Heat Shock 70kDa Protein 5 (Glucose-Regulated Protein, 78kDa) (HSPA5) (full length) Protéine

Détails pour le produit réf. ABIN1686700
Nom de la protéine
  • GRP78
  • BiP
  • GRP-78
  • grp78
  • hspa5a
  • BIP
  • MIF2
  • AL022860
  • AU019543
  • Bip
  • D2Wsu141e
  • D2Wsu17e
  • Grp78
  • Hsce70
  • SEZ-7
  • Sez7
  • baffled
  • mBiP
  • cb865
  • fb60h09
  • fi36d04
  • wu:fb60h09
  • wu:fi36d04
  • zgc:55994
  • zgc:77606
  • 78 kDa glucose-regulated protein
  • heat shock protein family A (Hsp70) member 5
  • BiP/GRP78
  • glucose-regulated protein 78
  • putative glucose-regulated protein 78
  • Hsp70 family ATPase KAR2
  • heat shock protein family A (Hsp70) member 5 S homeolog
  • heat shock 70 kDa protein 5a
  • heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa)
  • heat shock protein 5
  • heat shock protein family A member 5
  • CpipJ_CPIJ003550
  • HSPA5
  • grp78
  • LOC100533358
  • BiP/grp78
  • Tc00.1047053506585.40
  • Tb11.02.5450
  • Tb11.02.5500
  • LMJF_28_1200
  • KAR2
  • LOC100135840
  • hspa5.S
  • hspa5
  • Hspa5
Attributs du protein
full length
4
2
1
1
1
1
1
1
Origine
Humain
15
3
2
1
Source
Escherichia coli (E. coli)
14
2
2
1
1
Type de proteíne
Recombinant
Application
Activity Assay (AcA), ELISA, Functional Studies (Func), SDS-PAGE (SDS), Western Blotting (WB)
Options
Séquence MKLSLVAAML LLLSAARAEE EDKKEDVGTV VGIDLGTTYS CVGVFKNGRV EIIANDQGNR ITPSYVAFTP EGERLIGDAA KNQLTSNPEN TVFDAKRLIG RTWNDPSVQQ DIKFLPFKVV EKKTKPYIQV DIGGGQTKTF APEEISAMVL TKMKETAEAY LGKKVTHAVV TVPAYFNDAQ RQATKDAGTI AGLNVMRIIN EPTAAAIAYG LDKREGEKNI LVFDLGGGTF DVSLLTIDNG VFEVVATNGD THLGGEDFDQ RVMEHFIKLY KKKTGKDVRK DNRAVQKLRR EVEKAKRALS SQHQARIEIE SFYEGEDFSE TLTRAKFEEL NMDLFRSTMK PVQKVLEDSD LKKSDIDEIV LVGGSTRIPK IQQLVKEFFN GKEPSRGINP DEAVAYGAAV QAGVLSGDQD TGDLVLLDVC PLTLGIETVG GVMTKLIPRN TVVPTKKSQI FSTASDNQPT VTIKVYEGER PLTKDNHLLG TFDLTGIPPA PRGVPQIEVT FEIDVNGILR VTAEDKGTGN KNKITITNDQ NRLTPEEIER MVNDAEKFAE EDKKLKERID TRNELESYAY SLKNQIGDKE KLGGKLSSED KETMEKAVEE KIEWLESHQD ADIEDFKAKK KELEEIVQPI ISKLYGSAGP PPTGEEDTAE KDEL
Specificité ~78 kDa
Purification Affinity Purified
Pureté >90%
Nom de la protéine
Sujet GRP78 is a ubiquitously expressed, 78- kDa glucose-regulated protein, and is commonly referred to as an immunoglobin chain binding protein (BiP). The BiP proteins are categorized as stress response proteins because they play an important role in the proper folding and assembly of nascent protein and in the scavenging of misfolded proteins in the endoplasmic reticulum lumen. Translation of BiP is directed by an internal ribosomal entry site (IRES) in the 5' non-translated region of the BiP mRNA. BiP IRES activity increases when cells are heat stressed (1). GRP78 is also critical for maintenance of cell homeostasis and the prevention of apoptosis (2). Luo et al. have provided findings that suggest GRP78 is essential for embryonic cell growth and pluripotent cell survival (3). In terms of diseases, GRP78 has been shown to be a reliable biomarker of hypoglycemia (Barnes), to serve a neuroprotective function in neurons exposed to glutamate and oxidative stress (4), and its protein levels are reduced in the brains of Alzheimer's patients (5). Also, the induction of the GRP78 protein that results in severe glucose and oxygen deprivation could possible lead to drug resistance to anti-tumor drugs (6, 7).
Poids moléculaire approx. 78 kDa
ID gène 3309
NCBI Accession NM_005347
UniProt P11021
Pathways Thyroid Hormone Synthesis, ER-Nucleus Signaling
Commentaires

