HSPA6 (1-643, His-tag) Human Protein

CAT#: AR09311PU-N

HSPA6 (1-643, His-tag) human recombinant protein, 0.1 mg


USD 384.00

3 Weeks*

Size
    • 100 ug

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Specifications

Product Data
Species Human
Expression Host E. coli
Expression cDNA Clone or AA Sequence
MGSSHHHHHH SSGLVPRGSH MQAPRELAVG IDLGTTYSCV GVFQQGRVEI LANDQGNRTT PSYVAFTDTE RLVGDAAKSQ AALNPHNTVF DAKRLIGRKF ADTTVQSDMK HWPFRVVSEG GKPKVRVCYR GEDKTFYPEE ISSMVLSKMK ETAEAYLGQP VKHAVITVPA YFNDSQRQAT KDAGAIAGLN VLRIINEPTA AAIAYGLDRR GAGERNVLIF DLGGGTFDVS VLSIDAGVFE VKATAGDTHL GGEDFDNRLV NHFMEEFRRK HGKDLSGNKR ALRRLRTACE RAKRTLSSST QATLEIDSLF EGVDFYTSIT RARFEELCSD LFRSTLEPVE KALRDAKLDK AQIHDVVLVG GSTRIPKVQK LLQDFFNGKE LNKSINPDEA VAYGAAVQAA VLMGDKCEKV QDLLLLDVAP LSLGLETAGG VMTTLIQRNA TIPTKQTQTF TTYSDNQPGV FIQVYEGERA MTKDNNLLGR FELSGIPPAP RGVPQIEVTF DIDANGILSV TATDRSTGKA NKITITNDKG RLSKEEVERM VHEAEQYKAE DEAQRDRVAA KNSLEAHVFH VKGSLQEESL RDKIPEEDRR KMQDKCREVL AWLEHNQLAE KEEYEHQKRE LEQICRPIFS RLYGGPGVPG GSSCGTQARQ GDPSTGPIIE EVD
Tag His-tag
Predicted MW 73.2 kDa
Concentration lot specific
Purity >90% by SDS - PAGE
Presentation Purified
Buffer Presentation State: Purified
State: Liquid purified protein
Buffer System: 20 mM Tris-HCl buffer (pH 8.0) containing 100 mM NaCl, 10% glycerol
Preparation Liquid purified protein
Protein Description Recombinant human HSP70B, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography.
Storage Store undiluted at 2-8°C for up to two weeks or (in aliquots) at -20°C or -70°C for longer.
Avoid repeated freezing and thawing.
Stability Shelf life: one year from despatch.
Reference Data
RefSeq NP_002146
Locus ID 3310
UniProt ID P17066, A0A384NKX5, B3KSM6
Cytogenetics 1q23.3
Synonyms HSP70B'
Summary 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 (PubMed:26865365).[UniProtKB/Swiss-Prot Function]
Protein Pathways Antigen processing and presentation, Endocytosis, MAPK signaling pathway, Spliceosome

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