Human NGL-1/LRRC4C Antibody

Catalog #: MAB4899 Datasheet / COA / SDS

Catalog #	Availability	Size / Price	Qty
MAB4899
MAB4899-SP

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Summary Data Examples Preparation and Storage Reconstitution Calculator Background Product Datasheets Related Research Areas

Human NGL-1/LRRC4C Antibody Summary

Species Reactivity

Human

Specificity

Detects human NGL-1/LRRC4C in direct ELISAs. In direct ELISAs, no cross-reactivity with recombinant human (rh) LRRC4 or rhNGL‑3/LRRC4B is observed.

Source

Monoclonal Mouse IgG₁ Clone # 755720

Purification

Protein A or G purified from hybridoma culture supernatant

Immunogen

Mouse myeloma cell line NS0-derived recombinant human NGL-1/LRRC4C
Gln45-Lys527 (predicted)
Accession # Q9HCJ2

Formulation

Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.

Applications

Recommended Concentration

Sample

Immunohistochemistry

8-25 µg/mL

See below

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Scientific Data

Immunohistochemistry

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NGL‑1/LRRC4C in Human Spinal Cord. NGL-1/LRRC4C was detected in immersion fixed paraffin-embedded sections of human spinal cord using Mouse Anti-Human NGL-1/LRRC4C Monoclonal Antibody (Catalog # MAB4899) at 15 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Mouse HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS002) and counter-stained with hematoxylin (blue). Specific staining was localized to the dorsal horn. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.

Reconstitution Calculator

Preparation and Storage

Reconstitution

Sterile PBS to a final concentration of 0.5 mg/mL.

Shipping

The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C

Stability & Storage

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.

12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: NGL-1/LRRC4C

Human NGL-1 (Netrin-G1 ligand; gene name LRRC4C) is a 67 kDa (predicted for mature protein), type I transmembrane cell adhesion molecule that is a member of the NGL family of proteins (1, 2). It is synthesized from a precursor that is 640 amino acids (aa) in length that contains a 44 aa signal sequence, a 483 aa extracellular region, a 21 aa transmembrane region, and a short cytoplasmic tail of 92 aa. The extracellular region of NGL-1 consists of nine leucine-rich repeats (LRRs) that are flanked by LRR N-terminal and LRR C-terminal domains, and followed by an Ig-like C2‑type domain (1, 2). The cytoplasmic region contains a C‑terminal Glu-Thr-Gln-Ile sequence that corresponds to a potential PDZ (postsynaptic density-95/discs large/zona occludens-1) domain-binding motif (1, 2). Human NGL-1 shares 99.7% aa sequence identity with mouse NGL-1. Mouse NGL-1 is highly expressed in the developing cerebral cortex and the striatum at embryonic day 14 (1). Postnatally, NGL-1 is expressed exclusively in the brain, with the highest expression found in the cerebral cortex as a whole, and in individual neocortical areas such as the frontal, parietal and occipital lobes (1). Moderate expression of NGL-1 occurs in the putamen, amygdala, hippocampus and medulla oblongata (1). Weak expression is found in the caudate nucleus and thalamus (1). Functionally, membrane-bound cell-surface NGL-1 binds to netrin-G1 specifically through its LRR region, and in the developing brain, may promote neurite outgrowth of thalamocortical axons (1‑4).

References

Lin, J.C. et al. (2003) Nat. Neurosci. 6:1270.
Kim, S. et al. (2006) Nat. Neurosci. 9:1294.
Chen, Y. et al. (2006) Brain Res. Rev. 51:265.
Nishimura-Akiyoshi, S. et al. (2007) Proc. Natl. Acad. Sci. U.S.A. 104:14801.