Recombinant Human Heat shock protein 105 kDa (HSPH1), partial

Code CSB-YP852885HU
MSDS
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Source Yeast
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Code CSB-EP852885HU
MSDS
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Source E.coli
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Code CSB-EP852885HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP852885HU
MSDS
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Source Baculovirus
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Code CSB-MP852885HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Uniprot No.
Alternative Names
Antigen NY CO 25; Antigen NY-CO-25; DKFZp686M05240; Heat shock 105kD alpha; Heat shock 105kD; Heat shock 105kD beta; Heat shock 105kDa protein 1; Heat shock 105kDa protein; Heat shock 105kDa/110kDa protein 1 ; Heat shock 110 kDa protein; Heat shock 110kDa protein; Heat shock protein 105 kDa; HS105_HUMAN; HSP105; HSP105A; HSP105B; HSP110; HSPH 1; Hsph1; KIAA0201; NY CO 25
Species
Homo sapiens (Human)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
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 before Lyophilization
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℃/-80℃. 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.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release. Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities.
Gene References into Functions
  1. expression not an independent prognostic factor in gastric cancer patients with peritoneal metastasis, but might be a new marker of chemosensitivity PMID: 29204054
  2. Established heat shock protein 110 (HSP110) as a prognostic biomarker of colorectal carcinomas (CRCs) with microsatellite instability-high (MSI-H) by considering the intratumoral heterogeneity of HSP110 expression. The HSP110wt-low MSI-H CRCs were significantly correlated with larger deletions in the HSP110 T17 mononucleotide repeat (>/=4 bp; p < 0.001). PMID: 28971530
  3. HSP110 HT17 alone correctly classified samples judged to be uncertain with the pentaplex panel. PMID: 26831756
  4. deletion of the HSP110 T17 repeat was frequently observed in microsatellite-unstable advanced gastric cancers. PMID: 28811251
  5. Hsp105alpha localizes to the nucleus, interacts with HIF-1alpha and induces HIF-1a accumulation in CoCl2-treated cells. PMID: 28185835
  6. the expression of HSP110 in colon cancer contributes to STAT3-dependent tumor growth PMID: 27819670
  7. About 25% of patients with stages II-III colorectal tumors with microsatellite instability have an excellent response to chemotherapy, due to large, biallelic deletions in the T(17) intron repeat of HSP110 in tumor DNA. PMID: 24512910
  8. HSP105 depletion disrupts the integration of protein phosphatase 2A into the beta-catenin degradation complex, favoring the hyperphosphorylation and degradation of beta-catenin. PMID: 25645927
  9. A receiver operating characteristic curve constructed with HSP105 and TIM gave a sensitivity of 54.3% and 95% (38/40) specificity in discriminating esophageal squamous cell carcinoma from matched controls. PMID: 24157810
  10. we measured the binding of human Hsp72 (HSPA1A) to BAG1, BAG2, BAG3, and the unrelated NEF Hsp105. These studies revealed a clear hierarchy of affinities: BAG3 > BAG1 > Hsp105 >> BAG2. PMID: 24318877
  11. HSPH1 and HSPH2 are bona fide chaperones on their own that collaborate with DNAJA1 and DNAJB1 to hydrolyze ATP and unfold polypeptides and HSPA1A and HSPH1 formed a powerful molecular machinery. PMID: 23737532
  12. High HSP105 expression is associated with Barrett's esophagus. PMID: 22901192
  13. It restricts aggregation of denaturated proteins,plays a role in protein folding in cytoplasms,and enhance expression of hsp70 in cell nucleus.(review) PMID: 22712230
  14. The Hsp105-mediated multilevel regulation of DeltaF508 CFTR folding and quality control provides new opportunities to understand how chaperone machinery regulates the homeostasis and functional expression of misfolded proteins in the cell. PMID: 22505710
  15. A direct correlation between HSP105 expression and lymphoma aggressiveness was also apparent. PMID: 21860023
  16. Hsp105alpha and Hsp105beta suppressed the expanded polyQ tract-induced protein aggregation and apoptosis through the induction of Hsp70. PMID: 20542028
  17. Heat shock protein 105 is overexpressed in a variety of human tumors PMID: 14534695
  18. HSP105 appears to chaperone the responses to endoplasmic reticulum (ER) stress through its interactions with GRP78 and GSK3, and without HSP105 cell death following ER stress proceeds by a non-caspase-3-dependent process. PMID: 18083346
  19. HSP105 analysis may be a helpful tool as a poor prognostic indicator and as a diagnostic aid in problematic lesions. PMID: 18477890
  20. HSP 105 is thought to be a more relevant tumor-associated antigen in malignant melanoma than is HSP 70. PMID: 19476517

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Subcellular Location
Cytoplasm.
Protein Families
Heat shock protein 70 family
Tissue Specificity
Highly expressed in testis. Present at lower levels in most brain regions, except cerebellum. Overexpressed in cancer cells.
Database Links

HGNC: 16969

OMIM: 610703

KEGG: hsa:10808

STRING: 9606.ENSP00000318687

UniGene: Hs.743267

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