Recombinant Human Immunoglobulin heavy constant gamma 1 (IGHG1) (D239E,L241M), partial (Active)

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Code CSB-AP005531HU
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Size $58
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 95% as determined by SDS-PAGE.
Endotoxin
Less than 1.0 EU/μg as determined by LAL method.
Activity
The ED50 as determined by its ability to bind Human FCGR3A in functional ELISA is less than 10 ug/ml.
Target Names
IGHG1
Uniprot No.
Research Area
Cancer
Alternative Names
IGHG1; Immunoglobulin heavy constant gamma 1; Ig gamma-1 chain C region; Ig gamma-1 chain C region EU; Ig gamma-1 chain C region KOL; Ig gamma-1 chain C region NIE
Species
Homo sapiens (Human)
Source
Mammalian cell
Expression Region
104-330aa(D239E,L241M)
Complete Sequence
DKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
Mol. Weight
25.9 kDa
Protein Length
Partial
Tag Info
Tag-Free
Form
Liquid or Lyophilized powder
Buffer
Lyophilized from a 0.2 μm filtered 1xPBS, pH 7.4.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
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°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Datasheet & COA
Please contact us to get it.
Description

The protein IGHG1, also called immunoglobulin gamma-1 heavy chain constant region, has gained attention in cancer research. It's been found to be more active in several types of cancer, such as gastric, brain, pancreatic, colorectal, breast, prostate, ovarian, and triple-negative breast cancers [1][2][3][4][5][6][7][8]. Its increased activity seems to encourage cancer growth, spread, and blood vessel formation [1][5]. In pancreatic cancer, it's even been linked to making tumors resistant to treatment [3], and in gastric cancer, it nudges cells into a more aggressive state [9]. Some suggest it might help cancer cells dodge the immune system too [10][11].

We've spotted IGHG1 in samples from various tumors like breast, lung, and oral cancers, plus in lab-grown cancer cells [12]. Shutting down IGHG1 in prostate cancer cells seems to slow their growth and make them more likely to self-destruct [13][14]. It's also been tied to how cancers progress [3].

Beyond cancer, IGHG1 seems to pitch in with the immune system by helping present antigens, forming part of the cell's framework, and grabbing onto antigens [2]. In triple-negative breast cancer, it might even hint at a better outcome [8]. And it's not just cancers - it's found in cells making antibodies and is a key player in certain nerve cells [15].

References:
[1] X. Li, W. Chen, C. Yang, Y. Huang, J. Jia, R. Xuet al., "Ighg1 upregulation promoted gastric cancer malignancy via akt/gsk-3β/β-catenin pathway", Cancer Cell International, vol. 21, no. 1, 2021. https://doi.org/10.1186/s12935-021-02098-1
[2] G. Wang, H. Li, J. Pan, T. Yan, H. Zhou, X. Hanet al., "Upregulated expression of cancer-derived immunoglobulin g is associated with progression in glioma", Frontiers in Oncology, vol. 11, 2021. https://doi.org/10.3389/fonc.2021.758856
[3] Y. Tian, W. Han, L. Fu, K. Lv, & X. Zhou, "Silencing of ighg1 reverses the resistance of pancreatic cancer to multidrug chemotherapy by modulating autophagy", Environmental Toxicology, vol. 38, no. 8, p. 1835-1845, 2023. https://doi.org/10.1002/tox.23810
[4] Y. Gao, G. Li, X. Du, W. Zhou, X. Zou, Y. Liuet al., "Down-regulation of ighg1 enhances protoporphyrin ix accumulation and inhibits hemin biosynthesis in colorectal cancer by suppressing the mek-fech axis", Open Life Sciences, vol. 16, no. 1, p. 930-936, 2021. https://doi.org/10.1515/biol-2021-0098
[5] Y. Zhang, X. Fang, & Y. Sun, "Ighg1 promotes malignant progression in breast cancer cells through the regulation of akt and vegf signaling", Biomolecules and Biomedicine, 2023. https://doi.org/10.17305/bb.2022.8508
[6] J. Chu, Y. Li, Z. Deng, Z. Zhang, Q. Xie, H. Zhanget al., "Ighg1 regulates prostate cancer growth via the mek/erk/c-myc pathway", Biomed Research International, vol. 2019, p. 1-10, 2019. https://doi.org/10.1155/2019/7201562
[7] J. Qian, F. Ji, Y. Xue, H. Cheng, R. Ma, X. Changet al., "Ighg1 promotes motility likely through epithelial-mesenchymal transition in ovarian cancer", Chinese Journal of Cancer Research, vol. 30, no. 2, p. 282-290, 2018. https://doi.org/10.21147/j.issn.1000-9604.2018.02.11
[8] H. Hsu, C. Chu, Y. Chang, J. Yu, C. Chen, C. Jianet al., "Six novel immunoglobulin genes as biomarkers for better prognosis in triple-negative breast cancer by gene co-expression network analysis", Scientific Reports, vol. 9, no. 1, 2019. https://doi.org/10.1038/s41598-019-40826-w
[9] Y. Li, P. Wang, D. Ye, X. Bai, X. Zeng, Q. Zhaoet al., "Ighg1 induces emt in gastric cancer cells by regulating tgf-β/smad3 signaling pathway", Journal of Cancer, vol. 12, no. 12, p. 3458-3467, 2021. https://doi.org/10.7150/jca.56056
[10] P. Syed, S. Gupta, S. Choudhary, N. Pandala, A. Atak, A. Richhariaet al., "Autoantibody profiling of glioma serum samples to identify biomarkers using human proteome arrays", Scientific Reports, vol. 5, no. 1, 2015. https://doi.org/10.1038/srep13895
[11] O. Kholod, W. Basket, J. Mitchem, J. Kaifi, R. Hammer, C. Papageorgiouet al., "Immune-related gene signatures to predict the effectiveness of chemoimmunotherapy in triple-negative breast cancer using exploratory subgroup discovery", Cancers, vol. 14, no. 23, p. 5806, 2022. https://doi.org/10.3390/cancers14235806
[12] X. Zhang, W. Shen, X. Dong, J. Fan, L. Liu, X. Gaoet al., "Identification of novel autoantibodies for detection of malignant mesothelioma", Plos One, vol. 8, no. 8, p. e72458, 2013. https://doi.org/10.1371/journal.pone.0072458
[13] A. Kuot, M. Ronci, R. Mills, S. Klebe, G. Snibson, S. Wiffenet al., "Reduced expression of apolipoprotein e and immunoglobulin heavy constant gamma 1 proteins in fuchs endothelial corneal dystrophy", Clinical and Experimental Ophthalmology, vol. 47, no. 8, p. 1028-1042, 2019. https://doi.org/10.1111/ceo.13569
[14] B. Pan, S. Zheng, C. Liu, & Y. Xu, "Suppression of ighg1 gene expression by sirna leads to growth inhibition and apoptosis induction in human prostate cancer cell", Molecular Biology Reports, vol. 40, no. 1, p. 27-33, 2012. https://doi.org/10.1007/s11033-012-1944-x
[15] M. Gunasekaran, P. Chatterjee, A. Shih, G. Imperato, M. Addorisio, G. Kumaret al., "Immunization elicits antigen-specific antibody sequestration in dorsal root ganglia sensory neurons", Frontiers in Immunology, vol. 9, 2018. https://doi.org/10.3389/fimmu.2018.00638

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Target Background

Function
Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Involvement in disease
Multiple myeloma (MM)
Subcellular Location
Secreted. Cell membrane.
Database Links

HGNC: 5525

OMIM: 147100

UniGene: Hs.510635

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