Recombinant Human Heat Shock 70kDa protein 13

Product code: 32-5341

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20 µg
$388.00 

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Amount : 20 µg
Purification : Greater than 95% as determined by SDS-PAGE.
Content : The HSPA13 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 10% glycerol.
Storage condition : Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
AA sequence : MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSELEM QQYLPLPTPK VIGIDLGTTY CSVGVFFPGT GKVKVIPDEN GHISIPSMVS FTDNDVYVGY ESVELADSNP QNTIYDAKRF IGKIFTAEEL EAEIGRYPFK VLNKNGMVEF SVTSNETITV SPEYVGSRLL LKLKEMAEAY LGMPVANAVI SVPAEFDLKQ RNSTIEAANL AGLKILRVIN EPTAAAMAYG LHKADVFHVL VIDLGGGTLD VSLLNKQGGM FLTRAMSGNN KLGGQDFNQR LLQYLYKQIY QTYGFVPSRK EEIHRLRQAV EMVKLNLTLH QSAQLSVLLT VEEQDRKEPH SSDTELPKDK LSSADDHRVN SGFGRGLSDK KSGESQVLFE TEISRKLFDT LNEDLFQKIL VPIQQVLKEG HLEKTEIDEV VLVGGSTRIP RIRQVIQEFF GKDPNTSVDP DLAVVTGVAI QAGIDGGFWP LQVSALEIPN KHLQKTNFN.
Alternative Name : Heat shock protein 70kDa family member 13, STCH, Stress 70 protein chaperone microsome-associated 60kD, Microsomal stress-70 protein ATPase core.
Source : Escherichia Coli. HSPA13 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 489 amino acids (23-471a.a.) and having a molecular mass of 54.3 kDa. HSPA13 is fused to a 40 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. HSPA13 belongs to the heat shock protein 70 family and is related to microsomes. Members of this protein family take part in the processing of cytosolic and secretory proteins, in addition to the exclusion of denatured or incorrectly-folded proteins. HSPA13 is known to cooperate with PLIC-1 and PLIC-2, proteins which have a role in the signaling connection between the membrane receptors for thrombospondin and the cytoskeleton.

For Research Use Only. Not for use in diagnostic/therapeutics procedures.

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