Loading...All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.
Immunoglobulin superfamily containing leucine rich repeat 2 (ISLR2) is a single pass transmembrane cell surface protein encoded by ISLR2 gene. This protein localizes to plasma membrane of multiple cell populations. ISLR2 contains extracellular array of leucine rich repeat modules together with immunoglobulin like domains, one transmembrane helix and a short intracellular cytoplasmic segment. Extracellular repeat arrays project outward into extracellular space, while cytoplasmic segment resides on intracellular side of plasma membrane. Newly synthesized ISLR2 polypeptide undergoes folding inside endoplasmic reticulum, where chaperone molecules assist proper assembly of leucine rich repeat and immunoglobulin like structural units. Only correctly folded polypeptide can be transported to cell surface. ISLR2 shows variable expression across different tissue cell types, and protein abundance adjusts according to cellular requirement for cell surface molecular interaction capacity. Distinct cell types exhibit different expression magnitude, which shapes potential for intermolecular contact at cell surface.
The composite extracellular domain assembly of ISLR2 mediates intermolecular recognition with diverse cell surface or soluble partner molecules. Leucine rich repeat units and immunoglobulin like segments work together to form composite binding interfaces for target molecule engagement. Its short intracellular cytoplasmic segment can recruit limited sets of cytoplasmic adaptor components to assemble molecular complexes beneath plasma membrane. Other leucine rich repeat containing cell surface proteins share partial domain architecture but cannot fully reproduce the composite binding property brought by ISLR2 domain combination. Variations in ISLR2 surface abundance change total quantity of available composite recognition molecules at cell surface. Sequence alteration within leucine rich repeat or immunoglobulin like segments may disturb partner molecule recognition, while changes to cytoplasmic segment can reduce efficiency of intracellular adaptor recruitment. Changed protein abundance can modulate cell surface interaction potential without completely abolishing molecular contact activity.
Fig. 1 Schematic domain architecture of transmembrane ISLR2 (Linx). The extracellular region consists of leucine‑rich‑repeat modules and immunoglobulin‑like domain, supporting cell‑surface molecular recognition.1
The biological functions of ISLR2 are focused on composite extracellular molecular recognition, multi domain partner engagement and intracellular adaptor complex recruitment:
Creative Biolabs offers purified ISLR2 membrane samples via standardized preparation workflows, including full length ISLR2 constructs and isolated extracellular structural variants. Isolated extracellular fragments may not support complete composite molecular recognition and intracellular adaptor recruitment related behaviours, while full length constructs may be suited for immunoglobulin superfamily cell surface interaction associated research. All samples receive routine quality screening, and functional relevant observation may only be carried out with full length samples under simulated membrane environments. All sample batches follow unified processing standards to maintain consistent structural features for comparative laboratory analysis across separate test groups.
Not finding the membrane protein product you need? Contact us to start your one-stop custom service!
Creative Biolabs provides adjustable ISLR2 expression cell models with varied expression levels, applicable to transmembrane immunoglobulin superfamily protein structural characteristic observation and cell surface interaction related research. Sample evaluation includes sustained target expression detection and preliminary intermolecular interaction associated observation, which can support comparative analysis of receptor associated behaviours under different expression statuses. These cell systems can be matched with diverse laboratory analysis schemes to observe changes of molecular recognition efficiency under different target expression abundances.
Not finding the stable cell line product you need? Contact us to start your one-stop custom service!
Antibody reagents targeting ISLR2 are generated via mature protein preparation workflows, compatible with multiple routine laboratory detection methods for cellular localization profiling and molecular complex identification, to support systematic analysis of ISLR2 distribution and cell surface associated molecular complexes across diverse laboratory research setups. The antibody series can cooperate with other common laboratory detection reagents to complete multi dimensional observation of target distribution inside tissue samples.
Not finding the recombinant antibody product you need? Contact us to start your one-stop custom service!
Beyond catalog products, Creative Biolabs offers specialized custom services for ISLR2 research:
ISLR2 may function as transmembrane immunoglobulin superfamily protein and participate in composite extracellular molecular recognition and intracellular adaptor complex recruitment.
ISLR2 expression status may influence cell surface molecular recognition potential, serving as a major regulatory mediator of cell surface interaction related biological processes.
No, all ISLR2 related products and services are strictly for research use only, not intended for clinical related operations. All material designs and functional tests are only optimized for basic laboratory research scenarios, without matching clinical application standards.
Offerings include full length ISLR2 membrane protein, target specific recombinant antibodies and adjustable expression cell research models, supporting cell surface recognition and cell interaction research.
Laboratory observation schemes may include multi domain mediated intermolecular contact tests to analyse molecule associated behaviours under simulated cellular environments.