induced-phosphoprotein
1, Hsc70/Hsp90-organizing protein.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH
MEQVNELKEK GNKALSAGNI DDALQCYSEA IKLDPQNHVL YSNRSAAYAK KGDYQKAYED GCKTVDLKPD
WGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNLQLKE GLQNMEARLA ERKFMNPFNL PNLYQKLEND
PRTRSLLSDP TYRELIEQLQ NKPSDLGTKL QDPRVMTTLS VLLGVDLGSM DEEEEAATPP PPPPPKKEPK
PEPMEEDLPE NKKQALKEKE LGNDAYKKKD FDKALKHYDR AKELDPTNMT YITNQAAVHF EKGDYNKCRE
LCEKAIEVGR ENREDYRQIA KAYARIGNSY FKEEKYKDAI HFYNKSLAEH RTPDVLKKCQ QAEKILKEQE
RLAYINPDLA LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PRDAKLYSNR AACYTKLLEF QLALKDCEEC
IQLEPTFIKG YTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD SPEDVKRRAM
ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI AIR.
Product Science Overview
Gene and Protein Structure
Function and Mechanism
STIP1 acts as an adaptor protein that coordinates the functions of Hsp70 and Hsp90 in protein folding. It assists in the transfer of proteins from Hsp70 to Hsp90 by binding both Hsp90 and substrate-bound Hsp70 . This interaction is crucial for the proper folding and stabilization of proteins, especially under stress conditions.
Role in Disease
Research has shown that increased levels of STIP1 can have both protective and deleterious effects, depending on the context. For instance, in the context of Alzheimer’s disease (AD), elevated levels of STIP1 have been found to accelerate amyloid-β deposition in a mouse model, which worsens neurotoxicity and spatial memory deficits . This suggests that while STIP1 can protect neurons in vitro, its overexpression in vivo may contribute to disease pathology.
Experimental Findings
Genetic Studies
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