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Mouse Anti-AGR2 Recombinant Antibody (V2-634170) (CBMAB-AP204LY)


See all AGR2 antibodies
Published Data
Mouse Anti-AGR2 Recombinant Antibody (CAP086) (CBMAB-AP204LY) in ELISA
Verification of AGR2 in plasma from pancreatic cancer patients and healthy controls of similar age and sex. Plasma concentrations of the proteins were measured by ELISA. Mean values are indicated by a horizontal line and p values were calculated using the Mann-Whitney U test. Number of subjects = 20 pancreatic cancer and 20 controls. ...View More
Makawita, S., Smith, C., Batruch, I., Zheng, Y., Rückert, F., Grützmann, R., ... & Diamandis, E. P. (2011). Integrated proteomic profiling of cell line conditioned media and pancreatic juice for the identification of pancreatic cancer biomarkers. Molecular & cellular proteomics, 10(10).

Summary

Host Animal
Mouse
Specificity
Human
Clone
V2-634170
Antibody Isotype
IgG
Application
ICC, IHC, IP, WB

Basic Information

Immunogen
Recombinant protein.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:500-1:5,000
IHC1:50-1:200
IF(ICC)1:50-1:200

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH7.4, 50% glycerol
Preservative
0.02% sodium azide
Concentration
1 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Anterior Gradient 2, Protein Disulphide Isomerase Family Member
Introduction
This gene encodes a member of the disulfide isomerase (PDI) family of endoplasmic reticulum (ER) proteins that catalyze protein folding and thiol-disulfide interchange reactions. The encoded protein has an N-terminal ER-signal sequence, a catalytically active thioredoxin domain, and a C-terminal ER-retention sequence. This protein plays a role in cell migration, cellular transformation and metastasis and is as a p53 inhibitor. As an ER-localized molecular chaperone, it plays a role in the folding, trafficking, and assembly of cysteine-rich transmembrane receptors and the cysteine-rich intestinal gylcoprotein mucin. This gene has been implicated in inflammatory bowel disease and cancer progression. [provided by RefSeq, Mar 2017]
Entrez Gene ID
Human10551
Rat298961
UniProt ID
HumanO95994
RatD3ZIA7
Alternative Names
Anterior Gradient 2, Protein Disulphide Isomerase Family Member; Protein Disulfide Isomerase Family A, Member 17; Secreted Cement Gland Protein XAG-2 Homolog; HAG-2; AG-2; HPC8; AG2; Anterior Gradient 2 Homolog (Xenopus Laevis); Anterior Gradient Protein 2 Homolog;
Function
Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells (By similarity). Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth. Promotes cell adhesion.
Biological Process
Digestive tract morphogenesis
Mucus secretion
Negative regulation of cell death
Positive regulation of cell-substrate adhesion
Positive regulation of developmental growth
Positive regulation of epidermal growth factor receptor signaling pathway
Positive regulation of gene expression
Positive regulation of IRE1-mediated unfolded protein response
Positive regulation of PERK-mediated unfolded protein response
Positive regulation of protein localization to plasma membrane
Cellular Location
Secreted; Endoplasmic reticulum

Wang, Y., Jia, M., Liang, C., Sheng, N., Wang, X., Wang, F., ... & Yuan, H. (2021). Anterior gradient 2 increases long-chain fatty acid uptake via stabilizing FABP1 and facilitates lipid accumulation. International journal of biological sciences, 17(3), 834.

Delom, F., Mohtar, M. A., Hupp, T., & Fessart, D. (2020). The anterior gradient-2 interactome. American Journal of Physiology-Cell Physiology, 318(1), C40-C47.

Moidu, N. A., Rahman, N. S. A., Syafruddin, S. E., Low, T. Y., & Mohtar, M. A. (2020). Secretion of pro-oncogenic AGR2 protein in cancer. Heliyon, 6(9), e05000.

Wang, D., Xu, Q., Yuan, Q., Jia, M., Niu, H., Liu, X., ... & Yuan, H. (2019). Proteasome inhibition boosts autophagic degradation of ubiquitinated-AGR2 and enhances the antitumor efficiency of bevacizumab. Oncogene, 38(18), 3458-3474.

Maurel, M., Obacz, J., Avril, T., Ding, Y. P., Papadodima, O., Treton, X., ... & Ogier‐Denis, E. (2019). Control of anterior GR adient 2 (AGR 2) dimerization links endoplasmic reticulum proteostasis to inflammation. EMBO molecular medicine, 11(6), e10120.

Tiemann, K., Garri, C., Lee, S. B., Malihi, P. D., Park, M., Alvarez, R. M., ... & Kani, K. (2019). Loss of ER retention motif of AGR2 can impact mTORC signaling and promote cancer metastasis. Oncogene, 38(16), 3003-3018.

Zhang, Y., Xia, F., Zhang, F., Cui, Y., Wang, Q., Liu, H., & Wu, Y. (2019). miR-135b-5p enhances doxorubicin-sensitivity of breast cancer cells through targeting anterior gradient 2. Journal of Experimental & Clinical Cancer Research, 38(1), 1-13.

Li, J., Hu, J., Luo, Z., Zhou, C., Huang, L., Zhang, H., ... & Wang, Z. (2019). AGR2 is controlled by DNMT3a-centered signaling module and mediates tumor resistance to 5-Aza in colorectal cancer. Experimental cell research, 385(1), 111644.

Delom, F., Nazaraliyev, A., & Fessart, D. (2018). The role of protein disulphide isomerase AGR2 in the tumour niche. Biology of the Cell, 110(12), 271-282.

Zhu, Q., Mangukiya, H. B., Mashausi, D. S., Guo, H., Negi, H., Merugu, S. B., ... & Li, D. (2017). Anterior gradient 2 is induced in cutaneous wound and promotes wound healing through its adhesion domain. The FEBS journal, 284(17), 2856-2869.

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For research use only. Not intended for any clinical use.

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