Loricrin C-terminal Antibody [D17A11]

Application: Reactivity: Rat, Human

Usage Information

Dilution
IHC1:250 IF1:250

Application
IHC, IF

Reactivity
Rat, Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Positive Control	Human uterus tissue; Human skin tissue; Rat skin tissue; A431 cell
Negative Control

Datasheet & SDS

Biological Description

Specificity
Loricrin C-terminal Antibody [D17A11] detects endogenous levels of C-terminal region of total Loricrin protein.

Clone
D17A11

Synonym(s)
LOR; LRN; LORICRIN; Loricrin

Background
The Loricrin C-terminal domain constitutes the glutamine- and lysine-rich anchoring region of this predominant cornified envelope (CE) protein (accounting for over 70% of epidermal mass), featuring glycine-serine loops with multiple Q/K pairs—such as Gln451/Lys454 clusters—that act as primary transglutaminase 1/3 (TGM1/3) substrates for ε-(γ-glutamyl)lysine isopeptide bond formation, further reinforced by cysteine disulfide bridges conferring insolubility. During keratinocyte terminal differentiation, Ca²⁺-activated TGM1 mediates sequential intra- and extracellular cross-linking, where C-terminal glutamine residues are deamidated to glutamates to prime lysine ε-amino groups for nucleophilic attack, rigidly tethering loricrin to the involucrin/small proline-rich protein (SPR) scaffold in L-granules and subsequently to the plasma membrane, resulting in a 10–20 nm thick, mechanically resilient shell that is impermeable to water and pathogens, with flexible glycine loops absorbing tensile stress (modulus ~100 MPa). This post-translational insolubilization via TGM-catalyzed lattice polymerization mechanistically establishes epidermal barrier competence, transcriptionally driven by NFAT, AP1, and NRF2-mediated upregulation of LOR. Dominant frameshift mutations truncating the C-terminus produce arginine-rich nuclear localization signal (NLS) peptides that mislocalize to the nucleus and impair cross-linking, dominantly disrupting terminal differentiation and resulting in loricrin keratoderma (LK/Vohwinkel syndrome), characterized by palmoplantar hyperkeratosis, ichthyosis, and barrier fragility from incompetent cornified envelopes.

Background

The Loricrin C-terminal domain constitutes the glutamine- and lysine-rich anchoring region of this predominant cornified envelope (CE) protein (accounting for over 70% of epidermal mass), featuring glycine-serine loops with multiple Q/K pairs—such as Gln451/Lys454 clusters—that act as primary transglutaminase 1/3 (TGM1/3) substrates for ε-(γ-glutamyl)lysine isopeptide bond formation, further reinforced by cysteine disulfide bridges conferring insolubility. During keratinocyte terminal differentiation, Ca²⁺-activated TGM1 mediates sequential intra- and extracellular cross-linking, where C-terminal glutamine residues are deamidated to glutamates to prime lysine ε-amino groups for nucleophilic attack, rigidly tethering loricrin to the involucrin/small proline-rich protein (SPR) scaffold in L-granules and subsequently to the plasma membrane, resulting in a 10–20 nm thick, mechanically resilient shell that is impermeable to water and pathogens, with flexible glycine loops absorbing tensile stress (modulus ~100 MPa). This post-translational insolubilization via TGM-catalyzed lattice polymerization mechanistically establishes epidermal barrier competence, transcriptionally driven by NFAT, AP1, and NRF2-mediated upregulation of LOR. Dominant frameshift mutations truncating the C-terminus produce arginine-rich nuclear localization signal (NLS) peptides that mislocalize to the nucleus and impair cross-linking, dominantly disrupting terminal differentiation and resulting in loricrin keratoderma (LK/Vohwinkel syndrome), characterized by palmoplantar hyperkeratosis, ichthyosis, and barrier fragility from incompetent cornified envelopes.

References
https://pubmed.ncbi.nlm.nih.gov/35625601/ https://pubmed.ncbi.nlm.nih.gov/8673107/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%