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GRP78 Antikörper (AA 525-628)

HSPA5 Reaktivität: Human, Ratte, Maus, Hund WB, IF Wirt: Maus Monoclonal 40-BiP unconjugated
Produktnummer ABIN968290
  • Target Alle GRP78 (HSPA5) Antikörper anzeigen
    GRP78 (HSPA5) (Heat Shock 70kDa Protein 5 (Glucose-Regulated Protein, 78kDa) (HSPA5))
    Bindungsspezifität
    • 26
    • 16
    • 13
    • 8
    • 7
    • 6
    • 6
    • 6
    • 5
    • 5
    • 4
    • 4
    • 3
    • 3
    • 2
    • 2
    • 2
    • 2
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    AA 525-628
    Reaktivität
    • 186
    • 124
    • 107
    • 39
    • 38
    • 36
    • 34
    • 32
    • 31
    • 20
    • 16
    • 6
    • 5
    • 4
    • 4
    • 3
    • 3
    • 3
    • 2
    • 2
    • 2
    • 2
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    Human, Ratte, Maus, Hund
    Wirt
    • 131
    • 90
    • 9
    • 3
    • 1
    • 1
    Maus
    Klonalität
    • 134
    • 102
    Monoklonal
    Konjugat
    • 101
    • 21
    • 17
    • 14
    • 13
    • 12
    • 9
    • 8
    • 8
    • 8
    • 3
    • 2
    • 2
    • 2
    • 2
    • 2
    • 2
    • 2
    • 2
    • 2
    • 2
    • 2
    Dieser GRP78 Antikörper ist unkonjugiert
    Applikation
    • 221
    • 104
    • 88
    • 85
    • 76
    • 34
    • 31
    • 28
    • 26
    • 21
    • 13
    • 7
    • 6
    • 3
    • 3
    • 2
    • 1
    Western Blotting (WB), Immunofluorescence (IF)
    Kreuzreaktivität
    Hund, Ratte (Rattus), Maus
    Produktmerkmale
    1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
    2. Please refer to us for technical protocols.
    3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
    4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
    Aufreinigung
    The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.
    Immunogen
    Human BiP/GRP78 aa. 525-628
    Klon
    40-BiP
    Isotyp
    IgG2a
    Top Product
    Discover our top product HSPA5 Primärantikörper
  • Kommentare

    Related Products: ABIN968587, ABIN967389

    Beschränkungen
    Nur für Forschungszwecke einsetzbar
  • Format
    Liquid
    Konzentration
    250 μg/mL
    Buffer
    Aqueous buffered solution containing BSA, glycerol, and ≤0.09 % sodium azide.
    Konservierungsmittel
    Sodium azide
    Vorsichtsmaßnahmen
    This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
    Lagerung
    -20 °C
    Informationen zur Lagerung
    Store undiluted at -20°C.
  • Han, Kim, Lee, Lee, Lee, Ohba, Kuroki, Suh, Ryu: "Localization of phospholipase D1 to caveolin-enriched membrane via palmitoylation: implications for epidermal growth factor signaling." in: Molecular biology of the cell, Vol. 13, Issue 11, pp. 3976-88, (2002) (PubMed).

    Waelter, Boeddrich, Lurz, Scherzinger, Lueder, Lehrach, Wanker: "Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation." in: Molecular biology of the cell, Vol. 12, Issue 5, pp. 1393-407, (2001) (PubMed).

    Yamazaki, Chang, Haass, Ihara: "Accumulation and aggregation of amyloid beta-protein in late endosomes of Niemann-pick type C cells." in: The Journal of biological chemistry, Vol. 276, Issue 6, pp. 4454-60, (2001) (PubMed).

    Ting, Lee: "Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation." in: DNA (Mary Ann Liebert, Inc.), Vol. 7, Issue 4, pp. 275-86, (1988) (PubMed).

  • Target
    GRP78 (HSPA5) (Heat Shock 70kDa Protein 5 (Glucose-Regulated Protein, 78kDa) (HSPA5))
    Andere Bezeichnung
    BiP (HSPA5 Produkte)
    Synonyme
    GRP78 antikoerper, BiP antikoerper, GRP-78 antikoerper, grp78 antikoerper, hspa5a antikoerper, BIP antikoerper, MIF2 antikoerper, AL022860 antikoerper, AU019543 antikoerper, Bip antikoerper, D2Wsu141e antikoerper, D2Wsu17e antikoerper, Grp78 antikoerper, Hsce70 antikoerper, SEZ-7 antikoerper, Sez7 antikoerper, baffled antikoerper, mBiP antikoerper, cb865 antikoerper, fb60h09 antikoerper, fi36d04 antikoerper, wu:fb60h09 antikoerper, wu:fi36d04 antikoerper, zgc:55994 antikoerper, zgc:77606 antikoerper, 78 kDa glucose-regulated protein antikoerper, heat shock protein family A (Hsp70) member 5 antikoerper, BiP/GRP78 antikoerper, glucose-regulated protein 78 antikoerper, putative glucose-regulated protein 78 antikoerper, Hsp70 family ATPase KAR2 antikoerper, heat shock protein family A (Hsp70) member 5 S homeolog antikoerper, heat shock 70 kDa protein 5a antikoerper, heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa) antikoerper, heat shock protein 5 antikoerper, heat shock protein family A member 5 antikoerper, CpipJ_CPIJ003550 antikoerper, HSPA5 antikoerper, grp78 antikoerper, LOC100533358 antikoerper, BiP/grp78 antikoerper, Tc00.1047053506585.40 antikoerper, Tb11.02.5450 antikoerper, Tb11.02.5500 antikoerper, LMJF_28_1200 antikoerper, KAR2 antikoerper, LOC100135840 antikoerper, hspa5.S antikoerper, hspa5 antikoerper, Hspa5 antikoerper
    Hintergrund
    Synthesis of nascent proteins occurs at sites on the endoplasmic reticulum (ER) called translocons. Translocon proteins form a pore in the membrane that allow passage of the newly synthesized protein from the ribosome into the ER lumen. As the nascent protein enters the lumen, it is bound by BiP (binding protein), the major chaperone of the ER. This protein is identical to the 78kDa glucose regulated protein, GRP78. BiP binds short hydrophobic sequences of the emerging peptide and prevents denaturation or nonspecific aggregation. Hydrolysis of ATP by BiP results in the release of the nascent protein which quickly assumes its proper conformation. However, if folding is incorrect, BiP again binds the protein and prevents its exit from the ER. In addition, BiP binding is thought to enhance the movement of secretory polypeptides across the ER membrane, but it is not required for protein translocation. It is 60% identical to Hsp70 and is similarly increased by conditions that produce incorrectly folded proteins. Thus, BiP is a chaperone of the ER lumen that binds misfolded or unassembled secretory proteins and ensures proper movement of proteins from the ER to the Golgi apparatus.
    Molekulargewicht
    78 kDa
    Pathways
    Thyroid Hormone Synthesis, ER-Nucleus Signaling
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