Recombinant Pig Heat shock protein beta-1 (HSPB1)

Code
MSDS	MSDS Datasheet
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Source
Conjugate
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Target Background

Product Details

Abbreviation

HSPB1

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)

Source

Yeast

Expression Region

1-207

Target Protein Sequence

MTERRVPFSL LRSPSWDPFR DWYPAHSRLF DQAFGLPRLP EEWSQWLSHS GWPGYVRPLP PPAIEGPAAV AAPAYSRLLS RQLSSGVSEI QQTADRWRVS LDVNHFAPEE LTVKTKDGVV EITGKHEERQ DEHGFISRCF TRKYTLPPGV DPTQVSSSLS PEGTLSVEAP LPKPATQSAE ITIPVTFEAR AQLGGTEAGK SEKPGTK
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

full length protein

Tag Info

N-terminal His-tagged/Tag-Free
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.

Storage Condition

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.

Shelf Life

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

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

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
It indicated that Hsp27 was required for porcine circovirus type 2 replication in PK-15 cells culture. PMID:24907481
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
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
Data suggest that targeting HSP27 might offer a useful strategy in cancer treatment. PMID:22589302
Data show that the expression of HSP27 and CLIC1 was strongly positive in 61 (59.2%) and 49 cases (47.6%), respectively. PMID:21858536
Data suggest that HSP27 enhanced the metastatic property of NPC cells probably via the NF-kappaB-mediated activation of MMPs. PMID:21717573
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
HSP27 could be a good candidate involved in migration and/or function of neutrophils within the porcine endmetrium. PMID:20541878
HSP27 and HSP70 may be used as differential markers to distinguish conventional and low grade central osteosarcoma. PMID:20632817
HSP-27 and HSP-70 contribute to modulation of K(+) channel-induced pial artery dilation PMID:15908467
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
Extremely low frequency magnetic field exposure affected the cellular distribution of Hsp27; in particular a partial relocalization in the nucleus was observed. PMID:17080460
Hsp27 is dephosphorylated by PP2A in dorsal ruffles, in non-caveolar lipid raft microdomains. PMID:19109948