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HDEL antibody (C-Term) (PerCP)

This Mouse Monoclonal antibody specifically detects HDEL in WB, IF and ICC. It exhibits reactivity toward Saccharomyces cerevisiae.
Catalog No. ABIN2484717

Quick Overview for HDEL antibody (C-Term) (PerCP) (ABIN2484717)

Target

HDEL

Reactivity

  • 21
  • 12
  • 11
  • 10
  • 10
  • 10
  • 10
  • 10
  • 1
Saccharomyces cerevisiae

Host

  • 21
Mouse

Clonality

  • 21
Monoclonal

Conjugate

  • 4
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
  • 1
This HDEL antibody is conjugated to PerCP

Application

  • 21
  • 11
  • 10
  • 9
  • 1
Western Blotting (WB), Immunofluorescence (IF), Immunocytochemistry (ICC)

Clone

2E7
  • Binding Specificity

    C-Term

    Specificity

    Detects ~78 kDa.

    Cross-Reactivity

    Drosophila melanogaster, Plant, Saccharomyces cerevisiae

    Purification

    Protein G Purified

    Immunogen

    Raised against a synthetic HDEL peptide corresponding to the C-terminus of yeast Bip

    Isotype

    IgG2b
  • Application Notes

    • WB (1:1000)
    • ICC/IF (1:100)
    • optimal dilutions for assays should be determined by the user.

    Comment

    1 μg/ml of ABIN2484717 was sufficient for detection of HDEL-containing proteins in 10 μg of S. cerevisiae lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

    Restrictions

    For Research Use only
  • Format

    Liquid

    Concentration

    1 mg/mL

    Buffer

    PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide, Storage buffer may change when conjugated

    Preservative

    Sodium azide

    Precaution of Use

    This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

    Storage

    4 °C

    Storage Comment

    Conjugated antibodies should be stored at 4°C
  • Target

    HDEL

    Alternative Name

    HDEL

    Background

    HSP 70 family comprises four highly conserved proteins, HSP 70, HSC 70, GRP 75 and GRP 78, which serve a variety of roles. They act as molecular chaperones, facilitating the assembly of multi-protein complexes, participate in the translocation of polypeptides across cell membranes and to the nucleus, and aid in the proper folding of nascent polypeptide chains (1, 2). GRP 78 is localized in the endoplasmic reticulum (ER), where it receives imported secretory proteins and is involved in the folding and translocation of nascent peptide chains (2). Sorting of these proteins is dependent on a C-terminal tetrapeptide signal, usually KDEL in animal cells, and HDEL in S.cerevisiae (3). The 2E7 clone recognizes the C-terminal peptide HDEL, a common version of the endoplasmic reticulum retention signal found in yeast, plant, nematode and other ER proteins. 2E7 specifically stains HDEL proteins in barnyard grass, beet, cotton, mung bean, sorghum and wheat (4).
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