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 United States

KDEL, mAb (10C3)

 
ADI-SPA-827-D 50 µg 165.00 USD
 
ADI-SPA-827-F 200 µg 365.00 USD
 
ADI-SPA-827-J 1 mg 1'405.00 USD
 

Product Specification

Alternative Name:Grp78, Grp94, Lysine-aspartic acid-glutamate-leucine
 
Purity Detail:Protein G affinity purified.
 
Formulation:Liquid. In PBS, pH 7.2, containing 50% glycerol and 0.09% sodium azide.
 
Clone:10C3
 
Isotype:Mouse IgG2a
 
Immunogen:Synthetic peptide corresponding to aa 649-654 (S649EKDEL654) of rat Grp78.
 
Specificity:Recognizes proteins containing the KDEL sequence in mammals, birds and insects, plants, and yeast. Detects a band of ~94kDa by Western blot.
 
Application:EIA
Electron Microscopy
Flow Cytometry
Immunocytochemistry
Immunofluorescence
Immunohistochemistry (paraffin sections)
Immunoprecipitation
Western Blot (1:1000, colorimetric)
Optimal conditions must be determined individually for each application.
 
Long Term Storage:-20°C
 
Miscellaneous/General:The tetrapeptide KDEL, located at the carboxy-terminal sequences of luminal proteins, is a retrieval motif essential for the precise sorting of these proteins along the secretory pathway. KDEL proteins perform essential functions in the endoplasmic reticulum (ER) related to protein folding as well as assembly. The localization of chaperones and other soluble proteins to the ER is achieved by their continuous retrieval from post-ER compartments by the KDEL receptor (Erd2p), which is a membrane protein localized in the Golgi apparatus.
 
SPA-827 IHC
Immunohistochemistry analysis of human spleen tissue stained with KDEL, mAb (10C3) at 10µg/ml.
SPA-827 IF
Immunofluorescence analysis of endoplasmic reticulum staining of mouse C2C12 myoblasts transfected with wild type mouse ADAM12 using KDEL (Grp78, Grp94) mAb (10C3).
SPA-827 WB 01
Western blot analysis: Lane 1: Grp78 (BiP) recombinant protein (Prod No. ADI-SPP-765), Lane 2: RK-13, Lane 3: Mouse liver microsomes, Lane 4: Rat liver microsomes, Lane 5: HeLa Cell Lysate (heat shocked) (Prod No. ADI-LYC-HL101).
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SPA-827 IHC SPA-827 IF SPA-827 WB 01

Product Literature References

Endoplasmic Reticulum Stress Induces Leptin Resistance: K. Ozawa, et al. ; Mol. Pharmacol. 74, 1610 (2008), Application(s): WB using mouse & human cell lysates, Abstract;
Nedd4 Family-interacting Protein 1 (Ndfip1) Is Required for the Exosomal Secretion of Nedd4 Family Proteins: S. Tan, et al. ; J. Biol. Chem. 283, 32621 (2008), Application(s): IF using human tissue culture, Abstract;
Pofut1 is required for the proper localization of the Notch receptor during mouse development: Y. Saga, et al. ; Mech. Dev. 125, 663 (2008), Application(s): IF using mouse tissue, Abstract;
The Hepatitis B Virus Precore Protein Is Retrotransported from Endoplasmic Reticulum (ER) to Cytosol through the ER-associated Degradation Pathway: D. Sitterlin, et al. ; J. Biol. Chem. 283, 32352 (2008), Application(s): IP using human cell lysates, Abstract;
Molecular pathogenesis of seipin/BSCL2-related motor neuron diseases: D. Ito, et al. ; Ann. Neurol. 61, 237 (2007), Application(s): WB, ICC, IF, IHC using human & mouse cell lysates & tissue, Abstract;
Tissue and subcellular distribution of CLIC1: B. Ulmasov, et al.; BMC Cell Biol. 8, 8 (2007), Abstract;
Boca, an endoplasmic reticulum protein required for wingless signaling and trafficking of LDL receptor family members in Drosophila: J. Culi & R.S. Mann; Cell 112, 343 (2003), Abstract;
Overexpression of the 78-kDa glucose-regulated protein/immunoglobulin-binding protein (GRP78/BiP) inhibits tissue factor procoagulant activity: R.C. Austin, et al. ; J. Biol. Chem. 278, 17438 (2003), Application(s): WB using human samples, Abstract;
The amyloid precursor protein protects PC12 cells against endoplasmic reticulum stress-induced apoptosis: H.M. Prehn, et al. ; J. Neurochem. 87, 248 (2003), Application(s): WB using rat samples, Abstract;
A protein sequence that can encode native structure by disfavoring alternate conformations: W.C. Wigley, et al.; Nat. Struct. Biol. 9, 381 (2002), Abstract;
Decreased protein expression and intermittent recoveries in BiP levels result from cellular stress during heterologous protein expression in Saccharomyces cerevisiae: A.S. Robinson, et al. ; Biotechnol. Prog. 18, 942 (2002), Application(s): WB using yeast samples, Abstract;
Decreased protein expression and intermittent recoveries in BiP levels result from cellular stress during heterologous protein expression in Saccharomyces cerevisiae: K.J. Kauffman, et al.; Biotechnol. Prog. 18, 942 (2002), Abstract;
Developmental regulation of neuronal K(Ca) channels by TGFbeta1: an essential role for PI3 kinase signaling and membrane insertion: S.E. Dryer, et al. ; J. Neurophysiol. 88, 954 (2002), Application(s): ICC using chicken samples, Abstract;
Efficacy of plant-produced recombinant antibodies against HCG: R. Finnern, et al. ; Hum. Reprod. 17, 2054 (2002), Application(s): WB, EIA using plant (tobacco) samples, Abstract;
Efficacy of plant-produced recombinant antibodies against HCG: S. Kathuria, et al.; Hum. Reprod. 17, 2054 (2002), Abstract;
ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum: N. Shastri, et al. ; Nature 419, 480 (2002), Application(s): WB, ICC using monkey samples, Abstract;
ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum: T. Serwold, et al.; Nature 419, 480 (2002), Abstract;
Mass transport of proform of a KDEL-tailed cysteine proteinase (SH-EP) to protein storage vacuoles by endoplasmic reticulum-derived vesicle is involved in protein mobilization in germinating seeds: K. Toyooka, et al.; J. Cell Biol. 148, 453 (2000), Abstract;
Identification of amino acids in the binding pocket of the human KDEL receptor: A.A. Scheel & H.R. Pelham; J. Biol. Chem. 273, 2467 (1998), Abstract;
Involvement of endoplasmic reticulum chaperones in the folding of hepatitis C virus glycoproteins: A. Choukhi, et al.; J. Virol. 72, 3851 (1998), Abstract;
Mutants of the yeast Yarrowia lipolytica defective in protein exit from the endoplasmic reticulum are also defective in peroxisome biogenesis: V.I. Titorenko & R.A. Rachubinski; Mol. Cell Biol. 18, 2789 (1998), Abstract;
Identification by anti-idiotype antibodies of an intracellular membrane protein that recognizes a mammalian endoplasmic reticulum retention signal: D. Vaux, et al.; Nature 345, 495 (1990), Abstract;
The retention signal for soluble proteins of the endoplasmic reticulum: H.R. Pelham; Trends Biochem. Sci. 15, 483 (1990), Abstract;
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