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==Hibernation induction trigger (HIT) protein and recombinant protein technology== Hibernation induction trigger (HIT) proteins isolated from mammals have been used in the study of organ recovery rates. One study in 1997 found that ''delta 2'' opioid and hibernation induction trigger (HIT) proteins were not able to increase the recovery rate of heart tissue during ischemia. While unable to increase recovery rates at the time of ischemia, the protein precursors were identified to play a role in the preservation of veterinary organ function.<ref>{{cite journal |last=Bolling |first=S.F. |author2=Tramontini, N.L., Kilgore, K.S., Su, T-P., Oeltgen, P.R., Harlow, H.H. |year=1997 |title=Use of "Natural" Hibernation Induction Triggers for Myocardial Protection |url=http://www.annalsthoracicsurgery.org/article/S0003-4975(97)00631-0/fulltext |journal=The Annals of Thoracic Surgery |volume=64 |issue=3 |pages=623β627 |doi=10.1016/s0003-4975(97)00631-0 |pmid=9307448}}</ref> Recent advances in recombinant protein technology make it possible for scientists to manufacture hibernation induction trigger (HIT) proteins in the laboratory without the need for animal euthanasia. Bioengineering of proteins can aid in the protection of vulnerable populations of bears and other mammals that produce valuable proteins. Protein sequencing of HIT proteins, such as Ξ± 1-glycoprotein-like 88 kDa hibernation-related protein HRP, contributes to this research pool.<ref>{{Cite journal |last1=Horton |first1=Noel D |last2=Kaftani |first2=Dimitra J |last3=Bruce |first3=David S |last4=Bailey |first4=Evans C |last5=Krober |first5=Alan S |last6=Jones |first6=Jeffrey R |last7=Turker |first7=Mitchell |last8=Khattar |first8=Nada |last9=Su |first9=Tsung-Ping |last10=Bolling |first10=Steven F |last11=Oeltgen |first11=Peter R |date=1998 |title=Isolation and partial characterization of an opioid-like 88 kDa hibernation-related protein |url=https://linkinghub.elsevier.com/retrieve/pii/S030504919800056X |journal=Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology |language=en |volume=119 |issue=4 |pages=787β805 |doi=10.1016/S0305-0491(98)00056-X|pmid=9787770 }}</ref> A study in 2014 uses recombinant technology to construct, express, purify, and isolate animal proteins (HP-20, HP-25, and HP-27) outside of the animal to study key hibernation proteins (HP).<ref>{{Cite journal |last1=Seldin |first1=Marcus |last2=Byerly |first2=Mardi |last3=Petersen |first3=Pia |last4=Swason |first4=Roy |last5=Balkema-Buschmann |first5=Anne |last6=Groschup |first6=Martin |last7=Wong |first7=G. William |date=2014 |title=Seasonal oscillation of liver-derived hibernation protein complex in the central nervous system of non-hibernating mammals |url=https://doi.org/10.1242/jeb.095976 |journal=Journal of Experimental Biology |volume=217 |issue=15 |pages=2667β2679|doi=10.1242/jeb.095976 |pmid=25079892 |pmc=4117459 |bibcode=2014JExpB.217.2667S }}</ref>
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