Product Details

Purity

>85% (SDS-PAGE)

Target Names

Hspa2

Uniprot No.

P17156

Alternative Names

Hspa2; Hcp70.2; Hsp70-2; Heat shock-related 70 kDa protein 2; Heat shock protein 70.2

Species

Mus musculus (Mouse)

Expression Region

1-633

Target Protein Sequence

MSARGPAIGI DLGTTYSCVG VFQHGKVEII ANDQGNRTTP SYVAFTDTER LIGDAAKNQV AMNPTNTIFD AKRLIGRKFE DATVQSDMKH WPFRVVSEGG KPKVQVEYKG EMKTFFPEEI SSMVLTKMKE IAEAYLGGKV QSAVITVPAY FNDSQRQATK DAGTITGLNV LRIINEPTAA AIAYGLDKKG CAGGEKNVLI FDLGGGTFDV SILTIEDGIF EVKSTAGDTH LGGEDFDNRM VSHLAEEFKR KHKKDIGPNK RAVRRLRTAC ERAKRTLSSS TQASIEIDSL YEGVDFYTSI TRARFEELNA DLFRGTLEPV EKALRDAKLD KGQIQEIVLV GGSTRIPKIQ KLLQDFFNGK ELNKSINPDE AVAYGAAVQA AILIGDKSEN VQDLLLLDVT PLSLGIETAG GVMTPLIKRN TTIPTKQTQT FTTYSDNQSS VLVQVYEGER AMTKDNNLLG KFDLTGIPPA PRGVPQIEVT FDIDANGILN VTAADKSTGK ENKITITNDK GRLSKDDIDR MVQEAERYKS EDEANRDRVA AKNAVESYTY NIKQTVEDEK LRGKISEQDK NKILDKCQEV INWLDRNQMA EKDEYEHKQK ELERVCNPII SKLYQGGPGG GGSSGGPTIE EVD

Protein Length

Full length protein

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

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.

Target Background

Function

Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells.

Gene References into Functions

Proteolytic degradation of Hspa2 occurs in response to oxidative stress mediated by 4-hydroxynonenal in male germ cells of the mouse. PMID: 27932549
a candidate gene approach revealed that HSPA2 is a prominent molecular target of ELAVL1 PMID: 21737689
NASP controls the ability of HSPA2 to activate CDC2 for CDC2/cyclin B1 complex formation. PMID: 19553603
Data show that NFAT5/TonEBP stimulates transcription of HSP70-2, and is a master regulator of the renal medulla for cellular protection against high osmolality via organic osmolytes and molecular chaperones. PMID: 12138186
high-level testis-specific gene expression requires additional sequences localized upstream of the T2 transcription start site PMID: 14766014
role for HSPA2, which acquires new functions and becomes tightly associated with major spermatid DNA-packaging proteins, transition proteins 1 and 2 PMID: 17035236
Role of Hsp70.2/Hst70 gene in development of the nervous system. PMID: 17047988
Bat3 is identified as a critical regulator of Hsp70-2 in spermatogenesis, thereby providing a possible molecular target in idiopathic male infertility. PMID: 18678708
Hspa2 was detected in central and peripheral nervous system: in neuron's bodies and fiber tracts, in the subventricular zone of the lateral ventricles, in the dentate gyrus of the hippocampus, in enteric ganglia of the gastrointestinal tract PMID: 19462178
Data show that Parp2 interacts significantly with both the transition protein TP2 and the transition chaperone HSPA2, whereas Parp1 binds weakly to HSPA2. PMID: 19607827

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Subcellular Location

Cytoplasm, cytoskeleton, spindle.

Protein Families

Heat shock protein 70 family

Tissue Specificity

Expressed in male germ cells (at protein level).

Database Links

KEGG: mmu:15512

STRING: 10090.ENSMUSP00000079306

UniGene: Mm.296181

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Recombinant Mouse Heat shock-related 70 kDa protein 2 (Hspa2)

Product Details

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Target Background

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