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MABS1812M

Anti-Furin Antibody, clone 16B1.1

clone 16B1.1, from mouse

Synonym(s):

Anti-FUR, Anti-PACE, Anti-PCSK3, Anti-SPC1

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Conjugate:
unconjugated
Clone:
16B1.1, monoclonal
Application:
western blot
Species reactivity:
human
Citations:
Technique(s):
western blot: suitable
Uniprot accession no.:
P09958

Key Documents

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Product Name

Anti-Furin Antibody, clone 16B1.1, clone 16B1.1, from mouse

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

16B1.1, monoclonal

species reactivity

human

packaging

antibody small pack of 25 μg

technique(s)

western blot: suitable

isotype

IgG2bκ

NCBI accession no.

NP_001276752

UniProt accession no.

P09958

target post-translational modification

unmodified

Quality Level

100

Gene Information

human ... FURIN(5045)

Analysis Note

Evaluated by Western Blotting in U-251 cell lysate.

Western Blotting Analysis: 0.5 µg/mL of this antibody detected Furin in 10 µg of U-251 cell lysate.

Application

Anti-Furin, clone 16B1.1, Cat. No. MABS1812, is a mouse monoclonal antibody that detects Furin in human cells and has been tested for use in Western Blotting.

Biochem/physiol Actions

Clone 16B1.1 detects human Furin and it targets an epitope within 177 amino acids from the C-terminal half.

General description

Furin (UniProt: P09958; also known as EC: 3.4.2.75, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme, PACE) is encoded by the FURIN (also known as FUR, PACE, PCSK3) gene (Gene ID: 5045) in human. Furin is an ubiquitously expressed enzyme with endoprotease activity within constitutive secretory pathways and is capable of cleavage at the RX(K/R)R consensus motif. It is single-pass type I membrane protein that shuttles between the trans-Golgi network and the cell surface. It is synthesized with a signal peptide of 26 amino acids and a propeptide region (aa 27-107) that inhibits its activity. The inhibition peptide plays the role of an intramolecular chaperone. It is autocatalytically removed in the endoplasmic reticulum (ER) and remains non-covalently bound to furin as a potent autoinhibitor. Propeptide cleavage is a prerequisite for exit of Furin molecules out of the endoplasmic reticulum. A second cleavage within the propeptide region occurs in the trans-Golgi network, followed by the release of the propeptide and the activation of Furin. Mature Furin has a luminal region (aa 108-705), a helical domain (aa 716-738), and a cytoplasmic region (aa 739-794). The cytoplasmic domain responsible for its trans-Golgi network localization and recycling from the cell surface.
~100 kDa observed; 86.68 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

Immunogen

GST/His-tagged recombinant fragment corresponding to 177 amino acids from the C-terminal half of human Furin.

Other Notes

Concentration: Please refer to lot specific datasheet.

Physical form

Format: Purified

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Storage Class

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

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