HSPA5 Monoclonal Antibody (2G11)

Product Specific Information

Immunogen sequence: EEEDKKEDVG TVVGIDLGTT YSCVGVFKNG RVEIIANDQG NRITPSYVAF TPEGERLIGD AAKNQLTSNP ENTVFDAKRL IGRTWNDPSV QQDIKFLPFK VVEKKTKPYI QVDIGGGQTK TFAPEEISAM VLTKMKETAE AYLGKKVTHA VVTVPAYFND AQRQATKDAG TIAGLNVMRI INEPTAAAIA YGLDKREGEK NILVFDLGGG TFDVSLLTID NGVFEVVATN GDTHLGGEDF DQRVMEHFIK LYKKKTGKDV RKDNRAVQKL RREVEKAKRA LSSQHQARIE IESFYEGEDF SETLTRAKFE ELNMDLFRST MKPVQKVLED SDLKKSDIDE IVLVGGSTRI PKIQQLVKEF FNGKEPSRGI NPDEAVAYGA AVQAGVLSGD QDTGDLVLLD VCPLTLGIET VGGVMTKLIP RNTVVPTKKS QIFSTASDNQ PTVTIKVYEG ERPLTKDNHL LGTFDLTGIP PAPRGVPQIE VTFEIDVNGI LRVTAEDKGT GNKNKITITN DQNRLTPEEI ERMVNDAEKF AEEDKKLKER IDTRNELESY AYSLKNQIGD KEKLGGKLSS EDKETMEKAV EEKIEWLESH QDADIEDFKA KKKELEEIVQ PIISKLYGSA GPPPTGEEDT AEKDEL

Target Information

GRP78 is a 78 kDa glucose regulated protein that belongs to the family of heat shock proteins that include HSP70. GRP78 is a resident protein of the endoplasmic reticulum (ER) and associates transiently with a variety of newly synthesized secretory and membrane proteins. GRP78 may also interact with mutant and misfolded proteins, marking them for degradation. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the C-terminus of GRP78 and other resident ER proteins including glucose regulated protein 94 (GRP94) and protein disulfide isomerase (PDI). The KDEL signal is recognized by the KDEL receptor and this interaction ensures recycling of escaped ER proteins back to the ER. GRP78's involvement in correct folding of proteins and degradation of misfolded proteins is via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate. GRP78 is critical for maintenance of cell homeostasis and the prevention of apoptosis. GRP78 protein levels have been shown to be a reliable biomarker of hypoglycemia and serves a neuroprotective function in neurons exposed to glutamate and oxidative stress. GRP78 levels are reduced in the brains of Alzheimer's Disease patients, and decreased expression of GRP78 is found associated with missense mutations in the human presenilin-1 (PS1) gene. Further, the induction of the GRP78 protein has been associated with the development of drug-resistance to antitumor drugs.