P4HB Protein, Human (His)

The P4HB protein is a multifunctional entity that catalyzes disulfide bonding processes at the cell surface and within cells. As a reductase, it modifies outer surface proteins and participates in the formation of disulfide bonds in nascent proteins. P4HB Protein, Human (His) is the recombinant human-derived P4HB protein, expressed by E. coli , with N-6*His labeled tag. The total length of P4HB Protein, Human (His) is 490 a.a., with molecular weight of ~56 kDa.

The P4HB protein, a multifunctional entity, catalyzes the intricate processes of forming, breaking, and rearranging disulfide bonds. Positioned at the cell surface, it acts as a reductase, cleaving disulfide bonds of proteins linked to the cell and potentially causing structural modifications of exofacial proteins. Intracellularly, P4HB is involved in forming and rearranging disulfide bonds of nascent proteins. At elevated concentrations, and under the phosphorylation influence of FAM20C, it functions as a chaperone, preventing the aggregation of misfolded proteins. Conversely, at lower concentrations, it exhibits anti-chaperone activity by facilitating aggregation. P4HB's versatility extends to its participation as a structural subunit in various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Furthermore, it serves as a receptor for LGALS9, with this interaction influencing disulfide reductase activity at the cell surface of Th2 T helper cells, altering the plasma membrane's redox state, and enhancing cell migration. This diverse range of functions underscores the pivotal role of P4HB in cellular processes, including protein folding, redox regulation, and cell migration.

1.Thiol Protein Reductase Activity is 0.001 /650nm/ min^-2, determined by measuring the turbidityincrease at 650 nm due to insulin reduction.The activity is expressed as the ratio of the slope of a linear part of the turbidity curve to the lag tim.
2. Measured by its ability to promote aggregation of insulin in the presence of DTT. The specific activity is 9.375 A650/cm/min/mg.

Human

E. coli

N-6*His

P07237 (A19-L508)

5034  [NCBI]

APEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESEELTAERITEFCHRFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEDVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDMEEDDDQKAVKDEL

Approximately 56 kDa

• 
  Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.2 μm solution of 50 mM Tris-HCL, 300 mM NaCl, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US;may vary elsewhere.