Recombinant Pig Glutamate carboxypeptidase 2 (FOLH1), partial, Biotinylated

SKU:BHP10511643
Suppliers
CUSABIO TECHNOLOGY LLC
CUSABIO TECHNOLOGY LLC
Details Products
Overview
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Recombinant FOLH1 (Pig) protein produced in E.coli spanning 44-751aa with His tag(s). Supplied as Liquid or Lyophilized powder; ≥85% (SDS-PAGE). Commonly used in Neuroscience research, including assay development, binding assays.
Target FOLH1
Species Sus scrofa (Pig)
Conjugate(s) N-terminal MBP-tagged and C-terminal 6xHis-Avi-tagged
Expression System E.coli
Expression Region 44-751aa
Options selector
Catalog no. Size
CSB-EP008782PI11-B-1MG 1 mg
CSB-EP008782PI11-B-100UG 100 ug
CSB-EP008782PI11-B-20UG 20 ug
Available Options

Select the variant that best fits your experiment. Availability and lead time may vary by option.

  • Options: Size (3) - 1 mg, 20 ug, 100 ug
  • Lead time: 3-7 business days. See “Availability Content” for the exact estimate by variant; other statuses may take longer.
  • Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
  • Shipping: cold-chain shipment (typically with ice packs).
  • Upon receipt: store at the recommended temperature as soon as possible.
  • Sales terms and conditions: Please review prior to ordering.
Field Specification
Mfr No CSB-EP008782PI11-B
Activity
  • Not Test
Alternative Names (Folate hydrolase 1)(Folylpoly-gamma-glutamate carboxypeptidase)(FGCP)(Glutamate carboxypeptidase II)(GCPII)(Membrane glutamate carboxypeptidase)(mGCP)(N-acetylated-alpha-linked acidic dipeptidase I)(NAALADase I)(Prostate-specific membrane antigen homolog)(Pteroylpoly-gamma-glutamate carboxypeptidase)
Conjugate
  • N-terminal MBP-tagged and C-terminal 6xHis-Avi-tagged
Endotoxin Level Not test
Expression System
  • E.coli
Form Liquid or Lyophilized powder
Molecular Weight 128.0 kDa
Product Type
  • Proteins & Peptides
  • Recombinant Proteins
Protein Length Partial
Purity Greater than 85% as determined by SDS-PAGE.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Species Sus scrofa (Pig)
Storage The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃. Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.
Target FOLH1
UniProt # O77564

Overview

Recombinant Pig Glutamate carboxypeptidase 2 (FOLH1), partial, Biotinylated is a recombinant protein preparation from Sus scrofa (Pig) designed for use in assay development, binding studies, and functional characterization. Key attributes such as expression system, expressed region, and affinity tag(s) help researchers match the reagent to specific experimental readouts.

Key elements and design rationale

  • Expression system: E.coli expression is commonly used for rapid, scalable production. For targets that require glycosylation or other post-translational modifications, consider how a prokaryotic system may affect folding or activity.
  • Expression region: The expressed fragment (44-751aa) focuses the reagent on a defined domain/segment, which can influence binding interfaces and epitope availability.
  • Tag(s)/format: His tags can support purification and detection in pull-down or binding assays; confirm that the tag position does not interfere with the interaction of interest.
  • Purity: ≥85% (SDS-PAGE) provides a quick checkpoint for reagent quality in downstream analytical workflows.
  • Form: Supplied as Liquid or Lyophilized powder; select the format that best fits your lab’s handling and aliquoting preferences.

Recombinant design choices (expression host, fragment boundaries, and tag configuration) help balance yield, solubility, and assay compatibility. Choose conditions and controls that match the recombinant format to your experimental question.

Biological background

FOLH1 has been reported to be involved in Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. ; Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC.. When interpreting results, consider species context, domain architecture, and whether the recombinant format represents full-length or a defined region.

Research relevance and current trends

  • Mapping synaptic or sensory protein interactions using recombinant domains and binding assays.
  • Integrating protein-level readouts with transcriptomics for multi-omic interpretation in neural models.

Common research applications

  • Binding and interaction assays: quantify partner binding and rank conditions using plate-based formats or biophysical methods (SPR/BLI).
  • Enzymology: assess catalytic activity and compare substrate preferences or inhibitor effects using appropriate controls.
  • Assay development: use as a standard, spike-in control, or positive control where consistent specifications are required.

Interpretation typically relies on relative comparisons (treated vs control, mutant vs wild-type, or dose/time series) using consistent sample handling and appropriate normalization.

Notes for experimental interpretation

  • Post-translational modifications: expression system can affect glycosylation and processing; interpret differences cautiously when comparing to native protein.
  • Isoforms and domains: expressed regions may not capture all isoform-specific features; match fragment boundaries to your assay’s binding site.
  • Controls: include blank matrix controls, tag-only controls (where relevant), and orthogonal readouts (e.g., WB/qPCR/ELISA) to support interpretation.

Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.

Why is the actual band size different from the predicted?
a. Post-translational modification. Phosphorylation, glycosylation, etc which increases the size of the protein. b. Post-translational cleavage. Many proteins are synthesized as pro-proteins, and then cleaved to give the active form. c. Splice variants. Alternative splicing may create different sized proteins from the same gene. d. Relative charge. The composition of amino acids have different relative charge which will affect the electrophoretic mobility. e. Multimers such as dimerisation of a protein. This is usually prevented in reducing conditions, although strong interactions can result in the appearance of higher bands. f. Protein structure such as disulfide bond, protein secondary structure or protein 3D structure formation. g. Hydrophobic proteins, such as transmembrane proteins, may have difficulties in migrating into the gel, and thus resulting in different multi-banded patterns.
How should I reconstitute and store the products?
Centrifugate the reagent tube before opening the cap. As for short-term storage or usage, please use sterile deionized water to completely reconstitute proteins to 0.1-1.0 mg/mL. Aliquot after 10-15 minutes if needed and store at 4℃. As for long-term storage, the cytokines or recombinant proteins are recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
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