Creative Biolabs is offering the most comprehensive services for antibody development projects. With strict regulation and effective execution, we are dedicated to providing the most valuable solutions to complete your projects.
HighlightsCreative Biolabs is offering the most comprehensive services for antibody development projects. With strict regulation and effective execution, we are dedicated to providing the most valuable solutions to complete your projects.
HighlightsCreative Biolabs has established a broad range of platforms for developing novel antibodies or equivalents. These cutting-edge technologies enable our scientists to meet your demands from different aspects and tailor the most appropriate solution that contributes to the success of your projects.
HighlightsWith deep understanding in antibody-related realms and extensive project experience, Creative Biolabs offers a variety of references to help you learn more about our capacities and achievements, including infographic, flyer, case study, peer-reviewed publications, and all kinds of knowledge that can assist your projects. You are also welcome to contact us directly for more specific solutions.
HighlightsGet a real taste of Creative Biolabs, one of the most professional custom service providers in the world. We are committed to providing highly customized comprehensive solutions with the best quality to advance your projects.
Highlights
Loading...All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.
Structural characteristics and physiological metabolic functions: Folate hydrolase 1 (FOLH1, also known as PSMA/GCPII) is encoded by the FOLH1 gene; it belongs to the M28‑family type‑II transmembrane glycoprotein peptidase, and is primarily anchored within lipid bilayers of plasma membranes across multiple tissues including intestine, prostate, kidney and nervous system. Distinct from secreted soluble metabolic enzymes, FOLH1 features a short intracellular cytoplasmic tail, a single transmembrane helix and a large extracellular zinc‑dependent catalytic domain, and lacks intracellular kinase‑catalytic structural motifs. As a membrane‑anchored M28 peptidase, FOLH1 exerts glutamate‑carboxypeptidase activity under physiological homeostasis, catalyzing hydrolysis of polyglutamylated dietary folate substrates to generate bio‑available monoglutamyl folate for cellular uptake. When tissues lack sufficient functional FOLH1 peptidase, incomplete folate substrate processing readily occurs and disrupts local folate metabolic balance; FOLH1 provides critical metabolic buffering to sustain steady folate turnover across diverse tissue microenvironments. Multiple tissue compartments generate distinct pools of folate‑derived substrates, requiring properly functioning membrane‑bound peptidase such as FOLH1 to maintain tissue‑level folate metabolic homeostasis. Membrane‑localized FOLH1 continuously engages extracellular peptide‑folate substrates, limiting accumulation of unprocessed substrate intermediates and preserving stable extracellular folate‑metabolism equilibrium.
Variational effects, regulatory mechanisms, and research value: Variants of the FOLH1 gene can alter substrate‑binding affinity and enzymatic hydrolysis efficiency, correlating with perturbed tissue folate metabolism profiles. No other M28‑family peptidase paralog fully recapitulates FOLH1’s dual capability for polyglutamylated‑folate hydrolysis and neuropeptide substrate processing. Shifts in FOLH1 expression levels closely correlate with tissue folate‑metabolizing status, making it a valuable research target for investigating type‑II transmembrane M28 peptidase function and extracellular folate‑dependent substrate maturation. FOLH1 is stably embedded within plasma‑membrane lipid bilayers and executes extracellular catalytic reactions without triggering persistent intracellular downstream signaling cascades. Its unique transmembrane‑anchored localization differentiates it from soluble cytosolic hydrolases, conferring dual capacity to stabilize tissue folate homeostasis and drive conversion of extracellular folate precursor substrates. Loss or diminished functional FOLH1 elevates accumulation of unhydrolyzed polyglutamylated folate substrates and impairs tissue folate‑metabolic buffering capacity, further highlighting its research significance for fundamental M28‑family transmembrane peptidase studies.
Fig. 1 X‑ray crystal structure of FOLH1 extracellular catalytic domain. Left panel shows homodimer assembly; right panel displays monomer unit with bound substrate analog and dual‑zinc catalytic center within M28‑peptidase domain.1
The biological functions of transmembrane FOLH1 peptidase protein are focused on sustained extracellular peptide-folate substrate catalysis and tissue folate-metabolism coordination:
Creative Biolabs offers purified FOLH1 membrane samples produced under unified preparation workflows, including full-length FOLH1 constructs and isolated extracellular catalytic domain variants. Truncated extracellular fragments cannot support complete peptide-folate substrate hydrolysis behaviours, while full-length constructs suit research focused on extracellular peptidase catalysis and plasma-membrane anchoring. All batches receive uniform quality screening. Functional relevant observation may only be carried out with full-length samples under simulated membrane microenvironment setups. Consistent structural features are preserved across batches to support comparative laboratory analysis across separate test groups. Full-length FOLH1 samples retain intact zinc-dependent extracellular catalytic-domain conformation after standardized purification, which supports reliable detection of weak and transient enzyme-substrate contacts for comparative functional analysis.
Not finding the Membrane potein product you need? Contact us to start your one-stop custom service!
Creative Biolabs provides adjustable FOLH1 expression cell research models with varied expression levels, applicable to structural observation of type-II transmembrane M28-family peptidases and research into extracellular peptide-folate substrate catalytic interaction. Sample evaluation includes sustained target expression detection and preliminary substrate-interaction observation, enabling side-by-side comparison of enzyme catalytic behaviours under differing expression abundances. These cell systems can pair with diverse laboratory analysis schemes to track changes in substrate-processing efficiency alongside shifting target protein levels.
Not finding the stable cell line product you need? Contact us to start your one-stop custom service!
Anti-FOLH1 recombinant antibodies are generated via standardized protein preparation workflows, compatible with routine laboratory detection techniques for plasma membrane localization mapping and identification of enzyme-substrate molecular complexes. The antibody series can work alongside common laboratory detection reagents to realize multi-dimensional observation of target distribution within metabolic-related 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 FOLH1 research:
FOLH1 might act as a type-II transmembrane M28-family peptidase and participate in extracellular hydrolytic processing of polyglutamylated-folate-related peptide substrates.
FOLH1 expression status could alter extracellular peptide-folate substrate-processing efficiency and tissue folate-metabolic balance, serving as a major regulatory mediator of tissue folate-related biological processes.
No, all FOLH1 related products and services are strictly for research use only, and cannot be applied in clinical workflows. All material designs and functional tests are optimized exclusively for basic laboratory research scenarios, without matching clinical application standards.
Offerings include full-length FOLH1 membrane protein, target-specific recombinant antibodies and tunable expression cell research models, supporting research on cell-surface folate-metabolic homeostasis and extracellular peptide-substrate hydrolysis.
Laboratory observation schemes may include enzyme-substrate interaction related tests to analyze hydrolytic-associated behaviors under simulated membrane environments.
