Recombinant Pig Heat shock protein beta-1(HSPB1)

Code CSB-YP732844PI
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Source Yeast
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Code CSB-EP732844PI
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Source E.coli
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Code CSB-EP732844PI-B
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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-BP732844PI
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Source Baculovirus
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Code CSB-MP732844PI
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names HSPB1
Uniprot No. Q5S1U1
Alternative Names HSPB1; HSP27; Heat shock protein beta-1; HspB1; Heat shock 27 kDa protein; HSP 27
Species Sus scrofa (Pig)
Expression Region 1-207
Protein Length full length protein
Tag Info The following tags are available.
N-terminal His-tagged
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.
and FAQs
Protein 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

Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Plays a role in stress resistance and actin organization. Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins.
Gene References into Functions
  1. Here, heat shock protein 27 (Hsp27) has been identified as a novel binding partner of NS5A, a protein functioning in classical swine fever virus genome replication. Further findings clearly demonstrate that the inhibition of viral replication by Hsp27 is mediated via the NF-kappaB signaling pathway. PMID: 29525670
  2. It indicated that Hsp27 was required for porcine circovirus type 2 replication in PK-15 cells culture. PMID: 24907481
  3. HSP27 expression is gut region- and cell type-specific in response to dietary components, microbes, and microbial metabolites to which the mucosa surface is exposed. PMID: 24763551
  4. These results indicate that Hsp27 expression in the porcine gut could be associated with specific dietary fiber components but not the overall microbiota diversity. PMID: 23365273
  5. Data suggest that targeting HSP27 might offer a useful strategy in cancer treatment. PMID: 22589302
  6. Data show that the expression of HSP27 and CLIC1 was strongly positive in 61 (59.2%) and 49 cases (47.6%), respectively. PMID: 21858536
  7. Data suggest that HSP27 enhanced the metastatic property of NPC cells probably via the NF-kappaB-mediated activation of MMPs. PMID: 21717573
  8. Hsp27 expression and its direct chaperoning interaction increase Akt stability and p21 phosphorylation and nuclear-to-cytoplasm translocation, both essential effects for the survival of ultraviolet-induced DNA-damaged cells. PMID: 20858736
  9. HSP27 could be a good candidate involved in migration and/or function of neutrophils within the porcine endmetrium. PMID: 20541878
  10. HSP27 and HSP70 may be used as differential markers to distinguish conventional and low grade central osteosarcoma. PMID: 20632817
  11. HSP-27 and HSP-70 contribute to modulation of K(+) channel-induced pial artery dilation PMID: 15908467
  12. HSP27 in the retinas of 1-day-old piglets and showed that it was enhanced in the retinas of 6-month-old adult. And was seen mainly in ganglion cell bodies in the ganglion cell layer, and in some processes of astrocytes in the innermost nerve fiber layer. PMID: 16930837
  13. Extremely low frequency magnetic field exposure affected the cellular distribution of Hsp27; in particular a partial relocalization in the nucleus was observed. PMID: 17080460
  14. Hsp27 is dephosphorylated by PP2A in dorsal ruffles, in non-caveolar lipid raft microdomains. PMID: 19109948

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Subcellular Location Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle.
Protein Families Small heat shock protein (HSP20) family
Database Links

KEGG: ssc:493184

STRING: 9823.ENSSSCP00000008216

UniGene: Ssc.5832

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