This product has been certified >90% pure using SDS-PAGE analysis and gamma globulin as the protein concentration standard.

Restrictions For Research Use only
Concentration Lot specific
Buffer 20 mM Tris/HCl pH 7.5, 0.45M NaCl, 10 % glycerol, 0.5 mM DTT
Stock -20 °C
Produit citée dans: Kosakowska-Cholody, Lin, Srideshikan, Scheffer, Tarasova, Acharya: "HKH40A downregulates GRP78/BiP expression in cancer cells." dans: Cell death & disease, Vol. 5, pp. e1240, 2014 (PubMed).

Bruchmann, Roller, Walther, Schäfer, Lehmusvaara, Visakorpi, Klocker, Cato, Maddalo: "Bcl-2 associated athanogene 5 (Bag5) is overexpressed in prostate cancer and inhibits ER-stress induced apoptosis." dans: BMC cancer, Vol. 13, pp. 96, 2013 (PubMed).

Ding, Li, Wu, Yang, Luo, Xie, Druey, Zajac, Hsu, Mountz: "IL-17RA is essential for optimal localization of follicular Th cells in the germinal center light zone to promote autoantibody-producing B cells." dans: Journal of immunology (Baltimore, Md. : 1950), Vol. 191, Issue 4, pp. 1614-24, 2013 (PubMed).

Maddalo, Neeb, Jehle, Schmitz, Muhle-Goll, Shatkina, Walther, Bruchmann, Gopal, Wenzel, Ulrich, Cato: "A peptidic unconjugated GRP78/BiP ligand modulates the unfolded protein response and induces prostate cancer cell death." dans: PLoS ONE, Vol. 7, Issue 10, pp. e45690, 2012 (PubMed).

Background publications Dong, Ko, Baumeister, Swenson, Costa, Markland, Stiles, Patterson, Bates, Lee: "Vascular targeting and antiangiogenesis agents induce drug resistance effector GRP78 within the tumor microenvironment." dans: Cancer research, Vol. 65, Issue 13, pp. 5785-91, 2005 (PubMed).

Koomägi, Mattern, Volm: "Glucose-related protein (GRP78) and its relationship to the drug-resistance proteins P170, GST-pi, LRP56 and angiogenesis in non-small cell lung carcinomas." dans: Anticancer research, Vol. 19, Issue 5B, pp. 4333-6, 2000 (PubMed).

Mattern, Koomägi, Volm: "Biological characterization of subgroups of squamous cell lung carcinomas." dans: Clinical cancer research : an official journal of the American Association for Cancer Research, Vol. 5, Issue 6, pp. 1459-63, 1999 (PubMed).

Yang, Turner, Gaut: "The chaperone BiP/GRP78 binds to amyloid precursor protein and decreases Abeta40 and Abeta42 secretion." dans: The Journal of biological chemistry, Vol. 273, Issue 40, pp. 25552-5, 1998 (PubMed).

Laquerre, Anderson, Argnani, Glorioso: "Herpes simplex virus type 1 glycoprotein B requires a cysteine residue at position 633 for folding, processing, and incorporation into mature infectious virus particles." dans: Journal of virology, Vol. 72, Issue 6, pp. 4940-9, 1998 (PubMed).

Rechthand, Smith, Latker, Rapoport: "Altered blood-nerve barrier permeability to small molecules in experimental diabetes mellitus." dans: Journal of neuropathology and experimental neurology, Vol. 46, Issue 3, pp. 302-14, 1987 (PubMed).

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