Human HSPBP1 protein (Recombinant) (His-Tag) (STJP016694)
SPECIFICATIONS
HostE.coli
ImmunogenHuman
General Information
| Short Description | Recombinant-Human HSPBP1-His-Tag protein was developed from e.coli and has a target region of His-Tag. For use in research applications. |
| Applications | SDS-PAGE |
| Host | E.coli |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Concentration | 0.5 mg/mL |
| Formulation | Liquid in 20mM Tris-HCl buffer (pH 8.0) containing 2mM DTT, 30% Glycerol, 2mM EDTA, 0.1M NaCl |
| Storage Instruction | For short term storage, keep at +2C to +8C for up to 1 week. For long term storage, aliquot and store at-20C, and avoid repeat freeze-thaw cycles. |
Target Information
| Gene Symbol | HSPBP1 |
| Gene ID | 23640 |
| Uniprot ID | HPBP1_HUMAN |
| Accession Number | AAH01236 |
| Immunogen | Human |
| Immunogen Region | 1-362aa |
| Immunogen Sequence | MGSSHHHHHH SSGLVPRGSH MSDEGSRGSR LPLALPPASQ GCSSGGGGGG GGGSSAGGSG NSRPPRNLQG LLQMAITAGS EEPDPPPEPM SEERRQWLQE AMSAAFRGQR EEVEQMKSCL RVLSQPMPPT AGEAEQAADQ QEREGALELL ADLCENMDNA ADFCQLSGMH LLVGRYLEAG AAGLRWRAAQ LIGTCSQNVA AIQEQVLGLG ALRKLLRLLD RDACDTVR |
Additional Info
| Tissue Specificity | Ubiquitous. |
| Function | Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR. |
| Protein Name | Hsp70-Binding Protein 1Hspbp1Heat Shock Protein-Binding Protein 1Hsp70-Binding Protein 2Hspbp2Hsp70-Interacting Protein 1Hsp70-Interacting Protein 2 |
| Database Links | |
| Cellular Localisation | |
| Alternative Protein Names | Hsp70-Binding Protein 1 proteinHspbp1 proteinHeat Shock Protein-Binding Protein 1 proteinHsp70-Binding Protein 2 proteinHspbp2 proteinHsp70-Interacting Protein 1 proteinHsp70-Interacting Protein 2 proteinHSPBP1 proteinHSPBP proteinPP1845 protein |
Information sourced from Uniprot.org